Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  63 RAVLFVGLCDSGKTLLFVRLLTGQYRDTQTSITDSSAIYKVNNNRGNSLTLIDLPGHESLRLQFLDRFKSSARAVVFVVD 142
Cdd:cd04105   1 PTVLLLGPSDSGKTALFTKLTTGKVRSTVTSIEPNVASFYSNSSKGKKLTLVDVPGHEKLRDKLLEYLKASLKAIVFVVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217 143 SATFQREVKDVAEFLYQVLIDSMALKNTPAFLVACNKQDIAMAKSAKLIQQQLEKELNTLRVTRSAAPSTLDSSSTAPAQ 222
Cdd:cd04105  81 SATFQKNIRDVAEFLYDILTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELLEKEINTLRESRSKSLESLDGDDGSKDT 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 61676217 223 LG-KKGKEFEFSQLPLKVEFLECSAKGGRGdagsaDVQDLEKWLAKI 268
Cdd:cd04105 161 LGdKGGKDFEFDQLEGEVDFVEGSVKKSKG-----GIDDIEEWIDEL 202

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  63 RAVLFVGLCDSGKTLLFVRLLTGQYRDTQTSITDSSAIYKVNNNRGNSLTLIDLPGHESLRLQFLDRFKSSARAVVFVVD 142
Cdd:cd04105   1 PTVLLLGPSDSGKTALFTKLTTGKVRSTVTSIEPNVASFYSNSSKGKKLTLVDVPGHEKLRDKLLEYLKASLKAIVFVVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217 143 SATFQREVKDVAEFLYQVLIDSMALKNTPAFLVACNKQDIAMAKSAKLIQQQLEKELNTLRVTRSAAPSTLDSSSTAPAQ 222
Cdd:cd04105  81 SATFQKNIRDVAEFLYDILTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELLEKEINTLRESRSKSLESLDGDDGSKDT 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 61676217 223 LG-KKGKEFEFSQLPLKVEFLECSAKGGRGdagsaDVQDLEKWLAKI 268
Cdd:cd04105 161 LGdKGGKDFEFDQLEGEVDFVEGSVKKSKG-----GIDDIEEWIDEL 202

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217     65 VLFVGLCDSGKTLLFVRLLT---GQYRDTQTSITDSSAIYKVNnnrgnsLTLIDLPGHESLRLQFLDRFkSSARAVVFVV 141
Cdd:smart00178  20 ILFLGLDNAGKTTLLHMLKNdrlAQHQPTQHPTSEELAIGNIK------FTTFDLGGHQQARRLWKDYF-PEVNGIVYLV 92

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61676217    142 DSATFQREVKDVAEFlyQVLIDSMALKNTPaFLVACNKQDIAMAKSakliQQQLEKELNTLRVTRS 207
Cdd:smart00178  93 DAYDKERFAESKREL--DALLSDEELATVP-FLILGNKIDAPYAAS----EDELRYALGLTNTTTG 151

ADP-ribosylation factor; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217   52 WKFIWSRKSSQraVLFVGLCDSGKTLLFVRLLTGQYRDTQTSITDSSAIYKVNNnrgNSLTLIDLPGHESLRLQFLDRFK 131
Cdd:PLN00223   9 FSRLFAKKEMR--ILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKN---ISFTVWDVGGQDKIRPLWRHYFQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  132 SSaRAVVFVVDSATFQReVKDVAEFLYQVLIDSmALKNTpAFLVACNKQDIAMAKSAKLIQQQLekELNTLRVTRSAAPS 211
Cdd:PLN00223  84 NT-QGLIFVVDSNDRDR-VVEARDELHRMLNED-ELRDA-VLLVFANKQDLPNAMNAAEITDKL--GLHSLRQRHWYIQS 157

                 ....*
gi 61676217  212 TLDSS 216
Cdd:PLN00223 158 TCATS 162

Signal recognition particle receptor, beta subunit (SR-beta), together with SR-alpha, forms the heterodimeric signal recognition particle (SRP); Signal recognition particle receptor, beta subunit (SR-beta). SR-beta and SR-alpha form the heterodimeric signal recognition particle (SRP or SR) receptor that binds SRP to regulate protein translocation across the ER membrane. Nascent polypeptide chains are synthesized with an N-terminal hydrophobic signal sequence that binds SRP54, a component of the SRP. SRP directs targeting of the ribosome-nascent chain complex (RNC) to the ER membrane via interaction with the SR, which is localized to the ER membrane. The RNC is then transferred to the protein-conducting channel, or translocon, which facilitates polypeptide translation across the ER membrane or integration into the ER membrane. SR-beta is found only in eukaryotes; it is believed to control the release of the signal sequence from SRP54 upon binding of the ribosome to the translocon. High expression of SR-beta has been observed in human colon cancer, suggesting it may play a role in the development of this type of cancer.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  63 RAVLFVGLCDSGKTLLFVRLLTGQYRDTQTSITDSSAIYKVNNNRGNSLTLIDLPGHESLRLQFLDRFKSSARAVVFVVD 142
Cdd:cd04105   1 PTVLLLGPSDSGKTALFTKLTTGKVRSTVTSIEPNVASFYSNSSKGKKLTLVDVPGHEKLRDKLLEYLKASLKAIVFVVD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217 143 SATFQREVKDVAEFLYQVLIDSMALKNTPAFLVACNKQDIAMAKSAKLIQQQLEKELNTLRVTRSAAPSTLDSSSTAPAQ 222
Cdd:cd04105  81 SATFQKNIRDVAEFLYDILTDLEKIKNKIPILIACNKQDLFTAKPAKKIKELLEKEINTLRESRSKSLESLDGDDGSKDT 160

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 61676217 223 LG-KKGKEFEFSQLPLKVEFLECSAKGGRGdagsaDVQDLEKWLAKI 268
Cdd:cd04105 161 LGdKGGKDFEFDQLEGEVDFVEGSVKKSKG-----GIDDIEEWIDEL 202

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  65 VLFVGLCDSGKTLLFVRLLTGQYRDTQTSI-TDSSAI-YKvnnNRgnSLTLIDLPGHESLRlQFLDRFKSSARAVVFVVD 142
Cdd:cd00878   2 ILMLGLDGAGKTTILYKLKLGEVVTTIPTIgFNVETVeYK---NV--KFTVWDVGGQDKIR-PLWKHYYENTDGLIFVVD 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 61676217 143 SATFQR--EVKdvaEFLYQVLIDSMaLKNTPaFLVACNKQDIAMAKSAKLIQQQLE 196
Cdd:cd00878  76 SSDRERieEAK---NELHKLLNEEE-LKGAP-LLILANKQDLPGALTESELIELLG 126

Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  52 WKFIWSRKSSqraVLFVGLCDSGKTLLFVRLLTG---QYRDTQTSITDSSAIYKVNnnrgnsLTLIDLPGHESLRLQFLD 128
Cdd:cd00879  12 SLGLYKKEAK---IVFLGLDNAGKTTLLHMLKDDrlaQHVPTLHPTSEELTIGNVK------FTTFDLGGHEQARRVWKD 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61676217 129 RFKSSaRAVVFVVDSATFQR--EVKDVAEFLYQVLidsmALKNTPaFLVACNKQDIAMAKSakliQQQLEKELN 200
Cdd:cd00879  83 YFPEV-DGIVFLVDAADPERfqESKEELDSLLNDE----ELANVP-ILILGNKIDKPGAVS----EEELREALG 146

Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  65 VLFVGLCDSGKTLLFVRLLTGQyrDTQTSITDSSAIYKVNNNRGNSLTLIDLPGHESLRlQFLDRFKSSARAVVFVVDSA 144
Cdd:cd04156   2 VLLLGLDSAGKSTLLYKLKHAE--LVTTIPTVGFNVEMLQLEKHLSLTVWDVGGQEKMR-TVWKCYLENTDGLVYVVDSS 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 61676217 145 TFQREVKDVAEFlyQVLIDSMALKNTPAFLVAcNKQDIAMAKSAKLIQQQL 195
Cdd:cd04156  79 DEARLDESQKEL--KHILKNEHIKGVPVVLLA-NKQDLPGALTAEEITRRF 126

Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  65 VLFVGLCDSGKTLLFVRLLTGQYRDT--------QTSITDSSAIYKVNNNRgnsLTLIDLPGHESLRlQFLDRFKSSARA 136
Cdd:cd04160   2 VLILGLDNAGKTTFLEQTKTKFSKNYkglnpskiTPTVGLNIGTIEVGKAR---LMFWDLGGQEELR-SLWDKYYAESHG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217 137 VVFVVDSATFQR--EVKDVaeflYQVLIDSMALKNTPaFLVACNKQDIAMAKSAKLIQQQLE--KELNTLRVTRSAAPST 212
Cdd:cd04160  78 VIYVIDSTDRERfnESKSA----FEKVINNEALEGVP-LLVLANKQDLPDALSVAEIKEVFDdcIALIGRRDCLVQPVSA 152

                ..
gi 61676217 213 LD 214
Cdd:cd04160 153 LE 154

Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  58 RKSSQRA----VLFVGLCDSGKTLLFVRLLTgqyRDTQT-SITDSSAIyKVNNNRGNSLTLIDLPGHESLRLQFLDRFKS 132
Cdd:cd04154   6 RKTKQKEremrILMLGLDNAGKTTILKKFNG---EDISTiSPTLGFNI-KTLEYNGYKLNIWDVGGQKSLRSYWRNYFES 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 61676217 133 SaRAVVFVVDSATFQReVKDVAEFLYQVLIDSMALKNTpaFLVACNKQDIAMAKSAKLIQQQLE 196
Cdd:cd04154  82 T-DALIWVVDSSDRAR-LEDCKRELQKLLVEERLAGAT--LLIFANKQDLPGALSPEEIREVLE 141

Sar1p-like members of the Ras-family of small GTPases; Yeast SAR1 is an essential gene required for transport of secretory proteins from the endoplasmic reticulum to the Golgi apparatus.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217     65 VLFVGLCDSGKTLLFVRLLT---GQYRDTQTSITDSSAIYKVNnnrgnsLTLIDLPGHESLRLQFLDRFkSSARAVVFVV 141
Cdd:smart00178  20 ILFLGLDNAGKTTLLHMLKNdrlAQHQPTQHPTSEELAIGNIK------FTTFDLGGHQQARRLWKDYF-PEVNGIVYLV 92

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 61676217    142 DSATFQREVKDVAEFlyQVLIDSMALKNTPaFLVACNKQDIAMAKSakliQQQLEKELNTLRVTRS 207
Cdd:smart00178  93 DAYDKERFAESKREL--DALLSDEELATVP-FLILGNKIDAPYAAS----EDELRYALGLTNTTTG 151

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. ARFs are N-terminally myristoylated. Contains ATP/GTP-binding motif (P-loop).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217     65 VLFVGLCDSGKTLLFVRLLTGQYRDTQTSITDSSAIYKVNNNrgnSLTLIDLPGHESLRLQFLDRFKSSaRAVVFVVDSA 144
Cdd:smart00177  16 ILMVGLDAAGKTTILYKLKLGESVTTIPTIGFNVETVTYKNI---SFTVWDVGGQDKIRPLWRHYYTNT-QGLIFVVDSN 91

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 61676217    145 TFQReVKDVAEFLYQVLIDSmALKNTpAFLVACNKQDIAMAKSAKLIQQQL 195
Cdd:smart00177  92 DRDR-IDEAREELHRMLNED-ELRDA-VILVFANKQDLPDAMKAAEITEKL 139

ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor. Arf4 has also been shown to recognize the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialized post-Golgi rhodopsin transport carriers (RTCs). There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs).

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  65 VLFVGLCDSGKTLLFVRLLTGQYRDTQTSITDSSAIYKVNNNrgnSLTLIDLPGHESLRLQFLDRFKSSaRAVVFVVDSA 144
Cdd:cd04150   3 ILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNI---SFTVWDVGGQDKIRPLWRHYFQNT-QGLIFVVDSN 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 61676217 145 TFQReVKDVAEFLYQVLIDSmALKNTpAFLVACNKQDIAMAKSAKLIQQQLekELNTLR 203
Cdd:cd04150  79 DRER-IGEAREELQRMLNED-ELRDA-VLLVFANKQDLPNAMSAAEVTDKL--GLHSLR 132

Arf-like 9 (Arl9) and 10 (Arl10) GTPases; Arl10-like subfamily. Arl9/Arl10 was identified from a human cancer-derived EST dataset. No functional information about the subfamily is available at the current time, but crystal structures of human Arl10b and Arl10c have been solved.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  68 VGLCDSGKTLLFVRLLTGQY-RDTQTSItdSSAIYKVNnnRGN-SLTLIDLPGHESLRLQFlDRFKSSARAVVFVVDSAT 145
Cdd:cd04159   5 VGLQNSGKTTLVNVIASGQFsEDTIPTV--GFNMRKVT--KGNvTIKVWDLGGQPRFRSMW-ERYCRGVNAIVYVVDAAD 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 61676217 146 FQRevKDVAEFLYQVLIDSMALKNTPaFLVACNKQDIAMAKSAKLIQQQL 195
Cdd:cd04159  80 REK--LEVAKNELHDLLEKPSLEGIP-LLVLGNKNDLPGALSVDELIEQM 126

ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi complex, where it is believed to recruit effector proteins to the trans-Golgi network. Like most members of the Arf family, Arl1 is myristoylated at its N-terminal helix and mutation of the myristoylation site disrupts Golgi targeting. In humans, the Golgi-localized proteins golgin-97 and golgin-245 have been identified as Arl1 effectors. Golgins are large coiled-coil proteins found in the Golgi, and these golgins contain a C-terminal GRIP domain, which is the site of Arl1 binding. Additional Arl1 effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps53) vesicle-tethering complex and Arfaptin 2. Arl1 is not required for exocytosis, but appears necessary for trafficking from the endosomes to the Golgi. In Drosophila zygotes, mutation of Arl1 is lethal, and in the host-bloodstream form of Trypanosoma brucei, Arl1 is essential for viability.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  65 VLFVGLCDSGKTLLFVRLLTGQYRDTQTSI--TDSSAIYKvnnnrgN-SLTLIDLPGHESLRLqFLDRFKSSARAVVFVV 141
Cdd:cd04151   2 ILILGLDGAGKTTILYRLQVGEVVTTIPTIgfNVETVTYK------NlKFQVWDLGGQTSIRP-YWRCYYSNTDAIIYVV 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 61676217 142 DSATFQREVKDVAEFLYqvLIDSMALKNTPaFLVACNKQDIAMAKSAKLIQQQLE 196
Cdd:cd04151  75 DSTDRDRLGISKSELHA--MLEEEELKDAV-LLVFANKQDMPGALSEAEVAEKLG 126

Arf-like 4 (Arl4) and 7 (Arl7) GTPases; Arl4 (Arf-like 4) is highly expressed in testicular germ cells, and is found in the nucleus and nucleolus. In mice, Arl4 is developmentally expressed during embryogenesis, and a role in somite formation and central nervous system differentiation has been proposed. Arl7 has been identified as the only Arf/Arl protein to be induced by agonists of liver X-receptor and retinoid X-receptor and by cholesterol loading in human macrophages. Arl7 is proposed to play a role in transport between a perinuclear compartment and the plasma membrane, apparently linked to the ABCA1-mediated cholesterol secretion pathway. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  65 VLFVGLCDSGKTLLFVRLLTGQYRDTQTSITDSSAIYKVNNNRGNSLTLI--DLPGHESLRlqflDRFKSSAR---AVVF 139
Cdd:cd04152   6 IVMLGLDSAGKTTVLYRLKFNEFVNTVPTKGFNTEKIKVSLGNAKGVTFHfwDVGGQEKLR----PLWKSYTRctdGIVF 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 61676217 140 VVDSATFQREVKDVAEfLYQVLIDSMALkNTPAFLVAcNKQDIAMAKSAKLIQQQL 195
Cdd:cd04152  82 VVDSVDVERMEEAKTE-LHKITKFSENQ-GVPVLVLA-NKQDLPNALPVSEVEKLL 134

Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a subfamily of the Arf family of small GTPases. Arl2l1 was identified in human cells during a search for the gene(s) responsible for Bardet-Biedl syndrome (BBS). Like Arl6, the identified BBS gene, Arl2l1 is proposed to have cilia-specific functions. Arl13 is found on the X chromosome, but its expression has not been confirmed; it may be a pseudogene.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  65 VLFVGLCDSGKTLL---FVRLLTGQYRDTQTSITDSSAIYKVNnnrgnsLTLIDLPGHESLRLQFLDRFkSSARAVVFVV 141
Cdd:cd04161   2 LLTVGLDNAGKTTLvsaLQGEIPKKVAPTVGFTPTKLRLDKYE------VCIFDLGGGANFRGIWVNYY-AEAHGLVFVV 74

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 61676217 142 DSATFQReVKDVAEFLYQVLIDSMaLKNTPaFLVACNKQDIAMAKS-AKLIQQQLEKELntlrVTRSAAPSTLDSSST 218
Cdd:cd04161  75 DSSDDDR-VQEVKEILRELLQHPR-VSGKP-ILVLANKQDKKNALLgADVIEYLSLEKL----VNENKSLCHIEPCSA 145

ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 61676217  65 VLFVGLCDSGKTLLFVRLLTGQYRDTQTSITDSSAIYKVNNNRGNsltLIDLPGHESLRLQFLDRFkSSARAVVFVVDSA 144
Cdd:cd04149  12 ILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFN---VWDVGGQDKIRPLWRHYY-TGTQGLIFVVDSA 87

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 61676217 145 TFQReVKDVAEFLYQVLIDSmALKNTpAFLVACNKQDIAMAKSAKLIQQQLEKEL 199
Cdd:cd04149  88 DRDR-IDEARQELHRIINDR-EMRDA-LLLVFANKQDLPDAMKPHEIQEKLGLTR 139