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Conserved domains on  [gi|298676510|ref|NP_001177340|]
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rab effector Noc2 isoform 1 [Homo sapiens]

Protein Classification

FYVE zinc finger domain-containing protein( domain architecture ID 10491878)

FYVE (Fab1, YOTB, Vac1, and EEA1) zinc finger domain-containing protein binds phosphoinositide 3-kinase product PtdIns 3-phosphate (PtdIns(3)P)

Gene Ontology:  GO:0046872|GO:0008270
PubMed:  10564636|9697764

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FYVE_2 pfam02318
FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector ...
 47-159 5.14e-48

FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector proteins including rabphilin-3A and regulating synaptic membrane exocytosis protein 2.


:

Pssm-ID: 426716  Cd Length: 118  Bit Score: 156.76  E-value: 5.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676510   47 LSPAEVEAILQVIQRAERLDVLEQQRIGRLVERL--ETMRRNVMGN----GLSQCLLCGEVLGFLGSSSVFCKDCRKKVC 120
Cdd:pfam02318   3 LTDEEAEHVWEVVQRDFDLRKKEEERLGELKGKLdkESSKRELLGNqahlGETHCIRCLQPFGFLVNSKRQCLDCRKNVC 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 298676510  121 TKCGIEaspGQKRPLWLCKICSEQREVWKRSGAWFYKGL 159
Cdd:pfam02318  83 KKCGVY---NKPEQGWLCDPCSEARELKKGSLEWFYKNV 118
 
Name Accession Description Interval E-value
FYVE_2 pfam02318
FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector ...
 47-159 5.14e-48

FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector proteins including rabphilin-3A and regulating synaptic membrane exocytosis protein 2.


Pssm-ID: 426716  Cd Length: 118  Bit Score: 156.76  E-value: 5.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676510   47 LSPAEVEAILQVIQRAERLDVLEQQRIGRLVERL--ETMRRNVMGN----GLSQCLLCGEVLGFLGSSSVFCKDCRKKVC 120
Cdd:pfam02318   3 LTDEEAEHVWEVVQRDFDLRKKEEERLGELKGKLdkESSKRELLGNqahlGETHCIRCLQPFGFLVNSKRQCLDCRKNVC 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 298676510  121 TKCGIEaspGQKRPLWLCKICSEQREVWKRSGAWFYKGL 159
Cdd:pfam02318  83 KKCGVY---NKPEQGWLCDPCSEARELKKGSLEWFYKNV 118
FYVE_RPH3L cd15763
FYVE-related domain found in Rab effector Noc2 and similar proteins; Rab effector Noc2, also ...
 86-149 8.39e-40

FYVE-related domain found in Rab effector Noc2 and similar proteins; Rab effector Noc2, also termed No C2 domains protein, or rabphilin-3A-like protein (RPH3AL), is a Rab3 effector that mediates the regulation of secretory vesicle exocytosis in neurons and certain endocrine cells. It also functions as a Rab27 effector and is involved in isoproterenol (IPR)-stimulated amylase release from acinar cells. Noc2 contains an N-terminal Rab3A effector domain which harbors a conserved zinc finger, but lacks tandem C2 domains. The FYVE domain of Noc2 resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277302  Cd Length: 64  Bit Score: 133.94  E-value: 8.39e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298676510  86 NVMGNGLSQCLLCGEVLGFLGSSSVFCKDCRKKVCTKCGIEASPGQKRPLWLCKICSEQREVWK 149
Cdd:cd15763    1 NVMGNGLSQCLLCGELLGFLGSSSVFCQDCRKKVCTKCGIETSGSQKRPLWLCKICSEQREVWK 64
 
Name Accession Description Interval E-value
FYVE_2 pfam02318
FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector ...
 47-159 5.14e-48

FYVE-type zinc finger; This FYVE-type zinc finger is found at the N-terminus of effector proteins including rabphilin-3A and regulating synaptic membrane exocytosis protein 2.


Pssm-ID: 426716  Cd Length: 118  Bit Score: 156.76  E-value: 5.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676510   47 LSPAEVEAILQVIQRAERLDVLEQQRIGRLVERL--ETMRRNVMGN----GLSQCLLCGEVLGFLGSSSVFCKDCRKKVC 120
Cdd:pfam02318   3 LTDEEAEHVWEVVQRDFDLRKKEEERLGELKGKLdkESSKRELLGNqahlGETHCIRCLQPFGFLVNSKRQCLDCRKNVC 82

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 298676510  121 TKCGIEaspGQKRPLWLCKICSEQREVWKRSGAWFYKGL 159
Cdd:pfam02318  83 KKCGVY---NKPEQGWLCDPCSEARELKKGSLEWFYKNV 118
FYVE_RPH3L cd15763
FYVE-related domain found in Rab effector Noc2 and similar proteins; Rab effector Noc2, also ...
 86-149 8.39e-40

FYVE-related domain found in Rab effector Noc2 and similar proteins; Rab effector Noc2, also termed No C2 domains protein, or rabphilin-3A-like protein (RPH3AL), is a Rab3 effector that mediates the regulation of secretory vesicle exocytosis in neurons and certain endocrine cells. It also functions as a Rab27 effector and is involved in isoproterenol (IPR)-stimulated amylase release from acinar cells. Noc2 contains an N-terminal Rab3A effector domain which harbors a conserved zinc finger, but lacks tandem C2 domains. The FYVE domain of Noc2 resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277302  Cd Length: 64  Bit Score: 133.94  E-value: 8.39e-40
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 298676510  86 NVMGNGLSQCLLCGEVLGFLGSSSVFCKDCRKKVCTKCGIEASPGQKRPLWLCKICSEQREVWK 149
Cdd:cd15763    1 NVMGNGLSQCLLCGELLGFLGSSSVFCQDCRKKVCTKCGIETSGSQKRPLWLCKICSEQREVWK 64
FYVE_RP3A cd15762
FYVE-related domain found in rabphilin-3A and similar proteins; Rabphilin-3A, also termed ...
 89-169 1.01e-35

FYVE-related domain found in rabphilin-3A and similar proteins; Rabphilin-3A, also termed exophilin-1, is an effector protein that binds to the GTP-bound form of Rab3A, which is one of the most abundant Rab proteins in neurons and predominantly localized to synaptic vesicles. Rabphilin-3A is homologous to alpha-Rab3-interacting molecules (RIMs). It is a multi-domain protein containing an N-terminal Rab3A effector domain, a proline-rich linker region, and two tandem C2 domains. The effector domain binds specifically to the activated GTP-bound state of Rab3A and harbors a conserved FYVE zinc finger. The C2 domains are responsible for the binding of phosphatidylinositol-4,5-bisphosphate (PIP2) , a key player in the neurotransmitter release process. Thus, Rabphilin-3A has also been implicated in vesicle trafficking. The FYVE domain of Rabphilin-3A resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277301  Cd Length: 80  Bit Score: 123.91  E-value: 1.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 298676510  89 GNGLSQCLLCGEVLGFLGSSSVFCKDCRKKVCTKCGIEASpGQKRPLWLCKICSEQREVWKRSGAWFYKGLPKYILPLKT 168
Cdd:cd15762    1 GDGVNRCILCGEQLGGAGSACVVCEDCKKNVCTKCGVQTN-NRPHSVWLCKICSEQREVWKRSGAWFFKGLPKQVLPQPM 79


                 .
gi 298676510 169 P 169
Cdd:cd15762   80 P 80
FYVE_RP3A_like cd15746
FYVE-related domain found in rabphilin-3A, Rab effector Noc2, and similar proteins; This ...
 89-143 1.98e-28

FYVE-related domain found in rabphilin-3A, Rab effector Noc2, and similar proteins; This family includes rabphilin-3A and Rab effector Noc2. Rabphilin-3A, also termed exophilin-1, is an effector protein that binds to the GTP-bound form of Rab3A, which is one of the most abundant Rab proteins in neurons and predominantly localized to synaptic vesicles. Rabphilin-3A is homologous to alpha-Rab3-interacting molecules (RIMs). It is a multi-domain protein containing an N-terminal Rab3A effector domain, a proline-rich linker region, and two tandem C2 domains. The effector domain binds specifically to the activated GTP-bound state of Rab3A and harbors a conserved FYVE zinc finger. The C2 domains are responsible for the binding of phosphatidylinositol-4,5-bisphosphate (PIP2) , a key player in the neurotransmitter release process. Thus, Rabphilin-3A has also been implicated in vesicle trafficking. Rab effector Noc2, also termed No C2 domains protein, or rabphilin-3A-like protein (RPH3AL), is a Rab3 effector that mediates the regulation of secretory vesicle exocytosis in neurons and certain endocrine cells. It also functions as a Rab27 effector and is involved in isoproterenol (IPR)-stimulated amylase release from acinar cells. Noc2 contains an N-terminal Rab3A effector domain which only harbors a conserved FYVE zinc finger. The FYVE domains of Rabphilin-3A and Noc2 resemble a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277285  Cd Length: 55  Bit Score: 103.88  E-value: 1.98e-28
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 298676510  89 GNGLSQCLLCGEVLGFLGSSSVFCKDCRKKVCTKCGIEASPGQKRPLWLCKICSE 143
Cdd:cd15746    1 GNGVTQCILCGDEFGLLGASPVLCKDCRKAVCTKCGVETTNSNKQPIWLCKICSE 55
FYVE_BSN_PCLO cd15751
FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon ...
 95-146 1.07e-05

FYVE-related domain found in protein bassoon and piccolo; This family includes protein bassoon and piccolo. Protein bassoon, also termed zinc finger protein 231, is a core component of the presynaptic cytomatrix. It is a vertebrate-specific active zone scaffolding protein that plays a key role in structural organization and functional regulation of presynaptic release sites. Bassoon may modulate synaptic transmission efficiency by binding to presynaptic P/Q-type voltage-dependent calcium channel (VDCC) complexes and modify the channel function. As one of the most highly phosphorylated synaptic proteins, bassoon can interact with the small ubiquitous adaptor protein 14-3-3 in a phosphorylation-dependent manner, which modulates its anchoring to the presynaptic cytomatrix. Protein piccolo, also termed aczonin, is a neuron-specific presynaptic active zone scaffolding protein that mainly interacts with a detergent-resistant cytoskeletal-like subcellular fraction and is involved in the organization of the interplay between neurotransmitter vesicles, the cytoskeleton, and the plasma membrane at synaptic active zones. It binds profilin, an actin-binding protein implicated in actin cytoskeletal dynamics. It also functions as a presynaptic low-affinity Ca2+ sensor and has been implicated in Ca2+ regulation of neurotransmitter release. Both bassoon and piccolo contain two N-terminal FYVE zinc fingers, a PDZ domain and two C-terminal C2 domains. Their FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277290 [Multi-domain]  Cd Length: 62  Bit Score: 42.44  E-value: 1.07e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 298676510  95 CLLCGEVLGFLGSSS----VFCKDCRKKVCTKCGIEA-SPGQKRPLWLCKICSEQRE 146
Cdd:cd15751    3 CPLCGTSELPLGSKSppnyNTCTDCKNRVCNQCGFNStPPVTKVKEWLCLNCQKKRA 59
FYVE_Slp3_4_5 cd15747
FYVE-related domain found in the synaptotagmin-like proteins 3, 4, 5; The synaptotagmin-like ...
 95-143 1.02e-04

FYVE-related domain found in the synaptotagmin-like proteins 3, 4, 5; The synaptotagmin-like proteins 1-5 (Slp1-5) family belongs to the carboxyl-terminal-type (C-type) tandem C2 proteins superfamily, which also contains the synaptotagmin and the Doc2 families. Slp proteins are putative membrane trafficking proteins that are characterized by the presence of a unique N-terminal Slp homology domain (SHD), and C-terminal tandem C2 domains (known as the C2A domain and C2B domain). The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2. The SHD1 and SHD2 of Slp3, Slp4 and Slp5 are separated by a putative FYVE zinc finger. By contrast, Slp1 and Slp2 lack such zinc finger and their SHD1 and SHD2 are linked together. This model corresponds to the FYVE zinc finger. At this point, Slp1 and Slp2 are not included in this model. Moreover, the FYVE domains of Slp3, Slp4 and Slp5 resemble a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277286  Cd Length: 48  Bit Score: 39.20  E-value: 1.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 298676510  95 CLLCGEVLGFLGSSSVFCKDCRKKVCTKCGIEASPgqkRPLWLCKICSE 143
Cdd:cd15747    3 CARCREKLGFIFNRGARCPKCSHKVCKKCRVLTSN---TGKWLCTVCHK 48
FYVE_SlaC2-a cd15752
FYVE-related domain found in Slp homolog lacking C2 domains a (SlaC2-a) and similar proteins; ...
 93-156 7.25e-04

FYVE-related domain found in Slp homolog lacking C2 domains a (SlaC2-a) and similar proteins; SlaC2-a, also termed melanophilin, or exophilin-3, is a GTP-bound form of Rab27A-, myosin Va-, and actin-binding protein present on melanosomes. It is involved in the control of transferring of melanosomes from microtubules to actin filaments. It also functions as a melanocyte type myosin Va (McM5) binding partner and directly activates the actin-activated ATPase activity of McM5 through forming a tripartite protein complex with Rab27A and an actin-based motor myosin Va. SlaC2-a belongs to the Slp homolog lacking C2 domains (Slac2) family. It contains an N-terminal Slp homology domain (SHD), but lacks tandem C2 domains. The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of SlaC2-a are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. Moreover, Slac2-a has a middle myosin-binding domain and a C-terminal actin-binding domain.


Pssm-ID: 277291  Cd Length: 76  Bit Score: 37.86  E-value: 7.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 298676510  93 SQCLLCGEVLGFLGSSSVFCKDCRKKVCTKCgieaSPGQKRPL-WLCKICSEQREVWKRSGAWFY 156
Cdd:cd15752    1 THCARCLQPFQFLLNSGRQCLDCGLRTCKSC----SRYHPEEQgWVCDPCHLARVVKIGSLEWYY 61
FYVE_Slp4 cd15764
FYVE-related domain found in synaptotagmin-like protein 4 (Slp4) and similar proteins; Slp4, ...
 95-142 2.84e-03

FYVE-related domain found in synaptotagmin-like protein 4 (Slp4) and similar proteins; Slp4, also termed exophilin-2, or granuphilin, has been characterized as a regulator of the release of insulin granules from pancreatic beta-cells and dense core granules from PC12 neuronal cells by binding to Rab27A , and amylase granules from parotid gland acinar cells through interaction with syntaxin-2/3 in a Munc18-2-dependent manner on the apical plasma membrane. It can binds to syntaxin 2 in parotid acinar cells. It is also involved in granule transport by recruitment of the motor protein myosin Va. Moreover, it requires Rab8 to increase granule release in platelets. Slp4 contains an N-terminal Slp homology domain (SHD) and C-terminal tandem C2 domains. The Slp homology domain (SHD) consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of Slp4 are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.


Pssm-ID: 277303  Cd Length: 50  Bit Score: 35.14  E-value: 2.84e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 298676510  95 CLLCGEVLGFLGSSSVFCKDCRKKVCTKCGIEASPGQkrplWLCKICS 142
Cdd:cd15764    6 CGRCQESLGRLSPKANQCRGCNHLVCRDCRAVRPNGS----WVCSVCA 49
FYVE_SlaC2-c cd15753
FYVE-related domain found in Slp homolog lacking C2 domains c (SlaC2-c) and similar proteins; ...
 95-145 5.02e-03

FYVE-related domain found in Slp homolog lacking C2 domains c (SlaC2-c) and similar proteins; SlaC2-c, also termed Rab effector MyRIP, or exophilin-8, or myosin-VIIa- and Rab-interacting protein, or synaptotagmin-like protein lacking C2 domains c, is a GTP-bound form of Rab27A-, myosin Va/VIIa-, and actin-binding protein mainly present on retinal melanosomes and secretory granules. It may play a role in insulin granule exocytosis. It is also involved in the control of isoproterenol (IPR)-induced amylase release from parotid acinar cells. SlaC2-c belongs to the Slp homolog lacking C2 domains (Slac2) family. It contains an N-terminal Slp homology domain (SHD), but lacks tandem C2 domains. The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of SlaC2-c are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. Moreover, Slac2-c has a middle myosin-binding domain and a C-terminal actin-binding domain.


Pssm-ID: 277292  Cd Length: 49  Bit Score: 34.69  E-value: 5.02e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 298676510  95 CLLCGEVLGFLGSSSVFCKDCRKKVCTKCgieASPGQKRPLWLCKICSEQR 145
Cdd:cd15753    2 CMRCCSPFTFLFNRKRQCRDCKFNVCKSC---ASYDKKEKGWTCNVCQKQR 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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