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Conserved domains on  [gi|1060098975|ref|NP_001317330|]
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sideroflexin-5 isoform 3 [Homo sapiens]

Protein Classification

sideroflexin family transporter( domain architecture ID 2167)

sideroflexin family transporter is a mitochondrial membrane protein implicated in one-carbon metabolism; similar to sideroflexin-1, which acts as a mitochondrial serine transporter

Gene Ontology:  GO:0055085|GO:0015075|GO:0006811|GO:0006730
PubMed:  8132491|33260588|33494450
TCDB:  2.A.54

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SFXNs super family cl04275
Sideroflexins; This family contains sideroflexin 1, 2 and 3 (SFXN1/2/3). SFXN1 is a multipass ...
 26-213 3.20e-101

Sideroflexins; This family contains sideroflexin 1, 2 and 3 (SFXN1/2/3). SFXN1 is a multipass mitochondrial membrane protein and is part of the sideroflexin family of proteins conserved throughout eukaryotes. In humans, SFXN1 is highly expressed in the blood, liver, and kidney, which are tissues with high one-carbon metabolism activity. SFXN1 functions as a mitochondrial serine transporter in one-carbon metabolism. SFXN1 and SFXN3 (and perhaps SFXN2) are the main mitochondrial serine transporters in human cells and Sfxn1-3 also have this function in D. melanogaster. SFXN1 and SFXN3 likely have other physiologically relevant substrates besides serine, such as alanine or cysteine. Because SFXN1 is expressed in many cancers most highly in leukemias and lymphomas and its expression is likely regulated by the Myc transcription factor, it is suggested that it may have roles in cancer cell growth. Furthermore, Myc-binding sites were found in the promoters of SFXN1, SFXN2, and SFXN3.


The actual alignment was detected with superfamily member pfam03820:

Pssm-ID: 470990  Cd Length: 319  Bit Score: 297.11  E-value: 3.20e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098975  26 QLGKPRFQQTSFYGRFRHFLDIIDPRTLFVTERRLREAVQLLEDYKHGTLRPGVTNEQLWSAQKIKQAILHPDTNEKIFM 105
Cdd:pfam03820   1 DLDKPRWDQSTYWGRLKHFFDITDPRTLLASDAELEEAKELVDDYKKGKEPPGTTEEELWRAKKLYDSAFHPDTGEKIFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098975 106 PFRMSGYIPFGTPIVVGLLLPNQTLASTVFWQWLNQSHNACVNYANRNATKPSPASKFIQGYLGAVISAVSIAVGLNVLV 185
Cdd:pfam03820  81 PFRMSAQVPMNMPITGGMLTPYKTTPAVIFWQWVNQSFNAAVNYANRNASSPMSTSQLAQAYVAAVTAACGVALGLNSLV 160

                         170       180
                  ....*....|....*....|....*...
gi 1060098975 186 QKaNKFTPATRLLIQRFVPFPAVGRLSC 213
Cdd:pfam03820 161 KR-LKLSPATRLLLGRLVPFAAVAAANC 187
 
Name Accession Description Interval E-value
SFXNs pfam03820
Sideroflexins; This family contains sideroflexin 1, 2 and 3 (SFXN1/2/3). SFXN1 is a multipass ...
 26-213 3.20e-101

Sideroflexins; This family contains sideroflexin 1, 2 and 3 (SFXN1/2/3). SFXN1 is a multipass mitochondrial membrane protein and is part of the sideroflexin family of proteins conserved throughout eukaryotes. In humans, SFXN1 is highly expressed in the blood, liver, and kidney, which are tissues with high one-carbon metabolism activity. SFXN1 functions as a mitochondrial serine transporter in one-carbon metabolism. SFXN1 and SFXN3 (and perhaps SFXN2) are the main mitochondrial serine transporters in human cells and Sfxn1-3 also have this function in D. melanogaster. SFXN1 and SFXN3 likely have other physiologically relevant substrates besides serine, such as alanine or cysteine. Because SFXN1 is expressed in many cancers most highly in leukemias and lymphomas and its expression is likely regulated by the Myc transcription factor, it is suggested that it may have roles in cancer cell growth. Furthermore, Myc-binding sites were found in the promoters of SFXN1, SFXN2, and SFXN3.


Pssm-ID: 461063  Cd Length: 319  Bit Score: 297.11  E-value: 3.20e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098975  26 QLGKPRFQQTSFYGRFRHFLDIIDPRTLFVTERRLREAVQLLEDYKHGTLRPGVTNEQLWSAQKIKQAILHPDTNEKIFM 105
Cdd:pfam03820   1 DLDKPRWDQSTYWGRLKHFFDITDPRTLLASDAELEEAKELVDDYKKGKEPPGTTEEELWRAKKLYDSAFHPDTGEKIFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098975 106 PFRMSGYIPFGTPIVVGLLLPNQTLASTVFWQWLNQSHNACVNYANRNATKPSPASKFIQGYLGAVISAVSIAVGLNVLV 185
Cdd:pfam03820  81 PFRMSAQVPMNMPITGGMLTPYKTTPAVIFWQWVNQSFNAAVNYANRNASSPMSTSQLAQAYVAAVTAACGVALGLNSLV 160

                         170       180
                  ....*....|....*....|....*...
gi 1060098975 186 QKaNKFTPATRLLIQRFVPFPAVGRLSC 213
Cdd:pfam03820 161 KR-LKLSPATRLLLGRLVPFAAVAAANC 187
mtc TIGR00798
tricarboxylate carrier; The MTC family consists of a limited number of homologues, all from ...
 23-208 5.63e-81

tricarboxylate carrier; The MTC family consists of a limited number of homologues, all from eukaryotes. A single member of the family has been functionally characterized, the tricarboxylate carrier from rat liver mitochondria. The rat liver mitochondrial tricarboxylate carrier has been reported to transport citrate, cis-aconitate, threo-D-isocitrate, D- and L-tartrate, malate, succinate and phosphoenolpyruvate. It presumably functions by a proton symport mechanism. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 129880  Cd Length: 318  Bit Score: 245.74  E-value: 5.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098975  23 PPFQLGKPRFQQTSFYGRFRHFLDIIDPRTLFVTERRLREAVQLLEDYKHGTLRPgVTNEQLWSAQKIKQAILHPDTNEK 102
Cdd:TIGR00798   1 PTFDISKPRWDQSTFLGRARHFFEITNPLTLFSSEKQLEKAREIVEDYKAGKASP-LTVDELWRAKKLYDSAFHPDTGEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098975 103 IFMPFRMSGYIPFGTPIVVGLLLPNQTLASTVFWQWLNQSHNACVNYANRNATKPSPASKFIQGYLGAVISAVSIAVGLN 182
Cdd:TIGR00798  80 MFLPGRMSAQVPMNMVITGGMLTPYRSTPGVVFWQWINQSFNAAVNYTNRSGDSPLTLSQLLVSYCAAVTGACGVALGLN 159

                         170       180
                  ....*....|....*....|....*.
gi 1060098975 183 VLVQKANKFTPatrlLIQRFVPFPAV 208
Cdd:TIGR00798 160 MMVKKSPSLSP----LIGRLVPFAAV 181
 
Name Accession Description Interval E-value
SFXNs pfam03820
Sideroflexins; This family contains sideroflexin 1, 2 and 3 (SFXN1/2/3). SFXN1 is a multipass ...
 26-213 3.20e-101

Sideroflexins; This family contains sideroflexin 1, 2 and 3 (SFXN1/2/3). SFXN1 is a multipass mitochondrial membrane protein and is part of the sideroflexin family of proteins conserved throughout eukaryotes. In humans, SFXN1 is highly expressed in the blood, liver, and kidney, which are tissues with high one-carbon metabolism activity. SFXN1 functions as a mitochondrial serine transporter in one-carbon metabolism. SFXN1 and SFXN3 (and perhaps SFXN2) are the main mitochondrial serine transporters in human cells and Sfxn1-3 also have this function in D. melanogaster. SFXN1 and SFXN3 likely have other physiologically relevant substrates besides serine, such as alanine or cysteine. Because SFXN1 is expressed in many cancers most highly in leukemias and lymphomas and its expression is likely regulated by the Myc transcription factor, it is suggested that it may have roles in cancer cell growth. Furthermore, Myc-binding sites were found in the promoters of SFXN1, SFXN2, and SFXN3.


Pssm-ID: 461063  Cd Length: 319  Bit Score: 297.11  E-value: 3.20e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098975  26 QLGKPRFQQTSFYGRFRHFLDIIDPRTLFVTERRLREAVQLLEDYKHGTLRPGVTNEQLWSAQKIKQAILHPDTNEKIFM 105
Cdd:pfam03820   1 DLDKPRWDQSTYWGRLKHFFDITDPRTLLASDAELEEAKELVDDYKKGKEPPGTTEEELWRAKKLYDSAFHPDTGEKIFL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098975 106 PFRMSGYIPFGTPIVVGLLLPNQTLASTVFWQWLNQSHNACVNYANRNATKPSPASKFIQGYLGAVISAVSIAVGLNVLV 185
Cdd:pfam03820  81 PFRMSAQVPMNMPITGGMLTPYKTTPAVIFWQWVNQSFNAAVNYANRNASSPMSTSQLAQAYVAAVTAACGVALGLNSLV 160

                         170       180
                  ....*....|....*....|....*...
gi 1060098975 186 QKaNKFTPATRLLIQRFVPFPAVGRLSC 213
Cdd:pfam03820 161 KR-LKLSPATRLLLGRLVPFAAVAAANC 187
mtc TIGR00798
tricarboxylate carrier; The MTC family consists of a limited number of homologues, all from ...
 23-208 5.63e-81

tricarboxylate carrier; The MTC family consists of a limited number of homologues, all from eukaryotes. A single member of the family has been functionally characterized, the tricarboxylate carrier from rat liver mitochondria. The rat liver mitochondrial tricarboxylate carrier has been reported to transport citrate, cis-aconitate, threo-D-isocitrate, D- and L-tartrate, malate, succinate and phosphoenolpyruvate. It presumably functions by a proton symport mechanism. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 129880  Cd Length: 318  Bit Score: 245.74  E-value: 5.63e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098975  23 PPFQLGKPRFQQTSFYGRFRHFLDIIDPRTLFVTERRLREAVQLLEDYKHGTLRPgVTNEQLWSAQKIKQAILHPDTNEK 102
Cdd:TIGR00798   1 PTFDISKPRWDQSTFLGRARHFFEITNPLTLFSSEKQLEKAREIVEDYKAGKASP-LTVDELWRAKKLYDSAFHPDTGEK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1060098975 103 IFMPFRMSGYIPFGTPIVVGLLLPNQTLASTVFWQWLNQSHNACVNYANRNATKPSPASKFIQGYLGAVISAVSIAVGLN 182
Cdd:TIGR00798  80 MFLPGRMSAQVPMNMVITGGMLTPYRSTPGVVFWQWINQSFNAAVNYTNRSGDSPLTLSQLLVSYCAAVTGACGVALGLN 159

                         170       180
                  ....*....|....*....|....*.
gi 1060098975 183 VLVQKANKFTPatrlLIQRFVPFPAV 208
Cdd:TIGR00798 160 MMVKKSPSLSP----LIGRLVPFAAV 181
 
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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