SERC5_RAT
ID SERC5_RAT Reviewed; 460 AA.
AC Q63175; G3V9U9;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Serine incorporator 5;
DE AltName: Full=Developmentally regulated protein TPO1 {ECO:0000303|PubMed:9326262};
GN Name=Serinc5; Synonyms=Tpo1 {ECO:0000303|PubMed:9326262};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INDUCTION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Sprague-Dawley; TISSUE=Telencephalon;
RX PubMed=9326262; DOI=10.1046/j.1471-4159.1997.69041343.x;
RA Krueger W.H.H., Gonye G.E., Madison D.L., Murray K.E., Kumar M.,
RA Spoerel N., Pfeiffer S.E.;
RT "TPO1, a member of a novel protein family, is developmentally regulated in
RT cultured oligodendrocytes.";
RL J. Neurochem. 69:1343-1355(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INDUCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=16120614; DOI=10.1074/jbc.m505712200;
RA Inuzuka M., Hayakawa M., Ingi T.;
RT "Serinc, an activity-regulated protein family, incorporates serine into
RT membrane lipid synthesis.";
RL J. Biol. Chem. 280:35776-35783(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Restriction factor required to restrict infectivity of
CC gammaretroviruses: acts by inhibiting early step of viral infection and
CC impairing the ability of the viral particle to translocate its content
CC to the cytoplasm (By similarity). Enhances the incorporation of serine
CC into phosphatidylserine and sphingolipids. May play a role in providing
CC serine molecules for the formation of myelin glycosphingolipids in
CC oligodendrocytes. {ECO:0000250|UniProtKB:Q86VE9,
CC ECO:0000269|PubMed:16120614, ECO:0000269|PubMed:9326262}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86VE9};
CC Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the cell
CC membrane, where it is efficiently incorporated into budding
CC gammaretrovirus virions and impairs subsequent virion penetration of
CC susceptible target cells. {ECO:0000250|UniProtKB:Q86VE9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q63175-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q63175-2; Sequence=VSP_033056;
CC -!- TISSUE SPECIFICITY: Brain. Expressed at high levels in the white matter
CC and the oligodendroglial cells of the brain. Expressed at low levels in
CC the liver. {ECO:0000269|PubMed:16120614, ECO:0000269|PubMed:9326262}.
CC -!- DEVELOPMENTAL STAGE: First detected in significant amounts at postnatal
CC day 2 (P2) and increases about twofold to a peak value at P17-P20 and
CC declines significantly thereafter. {ECO:0000269|PubMed:9326262}.
CC -!- INDUCTION: Up-regulated during the differentiation of oligodendrocyte
CC lineage cells and during brain development at the time of myelination.
CC Down-regulated in the hippocampal CA fields and dentate gyrus by
CC seizures. {ECO:0000269|PubMed:16120614, ECO:0000269|PubMed:9326262}.
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDM10024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; L20319; AAA41097.1; -; mRNA.
DR EMBL; DQ103710; AAZ80297.1; -; mRNA.
DR EMBL; AABR07007649; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07007650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07007651; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07072694; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130639; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473955; EDM10024.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_596886.2; NM_133395.2.
DR AlphaFoldDB; Q63175; -.
DR SMR; Q63175; -.
DR STRING; 10116.ENSRNOP00000060697; -.
DR GlyGen; Q63175; 2 sites.
DR PaxDb; Q63175; -.
DR GeneID; 170907; -.
DR KEGG; rno:170907; -.
DR UCSC; RGD:621571; rat. [Q63175-1]
DR CTD; 256987; -.
DR RGD; 621571; Serinc5.
DR eggNOG; KOG2592; Eukaryota.
DR InParanoid; Q63175; -.
DR OrthoDB; 1276632at2759; -.
DR PhylomeDB; Q63175; -.
DR TreeFam; TF312881; -.
DR Reactome; R-RNO-977347; Serine biosynthesis.
DR PRO; PR:Q63175; -.
DR Proteomes; UP000002494; Unplaced.
DR Proteomes; UP000234681; Chromosome 2.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0043209; C:myelin sheath; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL.
DR GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
DR GO; GO:0009597; P:detection of virus; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; ISS:UniProtKB.
DR GO; GO:0042552; P:myelination; IEP:RGD.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; IDA:HGNC-UCL.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1904219; P:positive regulation of CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IDA:BHF-UCL.
DR GO; GO:1904222; P:positive regulation of serine C-palmitoyltransferase activity; IDA:BHF-UCL.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS:HGNC-UCL.
DR InterPro; IPR029555; Serinc5.
DR InterPro; IPR005016; TDE1/TMS.
DR PANTHER; PTHR10383; PTHR10383; 1.
DR PANTHER; PTHR10383:SF16; PTHR10383:SF16; 1.
DR Pfam; PF03348; Serinc; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Antiviral defense; Cell membrane; Glycoprotein;
KW Immunity; Innate immunity; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..460
FT /note="Serine incorporator 5"
FT /id="PRO_0000330633"
FT TOPO_DOM 1..36
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 37..57
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 58..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..124
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 146..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..250
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..258
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..390
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..427
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..448
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..460
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9326262"
FT /id="VSP_033056"
SQ SEQUENCE 460 AA; 51856 MW; CB9DA60F66282FB3 CRC64;
MSARCCAGQL ACCCGSAGCA LCCGCCPKFR QSRSTRFMYL FYFTLVIIPC CVMMSPSVMK
QMTEHIPFFE DFCKGIKAGD TCENLVGYSA VYRVCFGMAC FFFVFCVLTF KVNNSKSCRA
SIHNGFWFFK LLLLGAMCSG AFFIPDQETF LNVWRYVGAV GSFFFICIQL LLIVEFAHKW
NKNWTAGTVR NKLWYASLSL ALIMYSIAVG GLALMAVFYT QWDDCMDNKI LLGVHGGLCV
LISLAAISPC VQNRQPHSGL LQPGLISCYV TYLTFSALTS KPEKVVKDEH GKNVTICVPD
FGQDFRRDES MVTWLGTLLL VVCISYSCLT STTRSSSDAL QRRYGAPELE VARCCFCFGP
DGEDTEEQQN VKEGPRVIYD EKKGTVYSYS YFHFVLLLAS LYVMMTLTSW FHYENATIET
FFVGSWSIFW VKMASCWMCV LLYLWTLVAP LCCPSRQFSV
