SERC4_RAT
ID SERC4_RAT Reviewed; 492 AA.
AC A8WCG0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Serine incorporator 4;
GN Name=Serinc4;
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] (ISOFORM 2).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Ingi T., Hayakawa M., Ohmori N.;
RT "Structure, localization, and functional diversity of serinc family
RT revealed by two novel subtypes, serinc3 and serinc4.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
CC -!- FUNCTION: Incorporates a polar amino acid serine into membranes and
CC facilitates the synthesis of two serine-derived lipids,
CC phosphatidylserine and sphingolipids. {ECO:0000250|UniProtKB:A6NH21}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A8WCG0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A8WCG0-2; Sequence=VSP_033586;
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
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DR EMBL; EU220432; ABW95046.1; -; mRNA.
DR EMBL; AC097745; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006234915.1; XM_006234853.3. [A8WCG0-1]
DR AlphaFoldDB; A8WCG0; -.
DR SMR; A8WCG0; -.
DR STRING; 10116.ENSRNOP00000021008; -.
DR PhosphoSitePlus; A8WCG0; -.
DR PaxDb; A8WCG0; -.
DR Ensembl; ENSRNOT00000089433; ENSRNOP00000072425; ENSRNOG00000015499. [A8WCG0-2]
DR GeneID; 311358; -.
DR UCSC; RGD:1566077; rat. [A8WCG0-1]
DR CTD; 619189; -.
DR RGD; 1566077; Serinc4.
DR VEuPathDB; HostDB:ENSRNOG00000015499; -.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR HOGENOM; CLU_029574_5_2_1; -.
DR InParanoid; A8WCG0; -.
DR OMA; IHNFWFL; -.
DR OrthoDB; 1276632at2759; -.
DR PhylomeDB; A8WCG0; -.
DR Reactome; R-RNO-977347; Serine biosynthesis.
DR PRO; PR:A8WCG0; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000015499; Expressed in heart and 19 other tissues.
DR ExpressionAtlas; A8WCG0; baseline.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR029563; Serinc4.
DR InterPro; IPR005016; TDE1/TMS.
DR PANTHER; PTHR10383; PTHR10383; 1.
DR PANTHER; PTHR10383:SF5; PTHR10383:SF5; 1.
DR Pfam; PF03348; Serinc; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Lipid biosynthesis; Lipid metabolism; Membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..492
FT /note="Serine incorporator 4"
FT /id="PRO_0000333873"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 421..441
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..229
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_033586"
FT CONFLICT 454
FT /note="K -> R (in Ref. 1; ABW95046)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="L -> P (in Ref. 1; ABW95046)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 54011 MW; C9B23FECC1898DF4 CRC64;
MGAKDITGRS TTQGFAQQHG GVSDVVVKTP FYQVSCCGPV SWTSGCHSLT ESTCSRLFYI
LLHMGASAIC CLLLSKTVVE RVWGKAHGIQ MPSVLCAHLF GNSDCPVLSG SGAVYRVCAG
TATFHLLQAV LLVRLHSPTS PRAQLHNSFW SLKLLFLLGL CTAAFCIPDE HLFPAWHYIG
ICGGFTFILL QLVLITAFAQ SWNKNWQTGA AQDCSWFLGV LLATLGFYSM AGVGAVLLFH
HYTHPDGCLL NKMLLSLHLC FCGLLSLLSI APCIRLRQPN SGLLQASIIS CYIMYLTFSA
LSSRPPETII FQGQNHTLCL PGQNKMEPQI PDASVAVFSA SIMYACVLFA CNEASYLAQL
FGPLWIIKVY KYEFQKPSVC FCCPQTVEPE DGQGSRARPA DQETPPAAQV QSQHLSYSYS
GFHFAFFLAS LYVMVTLTNW FSYEEAELEK TFTKGSWATF WVKVASCWAC VLLYLGLLLA
PLLAHHSESP PP
