SERC1_HUMAN
ID SERC1_HUMAN Reviewed; 453 AA.
AC Q9NRX5; B3KY69; E1P565; O75655; Q7Z2F5; Q8TAG1; Q9NTH8; Q9ULG7;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Serine incorporator 1;
DE AltName: Full=Tumor differentially expressed protein 1-like;
DE AltName: Full=Tumor differentially expressed protein 2;
GN Name=SERINC1; Synonyms=KIAA1253, TDE1L, TDE2; ORFNames=UNQ396/PRO732;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang M., Yu L., Wu Q., Zheng L.H., Wei Y.H., Wan B., Zhao S.Y.;
RT "Identification and characterization of TDE2, a plasma-membrane protein
RT with 11 transmembrane helices, and its variable expression in human lung
RT cancer and liver cancer tissues.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Subthalamic nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351; THR-352; SER-361 AND
RP SER-364, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-298.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=20213681; DOI=10.1002/pmic.200900783;
RA Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E.,
RA Tsunasawa S., Utsumi T.;
RT "Strategy for comprehensive identification of human N-myristoylated
RT proteins using an insect cell-free protein synthesis system.";
RL Proteomics 10:1780-1793(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-352 AND SER-364, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP MYRISTOYLATION AT GLY-2.
RX PubMed=24223779; DOI=10.1371/journal.pone.0078235;
RA Moriya K., Nagatoshi K., Noriyasu Y., Okamura T., Takamitsu E., Suzuki T.,
RA Utsumi T.;
RT "Protein N-myristoylation plays a critical role in the endoplasmic
RT reticulum morphological change induced by overexpression of protein
RT Lunapark, an integral membrane protein of the endoplasmic reticulum.";
RL PLoS ONE 8:E78235-E78235(2013).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Enhances the incorporation of serine into phosphatidylserine
CC and sphingolipids. {ECO:0000250|UniProtKB:Q7TNK0}.
CC -!- SUBUNIT: Interacts with SPTLC1. {ECO:0000250|UniProtKB:Q7TNK0}.
CC -!- INTERACTION:
CC Q9NRX5; O43315: AQP9; NbExp=3; IntAct=EBI-2683145, EBI-17444777;
CC Q9NRX5; O14843: FFAR3; NbExp=3; IntAct=EBI-2683145, EBI-17762181;
CC Q9NRX5; O15529: GPR42; NbExp=3; IntAct=EBI-2683145, EBI-18076404;
CC Q9NRX5; Q8TED1: GPX8; NbExp=3; IntAct=EBI-2683145, EBI-11721746;
CC Q9NRX5; Q06710: PAX8; NbExp=2; IntAct=EBI-2683145, EBI-2683132;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q7TNK0}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q7TNK0}.
CC -!- SIMILARITY: Belongs to the TDE1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF087902; AAP97200.1; -; mRNA.
DR EMBL; AF092436; AAP97211.1; -; Genomic_DNA.
DR EMBL; AB033079; BAA86567.1; ALT_INIT; mRNA.
DR EMBL; AL137261; CAB70662.2; -; mRNA.
DR EMBL; AF164794; AAF80758.1; -; mRNA.
DR EMBL; AY358429; AAQ88795.1; -; mRNA.
DR EMBL; AK128781; BAG54731.1; -; mRNA.
DR EMBL; Z99129; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48172.1; -; Genomic_DNA.
DR EMBL; CH471051; EAW48173.1; -; Genomic_DNA.
DR EMBL; BC028607; AAH28607.1; -; mRNA.
DR EMBL; BC033029; AAH33029.1; -; mRNA.
DR CCDS; CCDS5125.1; -.
DR RefSeq; NP_065806.1; NM_020755.3.
DR AlphaFoldDB; Q9NRX5; -.
DR SMR; Q9NRX5; -.
DR BioGRID; 121579; 84.
DR ELM; Q9NRX5; -.
DR IntAct; Q9NRX5; 40.
DR MINT; Q9NRX5; -.
DR STRING; 9606.ENSP00000342962; -.
DR GlyGen; Q9NRX5; 1 site.
DR iPTMnet; Q9NRX5; -.
DR PhosphoSitePlus; Q9NRX5; -.
DR SwissPalm; Q9NRX5; -.
DR BioMuta; SERINC1; -.
DR DMDM; 25453298; -.
DR EPD; Q9NRX5; -.
DR jPOST; Q9NRX5; -.
DR MassIVE; Q9NRX5; -.
DR MaxQB; Q9NRX5; -.
DR PaxDb; Q9NRX5; -.
DR PeptideAtlas; Q9NRX5; -.
DR PRIDE; Q9NRX5; -.
DR ProteomicsDB; 82437; -.
DR Antibodypedia; 46589; 185 antibodies from 25 providers.
DR DNASU; 57515; -.
DR Ensembl; ENST00000339697.5; ENSP00000342962.3; ENSG00000111897.7.
DR GeneID; 57515; -.
DR KEGG; hsa:57515; -.
DR MANE-Select; ENST00000339697.5; ENSP00000342962.3; NM_020755.4; NP_065806.1.
DR UCSC; uc003pyy.2; human.
DR CTD; 57515; -.
DR DisGeNET; 57515; -.
DR GeneCards; SERINC1; -.
DR HGNC; HGNC:13464; SERINC1.
DR HPA; ENSG00000111897; Low tissue specificity.
DR MIM; 614548; gene.
DR neXtProt; NX_Q9NRX5; -.
DR OpenTargets; ENSG00000111897; -.
DR PharmGKB; PA134973249; -.
DR VEuPathDB; HostDB:ENSG00000111897; -.
DR eggNOG; KOG2592; Eukaryota.
DR GeneTree; ENSGT01030000234623; -.
DR HOGENOM; CLU_029574_5_0_1; -.
DR InParanoid; Q9NRX5; -.
DR OMA; MEPDDKQ; -.
DR OrthoDB; 1276632at2759; -.
DR PhylomeDB; Q9NRX5; -.
DR TreeFam; TF312881; -.
DR PathwayCommons; Q9NRX5; -.
DR Reactome; R-HSA-977347; Serine biosynthesis.
DR SignaLink; Q9NRX5; -.
DR BioGRID-ORCS; 57515; 18 hits in 1075 CRISPR screens.
DR ChiTaRS; SERINC1; human.
DR GeneWiki; SERINC1; -.
DR GenomeRNAi; 57515; -.
DR Pharos; Q9NRX5; Tbio.
DR PRO; PR:Q9NRX5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9NRX5; protein.
DR Bgee; ENSG00000111897; Expressed in pons and 207 other tissues.
DR Genevisible; Q9NRX5; HS.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:HGNC-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:HGNC-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; ISS:BHF-UCL.
DR GO; GO:0044091; P:membrane biogenesis; ISS:BHF-UCL.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; ISS: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; ISS:HGNC.
DR GO; GO:1904222; P:positive regulation of serine C-palmitoyltransferase activity; ISS:BHF-UCL.
DR GO; GO:0006665; P:sphingolipid metabolic process; ISS:HGNC-UCL.
DR InterPro; IPR029557; Serinc1/3.
DR InterPro; IPR005016; TDE1/TMS.
DR PANTHER; PTHR10383; PTHR10383; 1.
DR PANTHER; PTHR10383:SF15; PTHR10383:SF15; 1.
DR Pfam; PF03348; Serinc; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism;
KW Lipoprotein; Membrane; Myristate; Phospholipid biosynthesis;
KW Phospholipid metabolism; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..453
FT /note="Serine incorporator 1"
FT /id="PRO_0000218966"
FT TOPO_DOM 2..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..88
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 110..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..151
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..197
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..231
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..309
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 331..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..426
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 448..453
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 352
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:20213681,
FT ECO:0000269|PubMed:24223779"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT VARIANT 199
FT /note="L -> V (in dbSNP:rs13210569)"
FT /id="VAR_052275"
FT VARIANT 216
FT /note="F -> V (in dbSNP:rs13210446)"
FT /id="VAR_052276"
FT VARIANT 225
FT /note="S -> G (in dbSNP:rs17260829)"
FT /id="VAR_052277"
FT CONFLICT 89
FT /note="A -> S (in Ref. 9; AAH28607)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="S -> F (in Ref. 1; AAP97200/AAP97211)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="Y -> S (in Ref. 5; AAQ88795)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 453 AA; 50495 MW; 3868DBF38165B78C CRC64;
MGSVLGLCSM ASWIPCLCGS APCLLCRCCP SGNNSTVTRL IYALFLLVGV CVACVMLIPG
MEEQLNKIPG FCENEKGVVP CNILVGYKAV YRLCFGLAMF YLLLSLLMIK VKSSSDPRAA
VHNGFWFFKF AAAIAIIIGA FFIPEGTFTT VWFYVGMAGA FCFILIQLVL LIDFAHSWNE
SWVEKMEEGN SRCWYAALLS ATALNYLLSL VAIVLFFVYY THPASCSENK AFISVNMLLC
VGASVMSILP KIQESQPRSG LLQSSVITVY TMYLTWSAMT NEPETNCNPS LLSIIGYNTT
STVPKEGQSV QWWHAQGIIG LILFLLCVFY SSIRTSNNSQ VNKLTLTSDE STLIEDGGAR
SDGSLEDGDD VHRAVDNERD GVTYSYSFFH FMLFLASLYI MMTLTNWYRY EPSREMKSQW
TAVWVKISSS WIGIVLYVWT LVAPLVLTNR DFD
