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 17-JUN-2020, entry version 166. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 BioGRID; 121579; 48. DR ELM; Q9NRX5; -. DR IntAct; Q9NRX5; 39. DR MINT; Q9NRX5; -. DR STRING; 9606.ENSP00000342962; -. 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; 157 antibodies. DR DNASU; 57515; -. DR Ensembl; ENST00000339697; ENSP00000342962; ENSG00000111897. DR GeneID; 57515; -. DR KEGG; hsa:57515; -. DR UCSC; uc003pyy.2; human. DR CTD; 57515; -. DR DisGeNET; 57515; -. DR EuPathDB; HostDB:ENSG00000111897.6; -. 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 eggNOG; KOG2592; Eukaryota. DR eggNOG; ENOG410XP7K; LUCA. DR GeneTree; ENSGT00950000182793; -. DR HOGENOM; CLU_029574_5_0_1; -. DR InParanoid; Q9NRX5; -. DR KO; K23544; -. DR OMA; VGIACIM; -. DR OrthoDB; 1276632at2759; -. DR PhylomeDB; Q9NRX5; -. DR TreeFam; TF312881; -. DR Reactome; R-HSA-977347; Serine biosynthesis. DR BioGRID-ORCS; 57515; 6 hits in 786 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 substantia nigra and 236 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:0019899; F:enzyme binding; IEA:Ensembl. 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:BHF-UCL. 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; Polymorphism; Reference proteome; KW Transmembrane; 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:0000244|PubMed:18669648" FT MOD_RES 352 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:23186163" FT MOD_RES 361 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648" FT MOD_RES 364 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:18669648, FT ECO:0000244|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 //