ID SORT_RAT Reviewed; 825 AA. AC O54861; O35389; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 20-DEC-2005, sequence version 3. DT 24-JAN-2024, entry version 177. DE RecName: Full=Sortilin {ECO:0000305}; DE AltName: Full=Glycoprotein 110; DE Short=Gp110; DE AltName: Full=Neurotensin receptor 3; DE Short=NTR3; DE Flags: Precursor; GN Name=Sort1 {ECO:0000312|RGD:619999}; 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 [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 [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 89-825, PROTEIN SEQUENCE OF 78-93, PARTIAL RP PROTEIN SEQUENCE, AND SUBCELLULAR LOCATION. RC STRAIN=Sprague-Dawley; TISSUE=Adipocyte; RX PubMed=9452485; DOI=10.1074/jbc.273.6.3582; RA Morris N.J., Ross S.A., Lane W.S., Moestrup S.K., Petersen C.M., RA Keller S.R., Lienhard G.E.; RT "Sortilin is the major 110-kDa protein in GLUT4 vesicles from adipocytes."; RL J. Biol. Chem. 273:3582-3587(1998). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 121-745, PARTIAL PROTEIN SEQUENCE, RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=Sprague-Dawley; TISSUE=Skeletal muscle; RX PubMed=9305862; DOI=10.1074/jbc.272.39.24145; RA Lin B.-Z., Pilch P.F., Kandror K.V.; RT "Sortilin is a major protein component of Glut4-containing vesicles."; RL J. Biol. Chem. 272:24145-24147(1997). RN [4] RP FUNCTION. RX PubMed=12771154; DOI=10.1074/jbc.c300141200; RA Conticello S.G., Kowalsman N.D., Jacobsen C., Yudkovsky G., Sato K., RA Elazar Z., Petersen C.M., Aronheim A., Fainzilber M.; RT "The prodomain of a secreted hydrophobic mini-protein facilitates its RT export from the endoplasmic reticulum by hitchhiking on sorting RT receptors."; RL J. Biol. Chem. 278:26311-26314(2003). RN [5] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12746864; DOI=10.1002/cne.10708; RA Sarret P., Krzywkowski P., Segal L., Nielsen M.S., Petersen C.M., RA Mazella J., Stroh T., Beaudet A.; RT "Distribution of NTS3 receptor/sortilin mRNA and protein in the rat central RT nervous system."; RL J. Comp. Neurol. 461:483-505(2003). RN [6] RP INTERACTION WITH BDNF. RX PubMed=15987945; DOI=10.1523/jneurosci.1017-05.2005; RA Chen Z.-Y., Ieraci A., Teng H., Dall H., Meng C.-X., Herrera D.G., RA Nykjaer A., Hempstead B.L., Lee F.S.; RT "Sortilin controls intracellular sorting of brain-derived neurotrophic RT factor to the regulated secretory pathway."; RL J. Neurosci. 25:6156-6166(2005). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-819, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22673903; DOI=10.1038/ncomms1871; RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., RA Olsen J.V.; RT "Quantitative maps of protein phosphorylation sites across 14 different rat RT organs and tissues."; RL Nat. Commun. 3:876-876(2012). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-404, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=24090084; DOI=10.1021/pr400783j; RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R., RA Graham M.E., Packer N.H., Cordwell S.J.; RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome RT heterogeneity."; RL J. Proteome Res. 12:5791-5800(2013). RN [9] RP CLEAVAGE OF SIGNAL PEPTIDE AFTER GLY-31, CLEAVAGE OF PROPEPTIDE AFTER RP TRP-73, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=26479776; DOI=10.1021/acs.jproteome.5b00820; RA Tsuchiya T., Osaki T., Minamino N., Sasaki K.; RT "Peptidomics for studying limited proteolysis."; RL J. Proteome Res. 14:4921-4931(2015). CC -!- FUNCTION: Functions as a sorting receptor in the Golgi compartment and CC as a clearance receptor on the cell surface. Required for protein CC transport from the Golgi apparatus to the lysosomes by a pathway that CC is independent of the mannose-6-phosphate receptor (M6PR). Lysosomal CC proteins bind specifically to the receptor in the Golgi apparatus and CC the resulting receptor-ligand complex is transported to an acidic CC prelysosomal compartment where the low pH mediates the dissociation of CC the complex. The receptor is then recycled back to the Golgi for CC another round of trafficking through its binding to the retromer. Also CC required for protein transport from the Golgi apparatus to the CC endosomes. Promotes neuronal apoptosis by mediating endocytosis of the CC proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also CC acts as a receptor for neurotensin. May promote mineralization of the CC extracellular matrix during osteogenic differentiation by scavenging CC extracellular LPL. Probably required in adipocytes for the formation of CC specialized storage vesicles containing the glucose transporter CC SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide CC a stable pool of SLC2A4 and confer increased responsiveness to insulin CC (By similarity). May also mediate transport from the endoplasmic CC reticulum to the Golgi (PubMed:12771154). CC {ECO:0000250|UniProtKB:Q99523, ECO:0000269|PubMed:12771154}. CC -!- SUBUNIT: Interacts with LPL and SLC2A4 (By similarity). Interacts with CC the cytosolic adapter proteins GGA1 and GGA2. Interacts with numerous CC ligands including the receptor-associated protein LRPAP1/RAP, GM2A and CC NTS. Forms a complex with NGFR which binds specifically to the CC precursor forms of NGFB (proNGFB) and BDNF (proBDNF) (PubMed:15987945). CC Interacts with the Trk receptors NTRK1, NTRK2 and NTRK3; may regulate CC their anterograde axonal transport and signaling. Interacts with CLN5. CC Interacts with PSAP. Interacts with GRN; this interaction mediates CC endocytosis and lysosome delivery of progranulin; interaction occurs at CC the neuronal cell surface in a stressed nervous system (By similarity). CC Interacts with the heterotrimeric retromer cargo-selective complex CC (CSC), also described as vacuolar protein sorting subcomplex (VPS), CC formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35; which is involved CC in retrograde trafficking of the receptor from endosomes to the Golgi CC apparatus (By similarity). Interacts with SMPD1; the interaction is CC required for SMPD1 targeting to lysosomes (By similarity). CC {ECO:0000250|UniProtKB:Q6PHU5, ECO:0000250|UniProtKB:Q99523, CC ECO:0000269|PubMed:15987945}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:Q99523}. Endosome membrane CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:Q99523}. Endoplasmic reticulum membrane CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:Q99523}. Nucleus membrane CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:Q99523}. Cell membrane CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:Q99523}; Extracellular side CC {ECO:0000250|UniProtKB:Q99523}. Lysosome membrane CC {ECO:0000250|UniProtKB:Q99523}; Single-pass type I membrane protein CC {ECO:0000250|UniProtKB:Q99523}. Note=Localized to membranes of the CC endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A CC small fraction of the protein is also localized to the plasma membrane. CC May also be found in SLC2A4/GLUT4 storage vesicles (GSVs) in CC adipocytes. Localization to the plasma membrane in adipocytes may be CC enhanced by insulin. {ECO:0000250|UniProtKB:Q99523}. CC -!- TISSUE SPECIFICITY: Highly expressed in fat, brain, and lung. Expressed CC in neuronal bodies and dendrites of the piriform cortex and CC hippocampus. Also expressed in the islands of Calleja, medial and CC lateral septal nuclei, amygdaloid nuclei, thalamic nuclei, the CC supraoptic nucleus, the substantia nigra, the Purkinje layer of the CC cerebellar cortex and the cranial motor nerve nuclei of the brainstem. CC {ECO:0000269|PubMed:12746864, ECO:0000269|PubMed:9305862}. CC -!- DOMAIN: The N-terminal propeptide may facilitate precursor transport CC within the Golgi stack. Intrachain binding of the N-terminal propeptide CC and the extracellular domain may also inhibit premature ligand binding CC (By similarity). {ECO:0000250}. CC -!- DOMAIN: The extracellular domain may be shed following protease CC cleavage in some cell types. {ECO:0000250}. CC -!- PTM: The N-terminal propeptide is cleaved by furin and possibly other CC homologous proteases. {ECO:0000250|UniProtKB:Q99523}. CC -!- PTM: Phosphorylation at Ser-819 facilitates the interaction with GGA1. CC {ECO:0000250|UniProtKB:Q99523}. CC -!- PTM: Palmitoylated. Undergoes cysteine S-palmitoylation which promotes CC the partitioning of the receptor into an endosomal membrane subdomain CC where it can interact with the retromer cargo-selective complex which CC mediates its retrograde trafficking to the Golgi apparatus. CC {ECO:0000250|UniProtKB:Q99523}. CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORT1 CC subfamily. {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; AABR03012291; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03012896; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03017724; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03019134; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AABR03020083; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF019109; AAC02932.1; -; mRNA. DR EMBL; AF023621; AAB81864.1; -; mRNA. DR RefSeq; NP_113955.1; NM_031767.1. DR AlphaFoldDB; O54861; -. DR SMR; O54861; -. DR IntAct; O54861; 4. DR MINT; O54861; -. DR STRING; 10116.ENSRNOP00000051102; -. DR GlyCosmos; O54861; 6 sites, 3 glycans. DR GlyGen; O54861; 6 sites, 3 N-linked glycans (1 site). DR iPTMnet; O54861; -. DR PhosphoSitePlus; O54861; -. DR SwissPalm; O54861; -. DR PaxDb; 10116-ENSRNOP00000051102; -. DR GeneID; 83576; -. DR KEGG; rno:83576; -. DR UCSC; RGD:619999; rat. DR AGR; RGD:619999; -. DR CTD; 6272; -. DR RGD; 619999; Sort1. DR VEuPathDB; HostDB:ENSRNOG00000031814; -. DR eggNOG; KOG3511; Eukaryota. DR HOGENOM; CLU_013596_0_0_1; -. DR InParanoid; O54861; -. DR OrthoDB; 5840at2759; -. DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis. DR PRO; PR:O54861; -. DR Proteomes; UP000002494; Chromosome 2. DR Bgee; ENSRNOG00000031814; Expressed in frontal cortex and 19 other cell types or tissues. DR GO; GO:0009986; C:cell surface; ISO:RGD. DR GO; GO:0150053; C:cerebellar climbing fiber to Purkinje cell synapse; ISO:RGD. DR GO; GO:0005905; C:clathrin-coated pit; ISO:RGD. DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:RGD. DR GO; GO:0005829; C:cytosol; IEA:GOC. DR GO; GO:0030425; C:dendrite; IDA:RGD. DR GO; GO:0005769; C:early endosome; ISO:RGD. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0010008; C:endosome membrane; ISO:RGD. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005764; C:lysosome; ISS:UniProtKB. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0043025; C:neuronal cell body; IDA:RGD. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0030140; C:trans-Golgi network transport vesicle; ISO:RGD. DR GO; GO:0019899; F:enzyme binding; ISO:RGD. DR GO; GO:0016492; F:G protein-coupled neurotensin receptor activity; TAS:RGD. DR GO; GO:0048406; F:nerve growth factor binding; ISO:RGD. DR GO; GO:0010465; F:nerve growth factor receptor activity; ISO:RGD. DR GO; GO:0030379; F:neurotensin receptor activity, non-G protein-coupled; ISO:RGD. DR GO; GO:1905394; F:retromer complex binding; ISO:RGD. DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB. DR GO; GO:0008333; P:endosome to lysosome transport; ISO:RGD. DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; ISO:RGD. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; ISO:RGD. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD. DR GO; GO:0046323; P:glucose import; ISO:RGD. DR GO; GO:0006895; P:Golgi to endosome transport; ISO:RGD. DR GO; GO:0090160; P:Golgi to lysosome transport; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; NAS:RGD. DR GO; GO:0099558; P:maintenance of synapse structure; ISO:RGD. DR GO; GO:0014902; P:myotube differentiation; ISO:RGD. DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD. DR GO; GO:0007218; P:neuropeptide signaling pathway; ISO:RGD. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; ISO:RGD. DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW. DR GO; GO:0048227; P:plasma membrane to endosome transport; ISO:RGD. DR GO; GO:1904037; P:positive regulation of epithelial cell apoptotic process; IMP:RGD. DR GO; GO:0006622; P:protein targeting to lysosome; ISO:RGD. DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD. DR GO; GO:0032868; P:response to insulin; ISO:RGD. DR GO; GO:0016050; P:vesicle organization; ISO:RGD. DR Gene3D; 2.10.70.80; -; 1. DR Gene3D; 3.30.60.270; -; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR031777; Sortilin_C. DR InterPro; IPR031778; Sortilin_N. DR InterPro; IPR006581; VPS10. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR PANTHER; PTHR12106:SF23; SORTILIN; 1. DR PANTHER; PTHR12106; SORTILIN RELATED; 1. DR Pfam; PF15902; Sortilin-Vps10; 1. DR Pfam; PF15901; Sortilin_C; 1. DR SMART; SM00602; VPS10; 1. DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2. DR Genevisible; O54861; RN. PE 1: Evidence at protein level; KW Cell membrane; Cleavage on pair of basic residues; Developmental protein; KW Differentiation; Direct protein sequencing; Disulfide bond; Endocytosis; KW Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; KW Lipoprotein; Lysosome; Membrane; Nucleus; Osteogenesis; Palmitate; KW Phosphoprotein; Receptor; Reference proteome; Repeat; Signal; KW Transmembrane; Transmembrane helix; Transport. FT SIGNAL 1..31 FT /evidence="ECO:0000269|PubMed:26479776" FT PROPEP 32..73 FT /note="Removed in mature form" FT /evidence="ECO:0000269|PubMed:26479776" FT /id="PRO_0000436378" FT CHAIN 74..825 FT /note="Sortilin" FT /id="PRO_0000045158" FT TOPO_DOM 74..754 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 755..775 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 776..825 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REPEAT 143..154 FT /note="BNR 1" FT REPEAT 196..207 FT /note="BNR 2" FT REPEAT 238..249 FT /note="BNR 3" FT REPEAT 285..296 FT /note="BNR 4" FT REPEAT 326..337 FT /note="BNR 5" FT REPEAT 375..386 FT /note="BNR 6" FT REPEAT 426..437 FT /note="BNR 7" FT REPEAT 504..515 FT /note="BNR 8" FT REPEAT 546..557 FT /note="BNR 9" FT REGION 48..59 FT /note="Intrachain binding of the propeptide and the FT extracellular domain" FT /evidence="ECO:0000250" FT REGION 610..754 FT /note="Interactions with LRPAP1 and NGFB" FT /evidence="ECO:0000250" FT REGION 777..825 FT /note="Golgi to endosome transport and interactions with FT GGA1 and GGA2" FT /evidence="ECO:0000250" FT MOTIF 785..790 FT /note="Endocytosis signal" FT /evidence="ECO:0000255" FT MOTIF 820..824 FT /note="DXXLL motif involved in the interaction with GGA1" FT /evidence="ECO:0000250|UniProtKB:Q99523" FT MOD_RES 809 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99523" FT MOD_RES 813 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99523" FT MOD_RES 819 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:22673903" FT LIPID 781 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250|UniProtKB:Q99523" FT CARBOHYD 96 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 160 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 272 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 404 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007744|PubMed:24090084" FT CARBOHYD 580 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 682 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 84..554 FT /evidence="ECO:0000250" FT DISULFID 255..275 FT /evidence="ECO:0000250" FT DISULFID 446..456 FT /evidence="ECO:0000250" FT DISULFID 610..649 FT /evidence="ECO:0000250" FT DISULFID 632..664 FT /evidence="ECO:0000250" FT DISULFID 666..721 FT /evidence="ECO:0000250" FT DISULFID 673..686 FT /evidence="ECO:0000250" FT DISULFID 700..738 FT /evidence="ECO:0000250" FT CONFLICT 91 FT /note="I -> V (in Ref. 2; AAC02932)" FT /evidence="ECO:0000305" FT CONFLICT 276..277 FT /note="KA -> T (in Ref. 3; AAB81864)" FT /evidence="ECO:0000305" FT CONFLICT 433 FT /note="G -> R (in Ref. 3; AAB81864)" FT /evidence="ECO:0000305" FT CONFLICT 507 FT /note="D -> Y (in Ref. 2; AAC02932)" FT /evidence="ECO:0000305" FT CONFLICT 659 FT /note="K -> Q (in Ref. 3; AA sequence)" FT /evidence="ECO:0000305" SQ SEQUENCE 825 AA; 91169 MW; 060B43A54993EF06 CRC64; MERPRGAADG LLRWPLGLLL LLQLLPPAAV GQDRLDAPPP PAPPLLRWAG PVGVSWGLRA AAPGGPVPRA GRWRRGAPAE DQDCGRLPDF IAKLTNNTHQ HVFDDLSGSV SLSWVGDSTG VILVLTTFQV PLVIVSFGQS KLYRSEDYGK NFKDITNLIN NTFIRTEFGM AIGPENSGKV ILTAEVSGGS RGGRVFRSSD FAKNFVQTDL PFHPLTQMMY SPQNSDYLLA LSTENGLWVS KNFGEKWEEI HKAVCLAKWG PNNIIFFTTH VNGSCKADLG ALELWRTSDL GKTFKTIGVK IYSFGLGGRF LFASVMADKD TTRRIHVSTD QGDTWSMAQL PSVGQEQFYS ILAANDDMVF MHVDEPGDTG FGTIFTSDDR GIVYSKSLDR HLYTTTGGET DFTNVTSLRG VYITSTLSED NSIQSMITFD QGGRWEHLQK PENSKCDATA KNKNECSLHI HASYSISQKL NVPMAPLSEP NAVGIVIAHG SVGDAISVMV PDVYISDDGG YSWAKMLEGP HYYTILDSGG IIVAIEHSNR PINVIKFSTD EGQCWQSYVF SQEPVYFTGL ASEPGARSMN ISIWGFTESF LTRQWVSYTI DFKDILERNC EENDYTTWLA HSTDPGDYKD GCILGYKEQF LRLRKSSVCQ NGRDYVVAKQ PSICPCSLED FLCDFGYFRP ENASECVEQP ELKGHELEFC LYGKEEHLTT NGYRKIPGDR CQGGMNPARE VKDLKKKCTS NFLNPKKQNS KSSSVPIILA IVGLMLVTVV AGVLIVKKYV CGGRFLVHRY SVLQQHAEAD GVEALDTASH AKSGYHDDSD EDLLE //