SORT_RAT
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 03-AUG-2022, entry version 170.
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}.
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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 GlyGen; O54861; 6 sites, 3 N-linked glycans (1 site).
DR iPTMnet; O54861; -.
DR PhosphoSitePlus; O54861; -.
DR SwissPalm; O54861; -.
DR PaxDb; O54861; -.
DR PRIDE; O54861; -.
DR GeneID; 83576; -.
DR KEGG; rno:83576; -.
DR UCSC; RGD:619999; rat.
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 OMA; FAPFYSV; -.
DR OrthoDB; 1046610at2759; -.
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 tissues.
DR Genevisible; O54861; RN.
DR GO; GO:0009986; C:cell surface; 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:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
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; IDA: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:0014902; P:myotube differentiation; ISO:RGD.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; ISO:RGD.
DR GO; GO:0051005; P:negative regulation of lipoprotein lipase activity; 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:0006892; P:post-Golgi vesicle-mediated transport; IBA:GO_Central.
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; 2.130.10.10; -; 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 Pfam; PF15902; Sortilin-Vps10; 1.
DR Pfam; PF15901; Sortilin_C; 1.
DR SMART; SM00602; VPS10; 1.
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
