[1]	NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, INTERACTION WITH LRPAP1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND GLYCOSYLATION. TISSUE=T-cell; DOI=10.1074/jbc.272.6.3599; PubMed=9013611 [NCBI, ExPASy, EBI, Israel, Japan] Petersen C.M., Nielsen M.S., Nykjaer A., Jacobsen L., Tommerup N., Rasmussen H.H., Roeigaard H., Gliemann J., Madsen P., Moestrup S.K.; "Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography."; J. Biol. Chem. 272:3599-3605(1997).
[2]	SEQUENCE REVISION. Madsen P.; Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan] Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; "The DNA sequence and biological annotation of human chromosome 1."; Nature 441:315-321(2006).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Muscle; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	PROTEIN SEQUENCE OF 78-100, AND IDENTIFICATION AS A NEUROTENSIN RECEPTOR. TISSUE=Brain; DOI=10.1074/jbc.273.41.26273; PubMed=9756851 [NCBI, ExPASy, EBI, Israel, Japan] Mazella J., Zsurger N., Navarro V., Chabry J., Kaghad M., Caput D., Ferrara P., Vita M., Gully D., Maffrand J.-P., Vincent J.-P.; "The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor."; J. Biol. Chem. 273:26273-26276(1998).
[6]	PARTIAL PROTEIN SEQUENCE, INTERACTION WITH LRPAP1, MUTAGENESIS OF 74-ARG--ARG-77 AND 76-ARG-ARG-77, CLEAVAGE BY FURIN, AND GLYCOSYLATION. DOI=10.1093/emboj/18.3.595; PubMed=9927419 [NCBI, ExPASy, EBI, Israel, Japan] Petersen C.M., Nielsen M.S., Jacobsen C., Tauris J., Jacobsen L., Gliemann J., Moestrup S.K., Madsen P.; "Propeptide cleavage conditions sortilin/neurotensin receptor-3 for ligand binding."; EMBO J. 18:595-604(1999).
[7]	INTERACTION WITH LRPAP1. DOI=10.1016/S0014-5793(98)00559-6; PubMed=9657377 [NCBI, ExPASy, EBI, Israel, Japan] Tauris J., Ellgaard L., Jacobsen C., Nielsen M.S., Madsen P., Thoegersen H.C., Gliemann J., Petersen C.M., Moestrup S.K.; "The carboxy-terminal domain of the receptor-associated protein binds to the Vps10p domain of sortilin."; FEBS Lett. 429:27-30(1998).
[8]	FUNCTION. DOI=10.1074/jbc.274.13.8832; PubMed=10085125 [NCBI, ExPASy, EBI, Israel, Japan] Nielsen M.S., Jacobsen C., Olivecrona G., Gliemann J., Petersen C.M.; "Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase."; J. Biol. Chem. 274:8832-8836(1999).
[9]	FUNCTION, INTERACTION WITH GGA2, AND MUTAGENESIS OF TYR-792; LEU-795 AND 829-LEU-LEU-830. DOI=10.1093/emboj/20.9.2180; PubMed=11331584 [NCBI, ExPASy, EBI, Israel, Japan] Nielsen M.S., Madsen P., Christensen E.I., Nykjaer A., Gliemann J., Kasper D., Pohlmann R., Petersen C.M.; "The sortilin cytoplasmic tail conveys Golgi-endosome transport and binds the VHS domain of the GGA2 sorting protein."; EMBO J. 20:2180-2190(2001).
[10]	FUNCTION, INTERACTION WITH GGA1 AND GGA2, AND MUTAGENESIS OF 823-ASP-ASP-824; SER-825; 826-ASP--ASP-828 AND 829-LEU-LEU-830. DOI=10.1074/jbc.C100218200; PubMed=11390366 [NCBI, ExPASy, EBI, Israel, Japan] Takatsu H., Katoh Y., Shiba Y., Nakayama K.; "Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains."; J. Biol. Chem. 276:28541-28545(2001).
[11]	CLEAVAGE OF THE EXTRACELLULAR DOMAIN. DOI=10.1016/S0006-291X(02)02564-0; PubMed=12419319 [NCBI, ExPASy, EBI, Israel, Japan] Navarro V., Vincent J.-P., Mazella J.; "Shedding of the luminal domain of the neurotensin receptor-3/sortilin in the HT29 cell line."; Biochem. Biophys. Res. Commun. 298:760-764(2002).
[12]	FUNCTION, AND INDUCTION. DOI=10.1002/jcp.10151; PubMed=12209882 [NCBI, ExPASy, EBI, Israel, Japan] Maeda S., Nobukuni T., Shimo-Onoda K., Hayashi K., Yone K., Komiya S., Inoue I.; "Sortilin is upregulated during osteoblastic differentiation of mesenchymal stem cells and promotes extracellular matrix mineralization."; J. Cell. Physiol. 193:73-79(2002).
[13]	INTERACTION WITH GGA1. DOI=10.1038/415937a; PubMed=11859376 [NCBI, ExPASy, EBI, Israel, Japan] Shiba T., Takatsu H., Nogi T., Matsugaki N., Kawasaki M., Igarashi N., Suzuki M., Kato R., Earnest T., Nakayama K., Wakatsuki S.; "Structural basis for recognition of acidic-cluster dileucine sequence by GGA1."; Nature 415:937-941(2002).
[14]	FUNCTION, INTERACTION WITH GM2A AND PSAP, AND SUBCELLULAR LOCATION. DOI=10.1093/emboj/cdg629; PubMed=14657016 [NCBI, ExPASy, EBI, Israel, Japan] Lefrancois S., Zeng J., Hassan A.J., Canuel M., Morales C.R.; "The lysosomal trafficking of sphingolipid activator proteins (SAPs) is mediated by sortilin."; EMBO J. 22:6430-6437(2003).
[15]	ERRATUM. Lefrancois S., Zeng J., Hassan A.J., Canuel M., Morales C.R.; EMBO J. 23:1680-1680(2004).
[16]	FUNCTION, AND SUBCELLULAR LOCATION. PubMed=12598608 [NCBI, ExPASy, EBI, Israel, Japan] Martin S., Vincent J.-P., Mazella J.; "Involvement of the neurotensin receptor-3 in the neurotensin-induced migration of human microglia."; J. Neurosci. 23:1198-1205(2003).
[17]	FUNCTION, AND SUBCELLULAR LOCATION. DOI=10.1016/j.biocel.2004.04.013; PubMed=15313463 [NCBI, ExPASy, EBI, Israel, Japan] Morinville A., Martin S., Lavallee M., Vincent J.-P., Beaudet A., Mazella J.; "Internalization and trafficking of neurotensin via NTS3 receptors in HT29 cells."; Int. J. Biochem. Cell Biol. 36:2153-2168(2004).
[18]	INTERACTION WITH LRPAP1 AND NGFB, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND DISULFIDE BONDS. DOI=10.1074/jbc.M408873200; PubMed=15364913 [NCBI, ExPASy, EBI, Israel, Japan] Westergaard U.B., Soerensen E.S., Hermey G., Nielsen M.S., Nykjaer A., Kirkegaard K., Jacobsen C., Gliemann J., Madsen P., Petersen C.M.; "Functional organization of the sortilin Vps10p domain."; J. Biol. Chem. 279:50221-50229(2004).
[19]	FUNCTION, AND INTERACTION WITH NGFB AND NGFR. DOI=10.1038/nature02319; PubMed=14985763 [NCBI, ExPASy, EBI, Israel, Japan] Nykjaer A., Lee R., Teng K.K., Jansen P., Madsen P., Nielsen M.S., Jacobsen C., Kliemannel M., Schwarz E., Willnow T.E., Hempstead B.L., Petersen C.M.; "Sortilin is essential for proNGF-induced neuronal cell death."; Nature 427:843-848(2004).
[20]	FUNCTION. DOI=10.1523/JNEUROSCI.5123-04.2005; PubMed=15930396 [NCBI, ExPASy, EBI, Israel, Japan] Teng H.K., Teng K.K., Lee R., Wright S., Tevar S., Almeida R.D., Kermani P., Torkin R., Chen Z.-Y., Lee F.S., Kraemer R.T., Nykjaer A., Hempstead B.L.; "ProBDNF induces neuronal apoptosis via activation of a receptor complex of p75NTR and sortilin."; J. Neurosci. 25:5455-5463(2005).
[21]	FUNCTION, AND INTERACTION WITH BDNF. DOI=10.1523/JNEUROSCI.1017-05.2005; PubMed=15987945 [NCBI, ExPASy, EBI, Israel, Japan] Chen Z.-Y., Ieraci A., Teng H., Dall H., Meng C.-X., Herrera D.G., Nykjaer A., Hempstead B.L., Lee F.S.; "Sortilin controls intracellular sorting of brain-derived neurotrophic factor to the regulated secretory pathway."; J. Neurosci. 25:6156-6166(2005).
[22]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-162, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1074/mcp.M500324-MCP200; PubMed=16263699 [NCBI, ExPASy, EBI, Israel, Japan] Lewandrowski U., Moebius J., Walter U., Sickmann A.; "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."; Mol. Cell. Proteomics 5:226-233(2006).
[23]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-825, AND MASS SPECTROMETRY. TISSUE=Platelet; DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan] Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.; "Phosphoproteome of resting human platelets."; J. Proteome Res. 7:526-534(2008).
[24]	IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. Colinge J., Superti-Furga G., Bennett K.L.; Submitted (OCT-2008) to UniProtKB.

Comments

FUNCTION: Functions as a sorting receptor in the Golgi compartment and as a clearance receptor on the cell surface. Required for protein transport from the Golgi apparatus to the lysosomes by a pathway that is independent of the mannose-6-phosphate receptor (M6PR). Also required for protein transport from the Golgi apparatus to the endosomes. Promotes neuronal apoptosis by mediating endocytosis of the proapoptotic precursor forms of BDNF (proBDNF) and NGFB (proNGFB). Also acts as a receptor for neurotensin. May promote mineralization of the extracellular matrix during osteogenic differentiation by scavenging extracellular LPL. Probably required in adipocytes for the formation of specialized storage vesicles containing the glucose transporter SLC2A4/GLUT4 (GLUT4 storage vesicles, or GSVs). These vesicles provide a stable pool of SLC2A4 and confer increased responsiveness to insulin. May also mediate transport from the endoplasmic reticulum to the Golgi.
SUBUNIT: Interacts with LPL and SLC2A4 (By similarity). Interacts with the cytosolic adapter proteins GGA1 and GGA2. Interacts with numerous ligands including the receptor-associated protein LRPAP1/RAP, GM2A and PSAP. Forms a complex with NGFR which binds specifically to the precursor forms of NGFB (proNGFB) and BDNF (proBDNF).
INTERACTION:
P24941:CDK2; NbExp=1; IntAct=EBI-1057058, EBI-375096;
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. Endoplasmic reticulum membrane; Single-pass type I membrane protein (Potential). Endosome membrane; Single-pass type I membrane protein (Potential). Golgi apparatus, Golgi stack membrane; Single-pass type I membrane protein (Potential). Lysosome membrane; Single-pass type I membrane protein (Potential). Nucleus membrane; Single-pass type I membrane protein (Potential). Cell membrane; Single-pass type I membrane protein; Extracellular side. Lysosome membrane; Single-pass type I membrane protein (Potential). Note=Localized to membranes of the endoplasmic reticulum, endosomes, Golgi stack, lysosomes and nucleus. A small fraction of the protein is also localized to the plasma membrane. May also be found in SLC2A4/GLUT4 storage vesicles (GSVs) in adipocytes. Localization to the plasma membrane in adipocytes may be enhanced by insulin.
TISSUE SPECIFICITY: Expressed at high levels in brain, spinal cord, heart, skeletal muscle, thyroid, placenta and testis. Expressed at lower levels in lymphoid organs, kidney, colon and liver.
INDUCTION: During osteoblast differentiation.
DOMAIN: The N-terminal propeptide may facilitate precursor transport within the Golgi stack. Intrachain binding of the N-terminal propeptide and the extracellular domain may also inhibit premature ligand binding.
DOMAIN: The extracellular domain may be shed following protease cleavage in some cell types.
PTM: The N-terminal propeptide is cleaved by furin and possibly other homologous proteases.
PTM: Contains 8 intrachain disulfide bonds.
PTM: N-glycosylated.
SIMILARITY: Contains 9 BNR repeats.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X98248; CAA66904.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL390252; CAI13180.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC023542; AAH23542.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00217882; -.

NP_002950.3; -.

3D structure databases

PDB

3F6K; X-ray; 2.00 A; A=78-756.

[ExPASy / RCSB / EBI]

PDBsum

3F6K; -.

ModBase

Q99523.

Protein-protein interaction databases

IntAct

Q99523; 1.

PTM databases

PhosphoSite

Q99523; -.

Enzyme and pathway databases

Pathway_Interaction_DB

p75ntrpathway; p75(NTR)-mediated signaling.

Organism-specific databases

GC01M109653; -.

HIX0000847; -.

HGNC:11186; SORT1.

HPA006889; -.

602458; gene. [NCBI / EBI]

PharmGKB

PA36023; -.

Gene expression databases

Q99523; -.

Q99523; -.

HS_SORT1; -.

ENSG00000134243; Homo sapiens.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0030136;	Cellular component: clathrin-coated vesicle (inferred from direct assay from UniProtKB).
GO:0005905;	Cellular component: coated pit (inferred from direct assay from UniProtKB).
GO:0005769;	Cellular component: early endosome (inferred from direct assay from UniProtKB).
GO:0005789;	Cellular component: endoplasmic reticulum membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0010008;	Cellular component: endosome membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0032580;	Cellular component: Golgi cisterna membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from direct assay from UniProtKB).
GO:0005765;	Cellular component: lysosomal membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005792;	Cellular component: microsome (inferred from direct assay from UniProtKB).
GO:0031965;	Cellular component: nuclear membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0048471;	Cellular component: perinuclear region of cytoplasm (inferred from direct assay from UniProtKB).
GO:0019899;	Molecular function: enzyme binding (inferred from physical interaction from UniProtKB).
GO:0048406;	Molecular function: nerve growth factor binding (inferred from physical interaction from UniProtKB).
GO:0010465;	Molecular function: nerve growth factor receptor activity (inferred from direct assay from UniProtKB).
GO:0030379;	Molecular function: neurotensin receptor activity, non-G-protein coupled (inferred from direct assay from UniProtKB).
GO:0006897;	Biological process: endocytosis (inferred from direct assay from UniProtKB).
GO:0008333;	Biological process: endosome to lysosome transport (inferred from direct assay from UniProtKB).
GO:0032509;	Biological process: endosome transport via multivesicular body sorting pathway (inferred from direct assay from UniProtKB).
GO:0046323;	Biological process: glucose import (inferred from mutant phenotype from UniProtKB).
GO:0006895;	Biological process: Golgi to endosome transport (inferred from direct assay from UniProtKB).
GO:0008624;	Biological process: induction of apoptosis by extracellular signals (inferred from mutant phenotype from UniProtKB).
GO:0014902;	Biological process: myotube differentiation (inferred from mutant phenotype from UniProtKB).
GO:0043066;	Biological process: negative regulation of apoptosis (inferred from direct assay from UniProtKB).
GO:0051005;	Biological process: negative regulation of lipoprotein lipase activity (inferred from direct assay from UniProtKB).
GO:0048011;	Biological process: nerve growth factor receptor signaling pathway (inferred from mutant phenotype from UniProtKB).
GO:0007218;	Biological process: neuropeptide signaling pathway (inferred from direct assay from UniProtKB).
GO:0001503;	Biological process: ossification (inferred from electronic annotation from UniProtKB-KW).
GO:0048227;	Biological process: plasma membrane to endosome transport (inferred from direct assay from UniProtKB).
GO:0010468;	Biological process: regulation of gene expression (inferred from mutant phenotype from UniProtKB).
GO:0032868;	Biological process: response to insulin stimulus (inferred from mutant phenotype from UniProtKB).
GO:0016050;	Biological process: vesicle organization (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR006581; VPS10.
Graphical view of domain structure.

SMART

SM00602; VPS10; 1.
SMART graphical view of domain structure.

Proteomic databases

PRIDE

Q99523; -.

Genome annotation databases

Ensembl

ENSG00000134243; Homo sapiens. [Contig view]

GeneID

6272; -.

KEGG

hsa:6272; -.

NMPDR

fig|9606.3.peg.1632; -.

Phylogenomic databases

HOGENOM

Q99523; -.

HOVERGEN

Q99523; -.

OMA

Q99523; LTQMMYS.

Other

24343; -.

SORT1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Cell membrane; Cleavage on pair of basic residues; Developmental protein; Differentiation; Direct protein sequencing; Disulfide bond; Endocytosis; Endoplasmic reticulum; Endosome; Glycoprotein; Golgi apparatus; Lysosome; Membrane; Nucleus; Osteogenesis; Phosphoprotein; Polymorphism; Receptor; Repeat; Signal; Transmembrane; Transport.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 33`	`33`	`Potential.`
`PROPEP`	`34 77`	`44`	`Removed in mature form.`	`PRO_0000033162`
`CHAIN`	`78 831`	`754`	`Sortilin.`	`PRO_0000033163`
`TOPO_DOM`	`78 755`	`678`	`Extracellular (Potential).`
`TRANSMEM`	`756 778`	`23`	`Potential.`
`TOPO_DOM`	`779 831`	`53`	`Cytoplasmic (Potential).`
`REPEAT`	`145 156`	`12`	`BNR 1.`
`REPEAT`	`198 209`	`12`	`BNR 2.`
`REPEAT`	`240 251`	`12`	`BNR 3.`
`REPEAT`	`287 298`	`12`	`BNR 4.`
`REPEAT`	`328 339`	`12`	`BNR 5.`
`REPEAT`	`377 388`	`12`	`BNR 6.`
`REPEAT`	`428 439`	`12`	`BNR 7.`
`REPEAT`	`506 517`	`12`	`BNR 8.`
`REPEAT`	`548 559`	`12`	`BNR 9.`
`REGION`	`50 61`	`12`	`Intrachain binding of the propeptide and the extracellular domain.`
`REGION`	`612 756`	`145`	`Interactions with LRPAP1 and NGFB.`
`REGION`	`779 831`	`53`	`Golgi to endosome transport and interactions with GGA1 and GGA2.`
`MOTIF`	`787 792`	`6`	`Endocytosis signal (Probable).`
`MOD_RES`	`825 825`		`Phosphoserine.`
`CARBOHYD`	`98 98`		`N-linked (GlcNAc...) (Probable).`
`CARBOHYD`	`162 162`		`N-linked (GlcNAc...).`
`CARBOHYD`	`274 274`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`406 406`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`582 582`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`684 684`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`86 556`
`DISULFID`	`257 277`
`DISULFID`	`448 458`
`DISULFID`	`612 651`
`DISULFID`	`634 666`
`DISULFID`	`668 723`
`DISULFID`	`675 688`
`DISULFID`	`702 740`
`VARIANT`	`358 358`	`1`	`D -> Y (in dbSNP:rs2228605 [NCBI]).`	`VAR_053681`
`MUTAGEN`	`74 77`		`RWRR->GWRA: Abrogates propeptide cleavage.`
`MUTAGEN`	`76 77`		`RR->GG: Abrogates propeptide cleavage.`
`MUTAGEN`	`792 792`		`Y->A: Reduces endocytosis and Golgi to endosome sorting; when associated with A-795.`
`MUTAGEN`	`795 795`		`L->A: Reduces endocytosis and Golgi to endosome sorting; when associated with A-792.`
`MUTAGEN`	`823 824`		`DD->NN: Reduces interaction with GGA1.`
`MUTAGEN`	`825 825`		`S->A: Reduces interaction with GGA1.`
`MUTAGEN`	`826 828`		`DED->NQN: Abrogates interaction with GGA1 and impairs localization to the Golgi.`
`MUTAGEN`	`829 830`		`LL->AA: Abrogates interaction with GGA1 and impairs localization to the Golgi.`
`MUTAGEN`	`829 830`		`Missing: Abrogates interaction with GGA2. Reduces endocytosis and Golgi to endosome sorting; when associated with A-792 and A-795.`
`CONFLICT`	`650 650`		`V -> M (in Ref. 1; CAA66904).`

Sequence information

Length: 831 AA [This is the length of the unprocessed precursor]

Molecular weight: 92068 Da [This is the MW of the unprocessed precursor]

CRC64: 91F96A3035A4B43A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MERPWGAADG LSRWPHGLGL LLLLQLLPPS TLSQDRLDAP PPPAAPLPRW SGPIGVSWGL 

        70         80         90        100        110        120 
RAAAAGGAFP RGGRWRRSAP GEDEECGRVR DFVAKLANNT HQHVFDDLRG SVSLSWVGDS 

       130        140        150        160        170        180 
TGVILVLTTF HVPLVIMTFG QSKLYRSEDY GKNFKDITDL INNTFIRTEF GMAIGPENSG 

       190        200        210        220        230        240 
KVVLTAEVSG GSRGGRIFRS SDFAKNFVQT DLPFHPLTQM MYSPQNSDYL LALSTENGLW 

       250        260        270        280        290        300 
VSKNFGGKWE EIHKAVCLAK WGSDNTIFFT TYANGSCKAD LGALELWRTS DLGKSFKTIG 

       310        320        330        340        350        360 
VKIYSFGLGG RFLFASVMAD KDTTRRIHVS TDQGDTWSMA QLPSVGQEQF YSILAANDDM 

       370        380        390        400        410        420 
VFMHVDEPGD TGFGTIFTSD DRGIVYSKSL DRHLYTTTGG ETDFTNVTSL RGVYITSVLS 

       430        440        450        460        470        480 
EDNSIQTMIT FDQGGRWTHL RKPENSECDA TAKNKNECSL HIHASYSISQ KLNVPMAPLS 

       490        500        510        520        530        540 
EPNAVGIVIA HGSVGDAISV MVPDVYISDD GGYSWTKMLE GPHYYTILDS GGIIVAIEHS 

       550        560        570        580        590        600 
SRPINVIKFS TDEGQCWQTY TFTRDPIYFT GLASEPGARS MNISIWGFTE SFLTSQWVSY 

       610        620        630        640        650        660 
TIDFKDILER NCEEKDYTIW LAHSTDPEDY EDGCILGYKE QFLRLRKSSV CQNGRDYVVT 

       670        680        690        700        710        720 
KQPSICLCSL EDFLCDFGYY RPENDSKCVE QPELKGHDLE FCLYGREEHL TTNGYRKIPG 

       730        740        750        760        770        780 
DKCQGGVNPV REVKDLKKKC TSNFLSPEKQ NSKSNSVPII LAIVGLMLVT VVAGVLIVKK 

       790        800        810        820        830 
YVCGGRFLVH RYSVLQQHAE ANGVDGVDAL DTASHTNKSG YHDDSDEDLL E

Q99523 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools