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Database: UniProt
Entry: Q92673
LinkDB: Q92673
Original site: Q92673 
ID   SORL_HUMAN              Reviewed;        2214 AA.
AC   Q92673; B2RNX7; Q92856;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   05-JUN-2019, entry version 196.
DE   RecName: Full=Sortilin-related receptor;
DE   AltName: Full=Low-density lipoprotein receptor relative with 11 ligand-binding repeats;
DE            Short=LDLR relative with 11 ligand-binding repeats;
DE            Short=LR11;
DE   AltName: Full=SorLA-1;
DE   AltName: Full=Sorting protein-related receptor containing LDLR class A repeats;
DE            Short=SorLA;
DE   Flags: Precursor;
GN   Name=SORL1; Synonyms=C11orf32;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS GLU-1074 AND ILE-1967.
RC   TISSUE=Brain;
RX   PubMed=9157966; DOI=10.1161/01.ATV.17.5.996;
RA   Morwald S., Yamazaki H., Bujo H., Kusunoki J., Kanaki T., Seimiya K.,
RA   Morisaki N., Nimpf J., Schneider W.J., Saito Y.;
RT   "A novel mosaic protein containing LDL receptor elements is highly
RT   conserved in humans and chickens.";
RL   Arterioscler. Thromb. Vasc. Biol. 17:996-1002(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, PARTIAL
RP   PROTEIN SEQUENCE, AND VARIANTS GLU-1074 AND ILE-1967.
RC   TISSUE=Brain, and T-cell;
RX   PubMed=8940146; DOI=10.1074/jbc.271.49.31379;
RA   Jacobsen L., Madsen P., Moestrup S.K., Lund A.H., Tommerup N.,
RA   Nykjaer A., Sottrup-Jensen L., Gliemann J., Petersen C.M.;
RT   "Molecular characterization of a novel human hybrid-type receptor that
RT   binds the alpha2-macroglobulin receptor-associated protein.";
RL   J. Biol. Chem. 271:31379-31383(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
RA   Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
RA   FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
RA   Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
RA   Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
RA   Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLU-1074
RP   AND ILE-1967.
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLU-1074 AND
RP   ILE-1967.
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PLAUR.
RX   PubMed=14764453; DOI=10.1161/01.RES.0000120862.79154.0F;
RA   Zhu Y., Bujo H., Yamazaki H., Ohwaki K., Jiang M., Hirayama S.,
RA   Kanaki T., Shibasaki M., Takahashi K., Schneider W.J., Saito Y.;
RT   "LR11, an LDL receptor gene family member, is a novel regulator of
RT   smooth muscle cell migration.";
RL   Circ. Res. 94:752-758(2004).
RN   [7]
RP   FUNCTION IN APP TRAFFICKING, SUBCELLULAR LOCATION, INTERACTION WITH
RP   APP, AND TISSUE SPECIFICITY.
RX   PubMed=16174740; DOI=10.1073/pnas.0503689102;
RA   Andersen O.M., Reiche J., Schmidt V., Gotthardt M., Spoelgen R.,
RA   Behlke J., von Arnim C.A., Breiderhoff T., Jansen P., Wu X.,
RA   Bales K.R., Cappai R., Masters C.L., Gliemann J., Mufson E.J.,
RA   Hyman B.T., Paul S.M., Nykjaer A., Willnow T.E.;
RT   "Neuronal sorting protein-related receptor sorLA/LR11 regulates
RT   processing of the amyloid precursor protein.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13461-13466(2005).
RN   [8]
RP   LACK OF ASSOCIATION WITH SUSCEPTIBILITY TO LATE-ONSET ALZHEIMER
RP   DISEASE.
RX   PubMed=18562096; DOI=10.1016/j.neulet.2008.05.082;
RA   Minster R.L., DeKosky S.T., Kamboh M.I.;
RT   "No association of SORL1 SNPs with Alzheimer's disease.";
RL   Neurosci. Lett. 440:190-192(2008).
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-99; ASN-1733; ASN-2010;
RP   ASN-2076 AND ASN-2092.
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
RT   multiple enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [11]
RP   INVOLVEMENT IN AD.
RX   PubMed=21220680; DOI=10.1001/archneurol.2010.346;
RG   Genetic and Environmental Risk in Alzheimer Disease 1 Consortium;
RA   Reitz C., Cheng R., Rogaeva E., Lee J.H., Tokuhiro S., Zou F.,
RA   Bettens K., Sleegers K., Tan E.K., Kimura R., Shibata N., Arai H.,
RA   Kamboh M.I., Prince J.A., Maier W., Riemenschneider M., Owen M.,
RA   Harold D., Hollingworth P., Cellini E., Sorbi S., Nacmias B.,
RA   Takeda M., Pericak-Vance M.A., Haines J.L., Younkin S., Williams J.,
RA   van Broeckhoven C., Farrer L.A., St George-Hyslop P.H., Mayeux R.;
RT   "Meta-analysis of the association between variants in SORL1 and
RT   Alzheimer disease.";
RL   Arch. Neurol. 68:99-106(2011).
RN   [12]
RP   PHOSPHORYLATION AT SER-2206, AND INTERACTION WITH ROCK2.
RX   PubMed=21147781; DOI=10.1074/jbc.M110.167239;
RA   Herskowitz J.H., Seyfried N.T., Gearing M., Kahn R.A., Peng J.,
RA   Levey A.I., Lah J.J.;
RT   "Rho kinase II phosphorylation of the lipoprotein receptor LR11/SORLA
RT   alters amyloid-beta production.";
RL   J. Biol. Chem. 286:6117-6127(2011).
RN   [13]
RP   INVOLVEMENT IN AD.
RX   PubMed=23565137; DOI=10.1371/journal.pone.0058618;
RG   Alzheimer Disease Genetics Consortium;
RA   Miyashita A., Koike A., Jun G., Wang L.S., Takahashi S., Matsubara E.,
RA   Kawarabayashi T., Shoji M., Tomita N., Arai H., Asada T., Harigaya Y.,
RA   Ikeda M., Amari M., Hanyu H., Higuchi S., Ikeuchi T., Nishizawa M.,
RA   Suga M., Kawase Y., Akatsu H., Kosaka K., Yamamoto T., Imagawa M.,
RA   Hamaguchi T., Yamada M., Moriaha T., Takeda M., Takao T., Nakata K.,
RA   Fujisawa Y., Sasaki K., Watanabe K., Nakashima K., Urakami K.,
RA   Ooya T., Takahashi M., Yuzuriha T., Serikawa K., Yoshimoto S.,
RA   Nakagawa R., Kim J.W., Ki C.S., Won H.H., Na D.L., Seo S.W.,
RA   Mook-Jung I., St George-Hyslop P., Mayeux R., Haines J.L.,
RA   Pericak-Vance M.A., Yoshida M., Nishida N., Tokunaga K., Yamamoto K.,
RA   Tsuji S., Kanazawa I., Ihara Y., Schellenberg G.D., Farrer L.A.,
RA   Kuwano R.;
RT   "SORL1 is genetically associated with late-onset Alzheimer's disease
RT   in Japanese, Koreans and Caucasians.";
RL   PLoS ONE 8:E58618-E58618(2013).
RN   [14]
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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [15]
RP   STRUCTURE BY NMR OF 1651-1745.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the second FN3 domain of human SORLA/LR11.";
RL   Submitted (OCT-2006) to the PDB data bank.
RN   [16]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2202-2214 IN COMPLEX WITH
RP   GGA1, AND INTERACTION WITH GGA1.
RX   PubMed=20015111; DOI=10.1111/j.1600-0854.2009.01017.x;
RA   Cramer J.F., Gustafsen C., Behrens M.A., Oliveira C.L., Pedersen J.S.,
RA   Madsen P., Petersen C.M., Thirup S.S.;
RT   "GGA autoinhibition revisited.";
RL   Traffic 11:259-273(2010).
RN   [17]
RP   VARIANTS [LARGE SCALE ANALYSIS] SER-120; LEU-1581 AND VAL-1972.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [18]
RP   POSSIBLE ASSOCIATION WITH SUSCEPTIBILITY TO LATE-ONSET ALZHEIMER
RP   DISEASE, AND VARIANT THR-528.
RX   PubMed=18407551; DOI=10.1002/humu.20725;
RA   Bettens K., Brouwers N., Engelborghs S., De Deyn P.P.,
RA   Van Broeckhoven C., Sleegers K.;
RT   "SORL1 is genetically associated with increased risk for late-onset
RT   Alzheimer disease in the Belgian population.";
RL   Hum. Mutat. 29:769-770(2008).
RN   [19]
RP   VARIANTS AD CYS-141; ARG-511; SER-924; SER-1358 AND ASP-1681.
RX   PubMed=22472873; DOI=10.1038/mp.2012.15;
RG   PHRC GMAJ Collaborators;
RA   Pottier C., Hannequin D., Coutant S., Rovelet-Lecrux A., Wallon D.,
RA   Rousseau S., Legallic S., Paquet C., Bombois S., Pariente J.,
RA   Thomas-Anterion C., Michon A., Croisile B., Etcharry-Bouyx F.,
RA   Berr C., Dartigues J.F., Amouyel P., Dauchel H.,
RA   Boutoleau-Bretonniere C., Thauvin C., Frebourg T., Lambert J.C.,
RA   Campion D.;
RT   "High frequency of potentially pathogenic SORL1 mutations in autosomal
RT   dominant early-onset Alzheimer disease.";
RL   Mol. Psychiatry 17:875-879(2012).
CC   -!- FUNCTION: Likely to be a multifunctional endocytic receptor, that
CC       may be implicated in the uptake of lipoproteins and of proteases.
CC       Binds LDL, the major cholesterol-carrying lipoprotein of plasma,
CC       and transports it into cells by endocytosis. Binds the receptor-
CC       associated protein (RAP). Could play a role in cell-cell
CC       interaction. Involved in APP trafficking to and from the Golgi
CC       apparatus. It probably acts as a sorting receptor that protects
CC       APP from trafficking to late endosome and from processing into
CC       amyloid beta, thereby reducing the burden of amyloidogenic peptide
CC       formation. Involved in the regulation of smooth muscle cells
CC       migration, probably through PLAUR binding and decreased
CC       internalization. {ECO:0000269|PubMed:14764453,
CC       ECO:0000269|PubMed:16174740}.
CC   -!- SUBUNIT: Interacts with GGA1 and ROCK2. Interacts with PLAUR.
CC       Interacts with APP. {ECO:0000269|PubMed:14764453,
CC       ECO:0000269|PubMed:16174740, ECO:0000269|PubMed:20015111,
CC       ECO:0000269|PubMed:21147781}.
CC   -!- INTERACTION:
CC       P05067:APP; NbExp=3; IntAct=EBI-1171329, EBI-2431589;
CC       P05067-4:APP; NbExp=7; IntAct=EBI-1171329, EBI-302641;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Golgi apparatus. Endosome.
CC       Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed mainly in brain, where it is most
CC       abundant in the cerebellum, cerebral cortex and the occipital
CC       pole; low expression in the putamen and the thalamus. Expression
CC       is significantly reduced in the frontal cortex of patients
CC       suffering from Alzheimer disease. According to PubMed:9157966,
CC       found in spinal cord, testis, liver, kidney and pancreas with
CC       detectable levels in placenta, lung and heart. According to
CC       PubMed:8940146, expressed in the prostate, ovary, thyroid and
CC       spleen, but not found in kidney, liver, lung, skeletal muscle,
CC       bone marrow and adrenals. {ECO:0000269|PubMed:16174740}.
CC   -!- PTM: The propeptide removed in the N-terminus may be cleaved by
CC       furin or homologous proteases.
CC   -!- DISEASE: Alzheimer disease (AD) [MIM:104300]: Alzheimer disease is
CC       a neurodegenerative disorder characterized by progressive
CC       dementia, loss of cognitive abilities, and deposition of fibrillar
CC       amyloid proteins as intraneuronal neurofibrillary tangles,
CC       extracellular amyloid plaques and vascular amyloid deposits. The
CC       major constituents of these plaques are neurotoxic amyloid-beta
CC       protein 40 and amyloid-beta protein 42, that are produced by the
CC       proteolysis of the transmembrane APP protein. The cytotoxic C-
CC       terminal fragments (CTFs) and the caspase-cleaved products, such
CC       as C31, are also implicated in neuronal death.
CC       {ECO:0000269|PubMed:21220680, ECO:0000269|PubMed:22472873,
CC       ECO:0000269|PubMed:23565137}. Note=The gene represented in this
CC       entry is involved in disease pathogenesis.
CC   -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORL1
CC       subfamily. {ECO:0000305}.
DR   EMBL; Y08110; CAA69325.1; -; mRNA.
DR   EMBL; U60975; AAC50891.2; -; mRNA.
DR   EMBL; AP000664; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP000977; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471065; EAW67525.1; -; Genomic_DNA.
DR   EMBL; BC137171; AAI37172.1; -; mRNA.
DR   CCDS; CCDS8436.1; -.
DR   RefSeq; NP_003096.1; NM_003105.5.
DR   PDB; 2DM4; NMR; -; A=1651-1745.
DR   PDB; 3G2S; X-ray; 1.70 A; C/D=2202-2214.
DR   PDB; 3G2T; X-ray; 2.00 A; C/D=2202-2214.
DR   PDB; 3WSX; X-ray; 2.35 A; A=29-753.
DR   PDB; 3WSY; X-ray; 3.11 A; A=86-753, C=42-56.
DR   PDB; 3WSZ; X-ray; 3.20 A; A=86-753.
DR   PDBsum; 2DM4; -.
DR   PDBsum; 3G2S; -.
DR   PDBsum; 3G2T; -.
DR   PDBsum; 3WSX; -.
DR   PDBsum; 3WSY; -.
DR   PDBsum; 3WSZ; -.
DR   SMR; Q92673; -.
DR   BioGrid; 112536; 65.
DR   DIP; DIP-41229N; -.
DR   IntAct; Q92673; 15.
DR   MINT; Q92673; -.
DR   STRING; 9606.ENSP00000260197; -.
DR   TCDB; 9.B.87.1.17; the selenoprotein p receptor (selp-receptor) family.
DR   GlyConnect; 1766; -.
DR   iPTMnet; Q92673; -.
DR   PhosphoSitePlus; Q92673; -.
DR   BioMuta; SORL1; -.
DR   DMDM; 296452912; -.
DR   EPD; Q92673; -.
DR   jPOST; Q92673; -.
DR   MaxQB; Q92673; -.
DR   PaxDb; Q92673; -.
DR   PeptideAtlas; Q92673; -.
DR   PRIDE; Q92673; -.
DR   ProteomicsDB; 75402; -.
DR   Ensembl; ENST00000260197; ENSP00000260197; ENSG00000137642.
DR   GeneID; 6653; -.
DR   KEGG; hsa:6653; -.
DR   UCSC; uc001pxx.4; human.
DR   CTD; 6653; -.
DR   DisGeNET; 6653; -.
DR   GeneCards; SORL1; -.
DR   HGNC; HGNC:11185; SORL1.
DR   HPA; CAB011500; -.
DR   HPA; HPA031321; -.
DR   MalaCards; SORL1; -.
DR   MIM; 104300; phenotype.
DR   MIM; 602005; gene.
DR   neXtProt; NX_Q92673; -.
DR   OpenTargets; ENSG00000137642; -.
DR   Orphanet; 1020; Early-onset autosomal dominant Alzheimer disease.
DR   Orphanet; 238616; NON RARE IN EUROPE: Alzheimer disease.
DR   PharmGKB; PA36022; -.
DR   eggNOG; KOG1215; Eukaryota.
DR   eggNOG; KOG3511; Eukaryota.
DR   eggNOG; ENOG410Y3W5; LUCA.
DR   GeneTree; ENSGT00950000182727; -.
DR   HOGENOM; HOG000007009; -.
DR   InParanoid; Q92673; -.
DR   OMA; QLKNNTC; -.
DR   OrthoDB; 1010560at2759; -.
DR   PhylomeDB; Q92673; -.
DR   TreeFam; TF324918; -.
DR   Reactome; R-HSA-977225; Amyloid fiber formation.
DR   SIGNOR; Q92673; -.
DR   ChiTaRS; SORL1; human.
DR   EvolutionaryTrace; Q92673; -.
DR   GenomeRNAi; 6653; -.
DR   PRO; PR:Q92673; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   Bgee; ENSG00000137642; Expressed in 235 organ(s), highest expression level in blood.
DR   ExpressionAtlas; Q92673; baseline and differential.
DR   Genevisible; Q92673; HS.
DR   GO; GO:0005769; C:early endosome; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR   GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0031985; C:Golgi cisterna; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0034362; C:low-density lipoprotein particle; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005641; C:nuclear envelope lumen; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0055037; C:recycling endosome; IMP:Alzheimers_University_of_Toronto.
DR   GO; GO:0005802; C:trans-Golgi network; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0030306; F:ADP-ribosylation factor binding; IPI:Alzheimers_University_of_Toronto.
DR   GO; GO:0001540; F:amyloid-beta binding; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0030169; F:low-density lipoprotein particle binding; IPI:BHF-UCL.
DR   GO; GO:0005041; F:low-density lipoprotein particle receptor activity; TAS:ARUK-UCL.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; TAS:ProtInc.
DR   GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
DR   GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
DR   GO; GO:1902430; P:negative regulation of amyloid-beta formation; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:1902960; P:negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:1902963; P:negative regulation of metalloendopeptidase activity involved in amyloid precursor protein catabolic process; IMP:Alzheimers_University_of_Toronto.
DR   GO; GO:1902997; P:negative regulation of neurofibrillary tangle assembly; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0050768; P:negative regulation of neurogenesis; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:1901215; P:negative regulation of neuron death; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:0032091; P:negative regulation of protein binding; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0032460; P:negative regulation of protein oligomerization; IMP:Alzheimers_University_of_Toronto.
DR   GO; GO:1902948; P:negative regulation of tau-protein kinase activity; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:1902771; P:positive regulation of choline O-acetyltransferase activity; ISS:Alzheimers_University_of_Toronto.
DR   GO; GO:1902955; P:positive regulation of early endosome to recycling endosome transport; IMP:Alzheimers_University_of_Toronto.
DR   GO; GO:2001137; P:positive regulation of endocytic recycling; IMP:Alzheimers_University_of_Toronto.
DR   GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IMP:Alzheimers_University_of_Toronto.
DR   GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IMP:Alzheimers_University_of_Toronto.
DR   GO; GO:1902966; P:positive regulation of protein localization to early endosome; IMP:Alzheimers_University_of_Toronto.
DR   GO; GO:0006892; P:post-Golgi vesicle-mediated transport; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0034067; P:protein localization to Golgi apparatus; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0051604; P:protein maturation; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0045053; P:protein retention in Golgi apparatus; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0006605; P:protein targeting; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0006622; P:protein targeting to lysosome; IDA:Alzheimers_University_of_Toronto.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; TAS:ProtInc.
DR   GO; GO:0014910; P:regulation of smooth muscle cell migration; IDA:UniProtKB.
DR   CDD; cd00063; FN3; 5.
DR   CDD; cd00112; LDLa; 11.
DR   Gene3D; 2.120.10.30; -; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 2.60.40.10; -; 3.
DR   Gene3D; 4.10.400.10; -; 11.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR000033; LDLR_classB_rpt.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
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; PF00041; fn3; 3.
DR   Pfam; PF00057; Ldl_recept_a; 10.
DR   Pfam; PF00058; Ldl_recept_b; 2.
DR   Pfam; PF15902; Sortilin-Vps10; 1.
DR   Pfam; PF15901; Sortilin_C; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00060; FN3; 6.
DR   SMART; SM00192; LDLa; 11.
DR   SMART; SM00135; LY; 5.
DR   SMART; SM00602; VPS10; 1.
DR   SUPFAM; SSF49265; SSF49265; 3.
DR   SUPFAM; SSF57424; SSF57424; 11.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50853; FN3; 4.
DR   PROSITE; PS01209; LDLRA_1; 10.
DR   PROSITE; PS50068; LDLRA_2; 11.
DR   PROSITE; PS51120; LDLRB; 5.
PE   1: Evidence at protein level;
KW   3D-structure; Alzheimer disease; Amyloidosis; Cholesterol metabolism;
KW   Cleavage on pair of basic residues; Complete proteome;
KW   Direct protein sequencing; Disease mutation; Disulfide bond;
KW   EGF-like domain; Endocytosis; Endosome; Glycoprotein; Golgi apparatus;
KW   LDL; Lipid metabolism; Lipid transport; Membrane; Neurodegeneration;
KW   Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
KW   Secreted; Signal; Steroid metabolism; Sterol metabolism;
KW   Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL        1     28       {ECO:0000255}.
FT   PROPEP       29     81       Removed in mature form.
FT                                {ECO:0000269|PubMed:8940146}.
FT                                /FTId=PRO_0000033164.
FT   CHAIN        82   2214       Sortilin-related receptor.
FT                                /FTId=PRO_0000033165.
FT   TOPO_DOM     82   2137       Extracellular. {ECO:0000255}.
FT   TRANSMEM   2138   2158       Helical. {ECO:0000255}.
FT   TOPO_DOM   2159   2214       Cytoplasmic. {ECO:0000255}.
FT   REPEAT      136    147       BNR 1.
FT   REPEAT      232    243       BNR 2.
FT   REPEAT      441    452       BNR 3.
FT   REPEAT      521    532       BNR 4.
FT   REPEAT      562    573       BNR 5.
FT   REPEAT      800    843       LDL-receptor class B 1.
FT   REPEAT      844    887       LDL-receptor class B 2.
FT   REPEAT      888    932       LDL-receptor class B 3.
FT   REPEAT      933    970       LDL-receptor class B 4.
FT   REPEAT      971   1013       LDL-receptor class B 5.
FT   DOMAIN     1026   1072       EGF-like.
FT   DOMAIN     1076   1114       LDL-receptor class A 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1115   1155       LDL-receptor class A 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1156   1194       LDL-receptor class A 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1198   1236       LDL-receptor class A 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1238   1272       LDL-receptor class A 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1273   1317       LDL-receptor class A 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1323   1361       LDL-receptor class A 7.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1366   1405       LDL-receptor class A 8.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1417   1455       LDL-receptor class A 9.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1469   1508       LDL-receptor class A 10.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1512   1551       LDL-receptor class A 11.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DOMAIN     1557   1649       Fibronectin type-III 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1653   1745       Fibronectin type-III 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1749   1844       Fibronectin type-III 3.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1843   1927       Fibronectin type-III 4.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     1934   2029       Fibronectin type-III 5.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   DOMAIN     2030   2118       Fibronectin type-III 6.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00316}.
FT   MOTIF        63     65       Cell attachment site. {ECO:0000255}.
FT   MOTIF      2172   2177       Endocytosis signal. {ECO:0000255}.
FT   MOD_RES     114    114       Phosphoserine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   MOD_RES    2206   2206       Phosphoserine; by ROCK2.
FT                                {ECO:0000269|PubMed:21147781}.
FT   CARBOHYD     99     99       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD    158    158       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    368    368       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    430    430       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    616    616       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    674    674       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    818    818       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    871    871       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1035   1035       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1068   1068       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1164   1164       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1191   1191       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1246   1246       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1367   1367       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1458   1458       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1608   1608       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1706   1706       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1733   1733       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   1809   1809       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1854   1854       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1894   1894       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1986   1986       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2010   2010       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   2054   2054       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2069   2069       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   2076   2076       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   CARBOHYD   2092   2092       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:19159218}.
FT   DISULFID   1078   1090       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1085   1103       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1097   1112       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1117   1131       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1125   1144       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1138   1153       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1158   1170       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1165   1183       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1177   1192       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1199   1211       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1206   1224       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1218   1235       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1239   1249       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1244   1262       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1256   1271       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1275   1289       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1283   1302       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1296   1315       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1325   1337       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1332   1350       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1344   1359       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1368   1381       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1376   1394       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1388   1403       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1419   1431       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1426   1444       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1438   1453       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1471   1484       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1478   1497       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1491   1506       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1514   1527       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1521   1540       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   DISULFID   1534   1549       {ECO:0000255|PROSITE-ProRule:PRU00124}.
FT   VARIANT     120    120       L -> S (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036371.
FT   VARIANT     141    141       Y -> C (in AD; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:22472873}.
FT                                /FTId=VAR_070012.
FT   VARIANT     511    511       G -> R (in AD; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:22472873}.
FT                                /FTId=VAR_070013.
FT   VARIANT     528    528       A -> T (in dbSNP:rs2298813).
FT                                {ECO:0000269|PubMed:18407551}.
FT                                /FTId=VAR_020360.
FT   VARIANT     924    924       N -> S (in AD; unknown pathological
FT                                significance; dbSNP:rs377498269).
FT                                {ECO:0000269|PubMed:22472873}.
FT                                /FTId=VAR_070014.
FT   VARIANT    1074   1074       Q -> E (in dbSNP:rs1699107).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:8940146,
FT                                ECO:0000269|PubMed:9157966,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_034508.
FT   VARIANT    1358   1358       N -> S (in AD; unknown pathological
FT                                significance; dbSNP:rs747306346).
FT                                {ECO:0000269|PubMed:22472873}.
FT                                /FTId=VAR_070015.
FT   VARIANT    1581   1581       M -> L (in a breast cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036372.
FT   VARIANT    1681   1681       G -> D (in AD; unknown pathological
FT                                significance).
FT                                {ECO:0000269|PubMed:22472873}.
FT                                /FTId=VAR_070016.
FT   VARIANT    1967   1967       V -> I (in dbSNP:rs1792120).
FT                                {ECO:0000269|PubMed:15489334,
FT                                ECO:0000269|PubMed:8940146,
FT                                ECO:0000269|PubMed:9157966,
FT                                ECO:0000269|Ref.4}.
FT                                /FTId=VAR_034509.
FT   VARIANT    1972   1972       L -> V (in a colorectal cancer sample;
FT                                somatic mutation; dbSNP:rs766895956).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_036373.
FT   STRAND       48     51       {ECO:0000244|PDB:3WSY}.
FT   STRAND       91     98       {ECO:0000244|PDB:3WSX}.
FT   STRAND      103    109       {ECO:0000244|PDB:3WSX}.
FT   STRAND      117    122       {ECO:0000244|PDB:3WSX}.
FT   STRAND      125    128       {ECO:0000244|PDB:3WSY}.
FT   STRAND      133    140       {ECO:0000244|PDB:3WSX}.
FT   STRAND      145    147       {ECO:0000244|PDB:3WSY}.
FT   HELIX       149    151       {ECO:0000244|PDB:3WSX}.
FT   STRAND      164    169       {ECO:0000244|PDB:3WSX}.
FT   STRAND      177    192       {ECO:0000244|PDB:3WSX}.
FT   STRAND      198    201       {ECO:0000244|PDB:3WSX}.
FT   STRAND      207    211       {ECO:0000244|PDB:3WSX}.
FT   STRAND      219    223       {ECO:0000244|PDB:3WSX}.
FT   STRAND      230    236       {ECO:0000244|PDB:3WSX}.
FT   STRAND      242    253       {ECO:0000244|PDB:3WSX}.
FT   TURN        256    258       {ECO:0000244|PDB:3WSX}.
FT   STRAND      264    268       {ECO:0000244|PDB:3WSX}.
FT   STRAND      271    273       {ECO:0000244|PDB:3WSY}.
FT   STRAND      275    282       {ECO:0000244|PDB:3WSX}.
FT   HELIX       287    289       {ECO:0000244|PDB:3WSX}.
FT   STRAND      290    298       {ECO:0000244|PDB:3WSX}.
FT   STRAND      300    303       {ECO:0000244|PDB:3WSX}.
FT   STRAND      306    313       {ECO:0000244|PDB:3WSX}.
FT   STRAND      318    320       {ECO:0000244|PDB:3WSY}.
FT   STRAND      323    330       {ECO:0000244|PDB:3WSX}.
FT   STRAND      333    337       {ECO:0000244|PDB:3WSZ}.
FT   STRAND      349    353       {ECO:0000244|PDB:3WSX}.
FT   STRAND      355    358       {ECO:0000244|PDB:3WSX}.
FT   STRAND      360    363       {ECO:0000244|PDB:3WSX}.
FT   HELIX       366    368       {ECO:0000244|PDB:3WSX}.
FT   STRAND      369    374       {ECO:0000244|PDB:3WSX}.
FT   STRAND      383    391       {ECO:0000244|PDB:3WSX}.
FT   STRAND      394    396       {ECO:0000244|PDB:3WSY}.
FT   TURN        397    400       {ECO:0000244|PDB:3WSY}.
FT   HELIX       402    405       {ECO:0000244|PDB:3WSY}.
FT   STRAND      411    416       {ECO:0000244|PDB:3WSX}.
FT   STRAND      420    422       {ECO:0000244|PDB:3WSX}.
FT   STRAND      424    428       {ECO:0000244|PDB:3WSX}.
FT   STRAND      431    434       {ECO:0000244|PDB:3WSY}.
FT   HELIX       435    437       {ECO:0000244|PDB:3WSY}.
FT   STRAND      439    445       {ECO:0000244|PDB:3WSX}.
FT   STRAND      451    453       {ECO:0000244|PDB:3WSY}.
FT   STRAND      460    462       {ECO:0000244|PDB:3WSY}.
FT   HELIX       469    471       {ECO:0000244|PDB:3WSY}.
FT   STRAND      473    479       {ECO:0000244|PDB:3WSX}.
FT   HELIX       480    485       {ECO:0000244|PDB:3WSY}.
FT   STRAND      492    495       {ECO:0000244|PDB:3WSX}.
FT   STRAND      504    510       {ECO:0000244|PDB:3WSX}.
FT   STRAND      519    525       {ECO:0000244|PDB:3WSX}.
FT   STRAND      531    536       {ECO:0000244|PDB:3WSX}.
FT   STRAND      538    543       {ECO:0000244|PDB:3WSX}.
FT   HELIX       544    546       {ECO:0000244|PDB:3WSX}.
FT   STRAND      548    553       {ECO:0000244|PDB:3WSX}.
FT   STRAND      560    566       {ECO:0000244|PDB:3WSX}.
FT   STRAND      572    575       {ECO:0000244|PDB:3WSX}.
FT   STRAND      577    579       {ECO:0000244|PDB:3WSY}.
FT   STRAND      581    588       {ECO:0000244|PDB:3WSX}.
FT   STRAND      596    602       {ECO:0000244|PDB:3WSX}.
FT   TURN        604    607       {ECO:0000244|PDB:3WSZ}.
FT   STRAND      610    616       {ECO:0000244|PDB:3WSX}.
FT   HELIX       618    621       {ECO:0000244|PDB:3WSX}.
FT   HELIX       627    629       {ECO:0000244|PDB:3WSX}.
FT   STRAND      630    633       {ECO:0000244|PDB:3WSX}.
FT   HELIX       635    637       {ECO:0000244|PDB:3WSY}.
FT   TURN        638    641       {ECO:0000244|PDB:3WSY}.
FT   STRAND      647    654       {ECO:0000244|PDB:3WSX}.
FT   STRAND      670    674       {ECO:0000244|PDB:3WSX}.
FT   HELIX       679    681       {ECO:0000244|PDB:3WSX}.
FT   STRAND      682    684       {ECO:0000244|PDB:3WSX}.
FT   STRAND      688    690       {ECO:0000244|PDB:3WSX}.
FT   HELIX       694    696       {ECO:0000244|PDB:3WSX}.
FT   STRAND      699    701       {ECO:0000244|PDB:3WSX}.
FT   HELIX       703    705       {ECO:0000244|PDB:3WSX}.
FT   STRAND      722    724       {ECO:0000244|PDB:3WSX}.
FT   STRAND      727    730       {ECO:0000244|PDB:3WSX}.
FT   TURN        740    745       {ECO:0000244|PDB:3WSX}.
FT   STRAND      748    750       {ECO:0000244|PDB:3WSX}.
FT   STRAND     1655   1660       {ECO:0000244|PDB:2DM4}.
FT   STRAND     1669   1674       {ECO:0000244|PDB:2DM4}.
FT   STRAND     1683   1692       {ECO:0000244|PDB:2DM4}.
FT   STRAND     1699   1710       {ECO:0000244|PDB:2DM4}.
FT   STRAND     1718   1729       {ECO:0000244|PDB:2DM4}.
FT   STRAND     1731   1734       {ECO:0000244|PDB:2DM4}.
FT   STRAND     1738   1741       {ECO:0000244|PDB:2DM4}.
SQ   SEQUENCE   2214 AA;  248426 MW;  4C215BB33E65C0B2 CRC64;
     MATRSSRRES RLPFLFTLVA LLPPGALCEV WTQRLHGGSA PLPQDRGFLV VQGDPRELRL
     WARGDARGAS RADEKPLRRK RSAALQPEPI KVYGQVSLND SHNQMVVHWA GEKSNVIVAL
     ARDSLALARP KSSDVYVSYD YGKSFKKISD KLNFGLGNRS EAVIAQFYHS PADNKRYIFA
     DAYAQYLWIT FDFCNTLQGF SIPFRAADLL LHSKASNLLL GFDRSHPNKQ LWKSDDFGQT
     WIMIQEHVKS FSWGIDPYDK PNTIYIERHE PSGYSTVFRS TDFFQSRENQ EVILEEVRDF
     QLRDKYMFAT KVVHLLGSEQ QSSVQLWVSF GRKPMRAAQF VTRHPINEYY IADASEDQVF
     VCVSHSNNRT NLYISEAEGL KFSLSLENVL YYSPGGAGSD TLVRYFANEP FADFHRVEGL
     QGVYIATLIN GSMNEENMRS VITFDKGGTW EFLQAPAFTG YGEKINCELS QGCSLHLAQR
     LSQLLNLQLR RMPILSKESA PGLIIATGSV GKNLASKTNV YISSSAGARW REALPGPHYY
     TWGDHGGIIT AIAQGMETNE LKYSTNEGET WKTFIFSEKP VFVYGLLTEP GEKSTVFTIF
     GSNKENVHSW LILQVNATDA LGVPCTENDY KLWSPSDERG NECLLGHKTV FKRRTPHATC
     FNGEDFDRPV VVSNCSCTRE DYECDFGFKM SEDLSLEVCV PDPEFSGKSY SPPVPCPVGS
     TYRRTRGYRK ISGDTCSGGD VEARLEGELV PCPLAEENEF ILYAVRKSIY RYDLASGATE
     QLPLTGLRAA VALDFDYEHN CLYWSDLALD VIQRLCLNGS TGQEVIINSG LETVEALAFE
     PLSQLLYWVD AGFKKIEVAN PDGDFRLTIV NSSVLDRPRA LVLVPQEGVM FWTDWGDLKP
     GIYRSNMDGS AAYHLVSEDV KWPNGISVDD QWIYWTDAYL ECIERITFSG QQRSVILDNL
     PHPYAIAVFK NEIYWDDWSQ LSIFRASKYS GSQMEILANQ LTGLMDMKIF YKGKNTGSNA
     CVPRPCSLLC LPKANNSRSC RCPEDVSSSV LPSGDLMCDC PQGYQLKNNT CVKQENTCLR
     NQYRCSNGNC INSIWWCDFD NDCGDMSDER NCPTTICDLD TQFRCQESGT CIPLSYKCDL
     EDDCGDNSDE SHCEMHQCRS DEYNCSSGMC IRSSWVCDGD NDCRDWSDEA NCTAIYHTCE
     ASNFQCRNGH CIPQRWACDG DTDCQDGSDE DPVNCEKKCN GFRCPNGTCI PSSKHCDGLR
     DCSDGSDEQH CEPLCTHFMD FVCKNRQQCL FHSMVCDGII QCRDGSDEDA AFAGCSQDPE
     FHKVCDEFGF QCQNGVCISL IWKCDGMDDC GDYSDEANCE NPTEAPNCSR YFQFRCENGH
     CIPNRWKCDR ENDCGDWSDE KDCGDSHILP FSTPGPSTCL PNYYRCSSGT CVMDTWVCDG
     YRDCADGSDE EACPLLANVT AASTPTQLGR CDRFEFECHQ PKTCIPNWKR CDGHQDCQDG
     RDEANCPTHS TLTCMSREFQ CEDGEACIVL SERCDGFLDC SDESDEKACS DELTVYKVQN
     LQWTADFSGD VTLTWMRPKK MPSASCVYNV YYRVVGESIW KTLETHSNKT NTVLKVLKPD
     TTYQVKVQVQ CLSKAHNTND FVTLRTPEGL PDAPRNLQLS LPREAEGVIV GHWAPPIHTH
     GLIREYIVEY SRSGSKMWAS QRAASNFTEI KNLLVNTLYT VRVAAVTSRG IGNWSDSKSI
     TTIKGKVIPP PDIHIDSYGE NYLSFTLTME SDIKVNGYVV NLFWAFDTHK QERRTLNFRG
     SILSHKVGNL TAHTSYEISA WAKTDLGDSP LAFEHVMTRG VRPPAPSLKA KAINQTAVEC
     TWTGPRNVVY GIFYATSFLD LYRNPKSLTT SLHNKTVIVS KDEQYLFLVR VVVPYQGPSS
     DYVVVKMIPD SRLPPRHLHV VHTGKTSVVI KWESPYDSPD QDLLYAVAVK DLIRKTDRSY
     KVKSRNSTVE YTLNKLEPGG KYHIIVQLGN MSKDSSIKIT TVSLSAPDAL KIITENDHVL
     LFWKSLALKE KHFNESRGYE IHMFDSAMNI TAYLGNTTDN FFKISNLKMG HNYTFTVQAR
     CLFGNQICGE PAILLYDELG SGADASATQA ARSTDVAAVV VPILFLILLS LGVGFAILYT
     KHRRLQSSFT AFANSHYSSR LGSAIFSSGD DLGEDDEDAP MITGFSDDVP MVIA
//
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