ID   PTPRM_HUMAN             Reviewed;        1452 AA.
AC   P28827; A7MBN1; D3DUH8; J3QL11;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 2.
DT   27-MAR-2024, entry version 230.
DE   RecName: Full=Receptor-type tyrosine-protein phosphatase mu;
DE            Short=Protein-tyrosine phosphatase mu;
DE            Short=R-PTP-mu;
DE            EC=3.1.3.48;
DE   Flags: Precursor;
GN   Name=PTPRM; Synonyms=PTPRL1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=1655529; DOI=10.1016/0014-5793(91)81241-y;
RA   Gebbink M.F.B.G., van Etten I., Hateboer G., Suijkerbuijk R.,
RA   Beijersbergen R., Geurts van Kessel A., Moolenaar W.H.;
RT   "Cloning, expression and chromosomal localization of a new putative
RT   receptor-like protein tyrosine phosphatase.";
RL   FEBS Lett. 290:123-130(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16177791; DOI=10.1038/nature03983;
RA   Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA   Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA   Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA   Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA   Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA   Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA   Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA   Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA   Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT   "DNA sequence and analysis of human chromosome 18.";
RL   Nature 437:551-555(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=10753936; DOI=10.1074/jbc.275.15.11264;
RA   Zondag G.C., Reynolds A.B., Moolenaar W.H.;
RT   "Receptor protein-tyrosine phosphatase RPTPmu binds to and dephosphorylates
RT   the catenin p120(ctn).";
RL   J. Biol. Chem. 275:11264-11269(2000).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-131.
RC   TISSUE=Plasma;
RX   PubMed=16335952; DOI=10.1021/pr0502065;
RA   Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA   Smith R.D.;
RT   "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT   hydrazide chemistry, and mass spectrometry.";
RL   J. Proteome Res. 4:2070-2080(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-821, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 879-1156.
RX   PubMed=9346878; DOI=10.1074/jbc.272.44.27505;
RA   Hoffmann K.M., Tonks N.K., Barford D.;
RT   "The crystal structure of domain 1 of receptor protein-tyrosine phosphatase
RT   mu.";
RL   J. Biol. Chem. 272:27505-27508(1997).
RN   [9]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=21998202; DOI=10.1091/mbc.e11-03-0175;
RA   Kim W.K., Jung H., Kim E.Y., Kim D.H., Cho Y.S., Park B.C., Park S.G.,
RA   Ko Y., Bae K.H., Lee S.C.;
RT   "RPTPmu tyrosine phosphatase promotes adipogenic differentiation via
RT   modulation of p120 catenin phosphorylation.";
RL   Mol. Biol. Cell 22:4883-4891(2011).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-279, FUNCTION, AND DISULFIDE
RP   BONDS.
RX   PubMed=16456543; DOI=10.1038/sj.emboj.7600974;
RA   Aricescu A.R., Hon W.-C., Siebold C., Lu W., van der Merwe P.A.,
RA   Jones E.Y.;
RT   "Molecular analysis of receptor protein tyrosine phosphatase mu-mediated
RT   cell adhesion.";
RL   EMBO J. 25:701-712(2006).
RN   [11] {ECO:0007744|PDB:2V5Y}
RP   X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 21-742, GLYCOSYLATION AT ASN-72;
RP   ASN-92; ASN-131; ASN-406; ASN-414; ASN-454 AND ASN-544, SUBCELLULAR
RP   LOCATION, SUBUNIT, AND MUTAGENESIS OF ARG-239; ARG-240; TYR-297 AND
RP   TRP-299.
RX   PubMed=17761881; DOI=10.1126/science.1144646;
RA   Aricescu A.R., Siebold C., Choudhuri K., Chang V.T., Lu W., Davis S.J.,
RA   van der Merwe P.A., Jones E.Y.;
RT   "Structure of a tyrosine phosphatase adhesive interaction reveals a spacer-
RT   clamp mechanism.";
RL   Science 317:1217-1220(2007).
CC   -!- FUNCTION: Receptor protein-tyrosine phosphatase that mediates homotypic
CC       cell-cell interactions and plays a role in adipogenic differentiation
CC       via modulation of p120 catenin/CTNND1 phosphorylation (PubMed:17761881,
CC       PubMed:10753936). Promotes CTNND1 dephosphorylation and prevents its
CC       cytoplasmic localization where it inhibits SLC2A4 membrane trafficking.
CC       In turn, SLC2A4 is directed to the plasma membrane and performs its
CC       glucose transporter function (PubMed:21998202).
CC       {ECO:0000269|PubMed:10753936, ECO:0000269|PubMed:16456543,
CC       ECO:0000269|PubMed:17761881, ECO:0000269|PubMed:21998202}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC         phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:82620; EC=3.1.3.48;
CC         Evidence={ECO:0000269|PubMed:10753936, ECO:0000269|PubMed:21998202};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17761881}.
CC   -!- INTERACTION:
CC       P28827; P28827: PTPRM; NbExp=2; IntAct=EBI-2257317, EBI-2257317;
CC       P28827; P09803: Cdh1; Xeno; NbExp=3; IntAct=EBI-2257317, EBI-984420;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10753936};
CC       Single-pass type I membrane protein. Note=Localizes in regions of cell-
CC       cell contact. {ECO:0000269|PubMed:10753936}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P28827-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P28827-2; Sequence=VSP_046677;
CC   -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC       Receptor class 2B subfamily. {ECO:0000305}.
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DR   EMBL; X58288; CAA41226.1; -; mRNA.
DR   EMBL; AC006566; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP000897; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP001094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP005118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP005227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP005900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471113; EAX01623.1; -; Genomic_DNA.
DR   EMBL; CH471113; EAX01624.1; -; Genomic_DNA.
DR   EMBL; BC151842; AAI51843.1; -; mRNA.
DR   CCDS; CCDS11840.1; -. [P28827-1]
DR   CCDS; CCDS58613.1; -. [P28827-2]
DR   PIR; S17669; S17669.
DR   RefSeq; NP_001098714.1; NM_001105244.1. [P28827-2]
DR   RefSeq; NP_002836.3; NM_002845.3. [P28827-1]
DR   PDB; 1RPM; X-ray; 2.30 A; A/B=879-1156.
DR   PDB; 2C9A; X-ray; 2.70 A; A=21-279.
DR   PDB; 2V5Y; X-ray; 3.10 A; A=21-742.
DR   PDB; 8A16; X-ray; 2.89 A; A/B=477-723.
DR   PDB; 8A17; X-ray; 3.09 A; A/B/C/D=477-723.
DR   PDBsum; 1RPM; -.
DR   PDBsum; 2C9A; -.
DR   PDBsum; 2V5Y; -.
DR   PDBsum; 8A16; -.
DR   PDBsum; 8A17; -.
DR   AlphaFoldDB; P28827; -.
DR   SASBDB; P28827; -.
DR   SMR; P28827; -.
DR   BioGRID; 111761; 66.
DR   DIP; DIP-668N; -.
DR   IntAct; P28827; 17.
DR   MINT; P28827; -.
DR   STRING; 9606.ENSP00000463325; -.
DR   BindingDB; P28827; -.
DR   ChEMBL; CHEMBL4661; -.
DR   GuidetoPHARMACOLOGY; 1860; -.
DR   DEPOD; PTPRM; -.
DR   GlyConnect; 1971; 13 N-Linked glycans (6 sites).
DR   GlyCosmos; P28827; 15 sites, 15 glycans.
DR   GlyGen; P28827; 15 sites, 14 N-linked glycans (6 sites), 1 O-linked glycan (1 site).
DR   iPTMnet; P28827; -.
DR   PhosphoSitePlus; P28827; -.
DR   SwissPalm; P28827; -.
DR   BioMuta; PTPRM; -.
DR   DMDM; 206729890; -.
DR   EPD; P28827; -.
DR   jPOST; P28827; -.
DR   MassIVE; P28827; -.
DR   MaxQB; P28827; -.
DR   PaxDb; 9606-ENSP00000463325; -.
DR   PeptideAtlas; P28827; -.
DR   ProteomicsDB; 54501; -. [P28827-1]
DR   Antibodypedia; 21926; 259 antibodies from 34 providers.
DR   DNASU; 5797; -.
DR   Ensembl; ENST00000332175.12; ENSP00000331418.8; ENSG00000173482.17. [P28827-1]
DR   Ensembl; ENST00000580170.6; ENSP00000463325.1; ENSG00000173482.17. [P28827-2]
DR   GeneID; 5797; -.
DR   KEGG; hsa:5797; -.
DR   MANE-Select; ENST00000580170.6; ENSP00000463325.1; NM_001105244.2; NP_001098714.1. [P28827-2]
DR   UCSC; uc002knn.5; human. [P28827-1]
DR   AGR; HGNC:9675; -.
DR   CTD; 5797; -.
DR   DisGeNET; 5797; -.
DR   GeneCards; PTPRM; -.
DR   HGNC; HGNC:9675; PTPRM.
DR   HPA; ENSG00000173482; Low tissue specificity.
DR   MIM; 176888; gene.
DR   neXtProt; NX_P28827; -.
DR   OpenTargets; ENSG00000173482; -.
DR   PharmGKB; PA34020; -.
DR   VEuPathDB; HostDB:ENSG00000173482; -.
DR   eggNOG; KOG4228; Eukaryota.
DR   GeneTree; ENSGT00940000155020; -.
DR   InParanoid; P28827; -.
DR   OrthoDB; 2875525at2759; -.
DR   PhylomeDB; P28827; -.
DR   TreeFam; TF312900; -.
DR   BRENDA; 3.1.3.48; 2681.
DR   PathwayCommons; P28827; -.
DR   SignaLink; P28827; -.
DR   BioGRID-ORCS; 5797; 20 hits in 1161 CRISPR screens.
DR   ChiTaRS; PTPRM; human.
DR   EvolutionaryTrace; P28827; -.
DR   GeneWiki; PTPRM; -.
DR   GenomeRNAi; 5797; -.
DR   Pharos; P28827; Tchem.
DR   PRO; PR:P28827; -.
DR   Proteomes; UP000005640; Chromosome 18.
DR   RNAct; P28827; Protein.
DR   Bgee; ENSG00000173482; Expressed in ventricular zone and 194 other cell types or tissues.
DR   ExpressionAtlas; P28827; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; IDA:UniProtKB.
DR   GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IDA:DisProt.
DR   GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0045296; F:cadherin binding; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0016791; F:phosphatase activity; IDA:UniProt.
DR   GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; IDA:UniProtKB.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IDA:UniProtKB.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IMP:UniProtKB.
DR   GO; GO:0010596; P:negative regulation of endothelial cell migration; IMP:UniProtKB.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IMP:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; IDA:UniProtKB.
DR   GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; IDA:UniProtKB.
DR   GO; GO:0010842; P:retina layer formation; IMP:UniProtKB.
DR   GO; GO:0031290; P:retinal ganglion cell axon guidance; IDA:UniProtKB.
DR   GO; GO:0007165; P:signal transduction; IDA:UniProtKB.
DR   CDD; cd00063; FN3; 3.
DR   CDD; cd06263; MAM; 1.
DR   CDD; cd14633; R-PTPc-M-1; 1.
DR   CDD; cd14635; R-PTPc-M-2; 1.
DR   DisProt; DP02580; -.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 4.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 2.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013151; Immunoglobulin.
DR   InterPro; IPR000998; MAM_dom.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000242; PTP_cat.
DR   InterPro; IPR045911; R-PTP-mu_cat_rpt1.
DR   InterPro; IPR016130; Tyr_Pase_AS.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR24051:SF12; PROTEIN TYROSINE PHOSPHATASE, RECEPTOR TYPE, M; 1.
DR   PANTHER; PTHR24051; SUSHI DOMAIN-CONTAINING PROTEIN 1; 1.
DR   Pfam; PF00041; fn3; 2.
DR   Pfam; PF00047; ig; 1.
DR   Pfam; PF00629; MAM; 1.
DR   Pfam; PF00102; Y_phosphatase; 2.
DR   PRINTS; PR00020; MAMDOMAIN.
DR   PRINTS; PR00700; PRTYPHPHTASE.
DR   SMART; SM00060; FN3; 4.
DR   SMART; SM00409; IG; 1.
DR   SMART; SM00137; MAM; 1.
DR   SMART; SM00194; PTPc; 2.
DR   SMART; SM00404; PTPc_motif; 2.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF49265; Fibronectin type III; 2.
DR   SUPFAM; SSF48726; Immunoglobulin; 1.
DR   PROSITE; PS50853; FN3; 3.
DR   PROSITE; PS50835; IG_LIKE; 1.
DR   PROSITE; PS00740; MAM_1; 1.
DR   PROSITE; PS50060; MAM_2; 1.
DR   PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
DR   PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
DR   Genevisible; P28827; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW   Disulfide bond; Glycoprotein; Hydrolase; Immunoglobulin domain; Membrane;
KW   Phosphoprotein; Protein phosphatase; Receptor; Reference proteome; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..1452
FT                   /note="Receptor-type tyrosine-protein phosphatase mu"
FT                   /id="PRO_0000025448"
FT   TOPO_DOM        21..742
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        743..764
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        765..1452
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          22..184
FT                   /note="MAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00128"
FT   DOMAIN          186..277
FT                   /note="Ig-like C2-type"
FT   DOMAIN          284..379
FT                   /note="Fibronectin type-III 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          382..480
FT                   /note="Fibronectin type-III 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          482..587
FT                   /note="Fibronectin type-III 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          589..671
FT                   /note="Fibronectin type-III 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          900..1154
FT                   /note="Tyrosine-protein phosphatase 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   DOMAIN          1186..1448
FT                   /note="Tyrosine-protein phosphatase 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT   ACT_SITE        1095
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        1389
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1063
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1095..1101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         1139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         821
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CARBOHYD        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        131
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16335952"
FT   CARBOHYD        249
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        406
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761881,
FT                   ECO:0007744|PDB:2V5Y"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761881,
FT                   ECO:0007744|PDB:2V5Y"
FT   CARBOHYD        454
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761881,
FT                   ECO:0007744|PDB:2V5Y"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        544
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:17761881,
FT                   ECO:0007744|PDB:2V5Y"
FT   CARBOHYD        598
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        651
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        681
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        27..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:16456543"
FT   DISULFID        96..182
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:16456543"
FT   DISULFID        206..260
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT                   ECO:0000269|PubMed:16456543"
FT   VAR_SEQ         842
FT                   /note="P -> PDPFVPTAILVPIN (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_046677"
FT   VARIANT         39
FT                   /note="S -> R (in dbSNP:rs35224276)"
FT                   /id="VAR_046634"
FT   MUTAGEN         239
FT                   /note="R->E: Abolishes dimerization."
FT                   /evidence="ECO:0000269|PubMed:17761881"
FT   MUTAGEN         240
FT                   /note="R->E: Abolishes dimerization."
FT                   /evidence="ECO:0000269|PubMed:17761881"
FT   MUTAGEN         297
FT                   /note="Y->A: Abolishes dimerization."
FT                   /evidence="ECO:0000269|PubMed:17761881"
FT   MUTAGEN         299
FT                   /note="W->A: Abolishes dimerization."
FT                   /evidence="ECO:0000269|PubMed:17761881"
FT   CONFLICT        3
FT                   /note="G -> T (in Ref. 1; CAA41226)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        68
FT                   /note="F -> L (in Ref. 1; CAA41226)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1300
FT                   /note="P -> L (in Ref. 4; AAI51843)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1384
FT                   /note="R -> P (in Ref. 1; CAA41226)"
FT                   /evidence="ECO:0000305"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   HELIX           33..36
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          42..45
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          49..52
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          66..72
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          81..85
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          96..104
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          111..120
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          129..132
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          140..147
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          155..163
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          169..180
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          183..185
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          194..196
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          198..200
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          202..210
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          217..222
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          230..237
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          240..247
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   HELIX           252..254
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          256..264
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          267..278
FT                   /evidence="ECO:0007829|PDB:2C9A"
FT   STRAND          284..286
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          289..293
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          298..301
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          305..309
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          315..326
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          328..332
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          335..340
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          348..356
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          370..373
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          384..391
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          396..401
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   HELIX           405..408
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          410..412
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          414..434
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          443..446
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          454..462
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          467..469
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          473..476
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   TURN            487..489
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          491..495
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          498..502
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          515..525
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          536..542
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          547..550
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          557..567
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   STRAND          570..580
FT                   /evidence="ECO:0007829|PDB:2V5Y"
FT   TURN            882..884
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   HELIX           885..905
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   TURN            916..919
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   HELIX           921..926
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   HELIX           936..938
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          939..941
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   TURN            949..952
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          953..961
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          964..971
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   HELIX           976..978
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   HELIX           979..988
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          993..996
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          1000..1002
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          1014..1019
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          1022..1032
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          1035..1044
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          1051..1058
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          1063..1065
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   HELIX           1071..1083
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          1091..1099
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   HELIX           1100..1118
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   STRAND          1119..1121
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   HELIX           1123..1133
FT                   /evidence="ECO:0007829|PDB:1RPM"
FT   HELIX           1141..1155
FT                   /evidence="ECO:0007829|PDB:1RPM"
SQ   SEQUENCE   1452 AA;  163682 MW;  8319E3D3A583E992 CRC64;
     MRGLGTCLAT LAGLLLTAAG ETFSGGCLFD EPYSTCGYSQ SEGDDFNWEQ VNTLTKPTSD
     PWMPSGSFML VNASGRPEGQ RAHLLLPQLK ENDTHCIDFH YFVSSKSNSP PGLLNVYVKV
     NNGPLGNPIW NISGDPTRTW NRAELAISTF WPNFYQVIFE VITSGHQGYL AIDEVKVLGH
     PCTRTPHFLR IQNVEVNAGQ FATFQCSAIG RTVAGDRLWL QGIDVRDAPL KEIKVTSSRR
     FIASFNVVNT TKRDAGKYRC MIRTEGGVGI SNYAELVVKE PPVPIAPPQL ASVGATYLWI
     QLNANSINGD GPIVAREVEY CTASGSWNDR QPVDSTSYKI GHLDPDTEYE ISVLLTRPGE
     GGTGSPGPAL RTRTKCADPM RGPRKLEVVE VKSRQITIRW EPFGYNVTRC HSYNLTVHYC
     YQVGGQEQVR EEVSWDTENS HPQHTITNLS PYTNVSVKLI LMNPEGRKES QELIVQTDED
     LPGAVPTESI QGSTFEEKIF LQWREPTQTY GVITLYEITY KAVSSFDPEI DLSNQSGRVS
     KLGNETHFLF FGLYPGTTYS FTIRASTAKG FGPPATNQFT TKISAPSMPA YELETPLNQT
     DNTVTVMLKP AHSRGAPVSV YQIVVEEERP RRTKKTTEIL KCYPVPIHFQ NASLLNSQYY
     FAAEFPADSL QAAQPFTIGD NKTYNGYWNT PLLPYKSYRI YFQAASRANG ETKIDCVQVA
     TKGAATPKPV PEPEKQTDHT VKIAGVIAGI LLFVIIFLGV VLVMKKRKLA KKRKETMSST
     RQEMTVMVNS MDKSYAEQGT NCDEAFSFMD THNLNGRSVS SPSSFTMKTN TLSTSVPNSY
     YPDETHTMAS DTSSLVQSHT YKKREPADVP YQTGQLHPAI RVADLLQHIT QMKCAEGYGF
     KEEYESFFEG QSAPWDSAKK DENRMKNRYG NIIAYDHSRV RLQTIEGDTN SDYINGNYID
     GYHRPNHYIA TQGPMQETIY DFWRMVWHEN TASIIMVTNL VEVGRVKCCK YWPDDTEIYK
     DIKVTLIETE LLAEYVIRTF AVEKRGVHEI REIRQFHFTG WPDHGVPYHA TGLLGFVRQV
     KSKSPPSAGP LVVHCSAGAG RTGCFIVIDI MLDMAEREGV VDIYNCVREL RSRRVNMVQT
     EEQYVFIHDA ILEACLCGDT SVPASQVRSL YYDMNKLDPQ TNSSQIKEEF RTLNMVTPTL
     RVEDCSIALL PRNHEKNRCM DILPPDRCLP FLITIDGESS NYINAALMDS YKQPSAFIVT
     QHPLPNTVKD FWRLVLDYHC TSVVMLNDVD PAQLCPQYWP ENGVHRHGPI QVEFVSADLE
     EDIISRIFRI YNAARPQDGY RMVQQFQFLG WPMYRDTPVS KRSFLKLIRQ VDKWQEEYNG
     GEGRTVVHCL NGGGRSGTFC AISIVCEMLR HQRTVDVFHA VKTLRNNKPN MVDLLDQYKF
     CYEVALEYLN SG
//