PTPRM_HUMAN
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 03-AUG-2022, entry version 221.
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 PDBsum; 1RPM; -.
DR PDBsum; 2C9A; -.
DR PDBsum; 2V5Y; -.
DR AlphaFoldDB; 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 GlyGen; P28827; 15 sites, 14 N-linked glycans (6 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P28827; -.
DR PhosphoSitePlus; P28827; -.
DR BioMuta; PTPRM; -.
DR DMDM; 206729890; -.
DR EPD; P28827; -.
DR jPOST; P28827; -.
DR MassIVE; P28827; -.
DR MaxQB; P28827; -.
DR PaxDb; P28827; -.
DR PeptideAtlas; P28827; -.
DR PRIDE; P28827; -.
DR ProteomicsDB; 54501; -. [P28827-1]
DR Antibodypedia; 21926; 239 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 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; 411281at2759; -.
DR PhylomeDB; P28827; -.
DR TreeFam; TF312900; -.
DR BRENDA; 3.1.3.48; 2681.
DR PathwayCommons; P28827; -.
DR SignaLink; P28827; -.
DR BioGRID-ORCS; 5797; 19 hits in 1066 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 192 other tissues.
DR ExpressionAtlas; P28827; baseline and differential.
DR Genevisible; P28827; HS.
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:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
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: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 DisProt; DP02580; -.
DR Gene3D; 2.60.40.10; -; 4.
DR Gene3D; 3.90.190.10; -; 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 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; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF52799; SSF52799; 2.
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.
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
