GPNMB_HUMAN
ID GPNMB_HUMAN Reviewed; 572 AA.
AC Q14956; A4D155; Q6UVX1; Q8N1A1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Transmembrane glycoprotein NMB;
DE AltName: Full=Hematopoietic growth factor inducible neurokinin-1 type {ECO:0000303|PubMed:12609765};
DE Flags: Precursor;
GN Name=GPNMB; Synonyms=HGFIN {ECO:0000303|PubMed:12609765}, NMB;
GN ORFNames=UNQ1725/PRO9925;
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 2), AND TISSUE SPECIFICITY.
RC TISSUE=Melanoma;
RX PubMed=7814155; DOI=10.1002/ijc.2910600111;
RA Weterman M.A.J., Ajubi N., van Dinter I.M.R., Degen W.G.J.,
RA van Muijen G.N.P., Ruiter D.J., Bloemers H.P.J.;
RT "NMB, a novel gene, is expressed in low-metastatic human melanoma cell
RT lines and xenografts.";
RL Int. J. Cancer 60:73-81(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INDUCTION
RP BY G-CSF AND M-CSF.
RC TISSUE=Peripheral blood;
RX PubMed=12609765; DOI=10.1016/s0167-0115(02)00288-4;
RA Bandari P.S., Qian J., Yehia G., Joshi D.D., Maloof P.B., Potian J.,
RA Oh H.S., Gascon P., Harrison J.S., Rameshwar P.;
RT "Hematopoietic growth factor inducible neurokinin-1 type: a transmembrane
RT protein that is similar to neurokinin 1 interacts with substance P.";
RL Regul. Pept. 111:169-178(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=12643545; DOI=10.1021/pr025562r;
RA Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J.,
RA Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F.,
RA Appella E.;
RT "Proteomic analysis of early melanosomes: identification of novel
RT melanosomal proteins.";
RL J. Proteome Res. 2:69-79(2003).
RN [9]
RP SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, GLYCOSYLATION,
RP ALTERNATIVE SPLICING, POTENTIAL TUMOR-ASSOCIATED ANTIGEN FOR IMMUNOTHERAPY,
RP AND DISEASE.
RX PubMed=16489096; DOI=10.1158/1078-0432.ccr-05-2018;
RA Tse K.F., Jeffers M., Pollack V.A., McCabe D.A., Shadish M.L.,
RA Khramtsov N.V., Hackett C.S., Shenoy S.G., Kuang B., Boldog F.L.,
RA MacDougall J.R., Rastelli L., Herrmann J., Gallo M., Gazit-Bornstein G.,
RA Senter P.D., Meyer D.L., Lichenstein H.S., LaRochelle W.J.;
RT "CR011, a fully human monoclonal antibody-auristatin E conjugate, for the
RT treatment of melanoma.";
RL Clin. Cancer Res. 12:1373-1382(2006).
RN [10]
RP SUBCELLULAR LOCATION, TOPOLOGY, TISSUE SPECIFICITY, ALTERNATIVE SPLICING,
RP AND DISEASE.
RX PubMed=16609006; DOI=10.1158/1078-0432.ccr-05-2797;
RA Kuan C.T., Wakiya K., Dowell J.M., Herndon J.E. II, Reardon D.A.,
RA Graner M.W., Riggins G.J., Wikstrand C.J., Bigner D.D.;
RT "Glycoprotein nonmetastatic melanoma protein B, a potential molecular
RT therapeutic target in patients with glioblastoma multiforme.";
RL Clin. Cancer Res. 12:1970-1982(2006).
RN [11]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-200; ASN-249; ASN-275; ASN-296;
RP ASN-300 AND ASN-306.
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 multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP VARIANTS [LARGE SCALE ANALYSIS] ASP-110 AND ILE-531.
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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [15]
RP INVOLVEMENT IN PLCA3, VARIANTS PLCA3 189-ARG--SER-572 DEL AND
RP 220-TYR--SER-572 DEL, CHARACTERIZATION OF VARIANT PLCA3 189-ARG--SER-572
RP DEL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANT PHE-294.
RX PubMed=29336782; DOI=10.1016/j.ajhg.2017.12.012;
RA Yang C.F., Lin S.P., Chiang C.P., Wu Y.H., H'ng W.S., Chang C.P.,
RA Chen Y.T., Wu J.Y.;
RT "Loss of GPNMB Causes Autosomal-Recessive Amyloidosis Cutis Dyschromica in
RT Humans.";
RL Am. J. Hum. Genet. 102:219-232(2018).
CC -!- FUNCTION: Could be a melanogenic enzyme. {ECO:0000250}.
CC -!- INTERACTION:
CC Q14956; P00533: EGFR; NbExp=3; IntAct=EBI-7250369, EBI-297353;
CC Q14956-1; P00533: EGFR; NbExp=2; IntAct=EBI-16191078, EBI-297353;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein {ECO:0000269|PubMed:16489096, ECO:0000269|PubMed:16609006}.
CC Melanosome membrane {ECO:0000269|PubMed:12643545,
CC ECO:0000269|PubMed:17081065}; Single-pass type I membrane protein
CC {ECO:0000305}. Early endosome membrane {ECO:0000269|PubMed:29336782};
CC Single-pass type I membrane protein {ECO:0000305}. Note=Identified by
CC mass spectrometry in melanosome fractions from stage I to stage IV.
CC {ECO:0000269|PubMed:17081065}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14956-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14956-2; Sequence=VSP_013001;
CC -!- TISSUE SPECIFICITY: Widely expressed, but very low expression, if any,
CC in the brain (PubMed:12609765, PubMed:16609006). Expressed in the
CC epidermis with higher levels in melanocytes compared with keratinocytes
CC and Langerhans cells (at protein level) (PubMed:29336782). Expressed in
CC peripheral blood, but not bone marrow mononuclear cells
CC (PubMed:12609765). Expressed in tissue macrophages, including liver
CC Kuppfer cells and lung alveolar macrophages, in podocytes and in some
CC cells of the ciliary body of the eye (at protein level)
CC (PubMed:16489096). May be overexpressed in various cancers, including
CC melanoma and glioblastoma multiforme (PubMed:7814155, PubMed:16489096,
CC PubMed:16609006). {ECO:0000269|PubMed:12609765,
CC ECO:0000269|PubMed:16489096, ECO:0000269|PubMed:16609006,
CC ECO:0000269|PubMed:29336782, ECO:0000269|PubMed:7814155}.
CC -!- INDUCTION: Up-regulated by G-CSF/CSF3 and M-CSF/CSF1 in bone marrow
CC mononuclear cells, hence up-regulation may be linked to
CC differentiation. {ECO:0000269|PubMed:12609765}.
CC -!- DISEASE: Note=Increased expression levels in glioblastoma multiforme
CC biopsy samples correlate with poor patient survival prognosis
CC (PubMed:16609006). Has been proposed as a potential target for
CC antibodies coupled to cytotoxic drugs in the context of cancer
CC immunotherapy, including that of melanoma (PubMed:16489096).
CC {ECO:0000269|PubMed:16489096, ECO:0000269|PubMed:16609006}.
CC -!- DISEASE: Amyloidosis, primary localized cutaneous, 3 (PLCA3)
CC [MIM:617920]: A primary amyloidosis characterized by localized
CC cutaneous amyloid deposition. This condition usually presents with
CC itching (especially on the lower legs) and visible changes of skin
CC hyperpigmentation and thickening that may be exacerbated by chronic
CC scratching and rubbing. Primary localized cutaneous amyloidosis is
CC often divided into macular and lichen subtypes although many affected
CC individuals often show both variants coexisting. Lichen amyloidosis
CC characteristically presents as a pruritic eruption of grouped
CC hyperkeratotic papules with a predilection for the shins, calves,
CC ankles and dorsa of feet and thighs. Papules may coalesce to form
CC hyperkeratotic plaques that can resemble lichen planus, lichen simplex
CC or nodular prurigo. Macular amyloidosis is characterized by small
CC pigmented macules that may merge to produce macular hyperpigmentation,
CC sometimes with a reticulate or rippled pattern. In macular and lichen
CC amyloidosis, amyloid is deposited in the papillary dermis in
CC association with grouped colloid bodies, thought to represent
CC degenerate basal keratinocytes. The amyloid deposits probably reflect a
CC combination of degenerate keratin filaments, serum amyloid P component,
CC and deposition of immunoglobulins. PLCA3 inheritance is autosomal
CC recessive. {ECO:0000269|PubMed:29336782}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the PMEL/NMB family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/GPNMBID40739ch7p15.html";
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DR EMBL; X76534; CAA54044.1; -; mRNA.
DR EMBL; AF322909; AAG42839.1; -; mRNA.
DR EMBL; AY359124; AAQ89481.1; -; mRNA.
DR EMBL; AC005082; AAP22336.1; -; Genomic_DNA.
DR EMBL; CH236948; EAL24259.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93782.1; -; Genomic_DNA.
DR EMBL; BC032783; AAH32783.1; -; mRNA.
DR CCDS; CCDS34610.1; -. [Q14956-1]
DR CCDS; CCDS5380.1; -. [Q14956-2]
DR PIR; I38065; I38065.
DR RefSeq; NP_001005340.1; NM_001005340.1. [Q14956-1]
DR RefSeq; NP_002501.1; NM_002510.2. [Q14956-2]
DR AlphaFoldDB; Q14956; -.
DR BioGRID; 115720; 19.
DR DIP; DIP-57606N; -.
DR IntAct; Q14956; 6.
DR MINT; Q14956; -.
DR STRING; 9606.ENSP00000371420; -.
DR ChEMBL; CHEMBL3712919; -.
DR DrugBank; DB05996; Glembatumumab vedotin.
DR GlyConnect; 1847; 27 N-Linked glycans (4 sites).
DR GlyGen; Q14956; 13 sites, 26 N-linked glycans (4 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q14956; -.
DR PhosphoSitePlus; Q14956; -.
DR BioMuta; GPNMB; -.
DR DMDM; 61252504; -.
DR EPD; Q14956; -.
DR jPOST; Q14956; -.
DR MassIVE; Q14956; -.
DR MaxQB; Q14956; -.
DR PaxDb; Q14956; -.
DR PeptideAtlas; Q14956; -.
DR PRIDE; Q14956; -.
DR ProteomicsDB; 60258; -. [Q14956-1]
DR ProteomicsDB; 60259; -. [Q14956-2]
DR ABCD; Q14956; 1 sequenced antibody.
DR Antibodypedia; 12086; 457 antibodies from 35 providers.
DR DNASU; 10457; -.
DR Ensembl; ENST00000258733.9; ENSP00000258733.5; ENSG00000136235.17. [Q14956-2]
DR Ensembl; ENST00000381990.6; ENSP00000371420.2; ENSG00000136235.17. [Q14956-1]
DR GeneID; 10457; -.
DR KEGG; hsa:10457; -.
DR MANE-Select; ENST00000258733.9; ENSP00000258733.5; NM_002510.3; NP_002501.1. [Q14956-2]
DR UCSC; uc003swb.4; human. [Q14956-1]
DR CTD; 10457; -.
DR DisGeNET; 10457; -.
DR GeneCards; GPNMB; -.
DR HGNC; HGNC:4462; GPNMB.
DR HPA; ENSG00000136235; Tissue enhanced (skin).
DR MalaCards; GPNMB; -.
DR MIM; 604368; gene.
DR MIM; 617920; phenotype.
DR neXtProt; NX_Q14956; -.
DR OpenTargets; ENSG00000136235; -.
DR Orphanet; 319635; Amyloidosis cutis dyschromia.
DR PharmGKB; PA28845; -.
DR VEuPathDB; HostDB:ENSG00000136235; -.
DR eggNOG; ENOG502QVWX; Eukaryota.
DR GeneTree; ENSGT00950000183188; -.
DR HOGENOM; CLU_017264_1_0_1; -.
DR InParanoid; Q14956; -.
DR OrthoDB; 833491at2759; -.
DR PhylomeDB; Q14956; -.
DR TreeFam; TF334865; -.
DR PathwayCommons; Q14956; -.
DR Reactome; R-HSA-8857538; PTK6 promotes HIF1A stabilization.
DR SignaLink; Q14956; -.
DR BioGRID-ORCS; 10457; 11 hits in 1073 CRISPR screens.
DR ChiTaRS; GPNMB; human.
DR GeneWiki; GPNMB; -.
DR GenomeRNAi; 10457; -.
DR Pharos; Q14956; Tbio.
DR PRO; PR:Q14956; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q14956; protein.
DR Bgee; ENSG00000136235; Expressed in upper leg skin and 202 other tissues.
DR ExpressionAtlas; Q14956; baseline and differential.
DR Genevisible; Q14956; HS.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042056; F:chemoattractant activity; NAS:ParkinsonsUK-UCL.
DR GO; GO:0008201; F:heparin binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0048018; F:receptor ligand activity; IMP:ParkinsonsUK-UCL.
DR GO; GO:0045545; F:syndecan binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; IMP:ParkinsonsUK-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0001818; P:negative regulation of cytokine production; IDA:ParkinsonsUK-UCL.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:ParkinsonsUK-UCL.
DR GO; GO:1901215; P:negative regulation of neuron death; IGI:ParkinsonsUK-UCL.
DR GO; GO:0050868; P:negative regulation of T cell activation; IMP:ParkinsonsUK-UCL.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0050918; P:positive chemotaxis; NAS:ParkinsonsUK-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:ParkinsonsUK-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IC:ParkinsonsUK-UCL.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045765; P:regulation of angiogenesis; NAS:ParkinsonsUK-UCL.
DR GO; GO:0034103; P:regulation of tissue remodeling; IDA:ParkinsonsUK-UCL.
DR GO; GO:0007165; P:signal transduction; IMP:ParkinsonsUK-UCL.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR045219; PKAT.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR11861; PTHR11861; 1.
DR Pfam; PF00801; PKD; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF49299; SSF49299; 1.
DR PROSITE; PS50093; PKD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amyloidosis; Cell membrane; Disease variant;
KW Endosome; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..572
FT /note="Transmembrane glycoprotein NMB"
FT /id="PRO_0000024709"
FT TOPO_DOM 23..498
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 240..327
FT /note="PKD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT REGION 320..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 64..66
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 320..336
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99P91"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 340..351
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12609765,
FT ECO:0000303|PubMed:7814155"
FT /id="VSP_013001"
FT VARIANT 110
FT /note="A -> D (in a breast cancer sample; somatic mutation;
FT dbSNP:rs755767733)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036262"
FT VARIANT 189..572
FT /note="Missing (in PLCA3; may be expressed at much lower
FT levels than wild-type protein; mislocalized to the
FT endoplasmic reticulum and nuclear envelope)"
FT /evidence="ECO:0000269|PubMed:29336782"
FT /id="VAR_080643"
FT VARIANT 195
FT /note="S -> C (in dbSNP:rs530436)"
FT /id="VAR_012076"
FT VARIANT 197
FT /note="N -> H (in dbSNP:rs530413)"
FT /id="VAR_012077"
FT VARIANT 220..572
FT /note="Missing (in PLCA3)"
FT /evidence="ECO:0000269|PubMed:29336782"
FT /id="VAR_080644"
FT VARIANT 294
FT /note="S -> F (in dbSNP:rs35499907)"
FT /evidence="ECO:0000269|PubMed:29336782"
FT /id="VAR_050603"
FT VARIANT 324
FT /note="P -> L (in dbSNP:rs35363287)"
FT /id="VAR_050604"
FT VARIANT 531
FT /note="S -> I (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036263"
FT VARIANT 538
FT /note="S -> R (in dbSNP:rs35878037)"
FT /id="VAR_050605"
FT CONFLICT 354
FT /note="A -> T (in Ref. 3; AAQ89481)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 572 AA; 63923 MW; 2465C12C2F0F3996 CRC64;
MECLYYFLGF LLLAARLPLD AAKRFHDVLG NERPSAYMRE HNQLNGWSSD ENDWNEKLYP
VWKRGDMRWK NSWKGGRVQA VLTSDSPALV GSNITFAVNL IFPRCQKEDA NGNIVYEKNC
RNEAGLSADP YVYNWTAWSE DSDGENGTGQ SHHNVFPDGK PFPHHPGWRR WNFIYVFHTL
GQYFQKLGRC SVRVSVNTAN VTLGPQLMEV TVYRRHGRAY VPIAQVKDVY VVTDQIPVFV
TMFQKNDRNS SDETFLKDLP IMFDVLIHDP SHFLNYSTIN YKWSFGDNTG LFVSTNHTVN
HTYVLNGTFS LNLTVKAAAP GPCPPPPPPP RPSKPTPSLA TTLKSYDSNT PGPAGDNPLE
LSRIPDENCQ INRYGHFQAT ITIVEGILEV NIIQMTDVLM PVPWPESSLI DFVVTCQGSI
PTEVCTIISD PTCEITQNTV CSPVDVDEMC LLTVRRTFNG SGTYCVNLTL GDDTSLALTS
TLISVPDRDP ASPLRMANSA LISVGCLAIF VTVISLLVYK KHKEYNPIEN SPGNVVRSKG
LSVFLNRAKA VFFPGNQEKD PLLKNQEFKG VS
