GPNMB_MOUSE
ID GPNMB_MOUSE Reviewed; 574 AA.
AC Q99P91; Q3U3R9; Q8BVV9; Q8BXL4; Q9QXA0;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Transmembrane glycoprotein NMB;
DE AltName: Full=DC-HIL;
DE AltName: Full=Dendritic cell-associated transmembrane protein;
DE AltName: Full=Osteoactivin;
DE Flags: Precursor;
GN Name=Gpnmb; Synonyms=Dchil, Hgfin, Nmb;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=11114299; DOI=10.1074/jbc.m008539200;
RA Shikano S., Bonkobara M., Zukas P.K., Ariizumi K.;
RT "Molecular cloning of a dendritic cell-associated transmembrane protein,
RT DC-HIL, that promotes RGD-dependent adhesion of endothelial cells through
RT recognition of heparan sulfate proteoglycans.";
RL J. Biol. Chem. 276:8125-8134(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=12638126; DOI=10.1016/s1567-133x(02)00012-1;
RA Bachner D., Schroder D., Gross G.;
RT "mRNA expression of the murine glycoprotein (transmembrane) nmb (Gpnmb)
RT gene is linked to the developing retinal pigment epithelium and iris.";
RL Gene Expr. Patterns 1:159-165(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Retina, and Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
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 TISSUE SPECIFICITY.
RX PubMed=17951401; DOI=10.1158/1541-7786.mcr-07-0119;
RA Rose A.A., Pepin F., Russo C., Abou Khalil J.E., Hallett M., Siegel P.M.;
RT "Osteoactivin promotes breast cancer metastasis to bone.";
RL Mol. Cancer Res. 5:1001-1014(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-546, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
CC -!- FUNCTION: Could be a melanogenic enzyme. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:Q14956}. Melanosome membrane; Single-
CC pass type I membrane protein {ECO:0000250|UniProtKB:Q14956}. Early
CC endosome membrane; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q14956}. Note=Identified by mass spectrometry in
CC melanosome fractions from stage I to stage IV.
CC {ECO:0000250|UniProtKB:Q14956}.
CC -!- TISSUE SPECIFICITY: May be up-regulated in bone metastatic breast
CC cancer cells. {ECO:0000269|PubMed:17951401}.
CC -!- DEVELOPMENTAL STAGE: At 9.5-10.5 dpc, highly expressed in the
CC developing eye, restricted to the outer layer of the retina. At
CC midgestation development, expression gets restricted to the forming
CC retinal pigment layer. At 18.5 dpc, expression remains high in the
CC retinal pigment epithelium and is also observed at the forming iris.
CC {ECO:0000269|PubMed:12638126}.
CC -!- SIMILARITY: Belongs to the PMEL/NMB family. {ECO:0000305}.
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DR EMBL; AF322054; AAK14240.1; -; mRNA.
DR EMBL; AJ251685; CAB65272.1; -; mRNA.
DR EMBL; AK044764; BAC32074.1; -; mRNA.
DR EMBL; AK076347; BAC36306.1; -; mRNA.
DR EMBL; AK150739; BAE29813.1; -; mRNA.
DR EMBL; AK154617; BAE32716.1; -; mRNA.
DR EMBL; AK170506; BAE41844.1; -; mRNA.
DR EMBL; AK171441; BAE42454.1; -; mRNA.
DR EMBL; AK171465; BAE42471.1; -; mRNA.
DR EMBL; AK171474; BAE42479.1; -; mRNA.
DR EMBL; AK171517; BAE42501.1; -; mRNA.
DR EMBL; BC026375; AAH26375.1; -; mRNA.
DR CCDS; CCDS20122.1; -.
DR RefSeq; NP_444340.3; NM_053110.4.
DR AlphaFoldDB; Q99P91; -.
DR BioGRID; 220244; 2.
DR IntAct; Q99P91; 2.
DR STRING; 10090.ENSMUSP00000031840; -.
DR GlyGen; Q99P91; 11 sites.
DR iPTMnet; Q99P91; -.
DR PhosphoSitePlus; Q99P91; -.
DR MaxQB; Q99P91; -.
DR PaxDb; Q99P91; -.
DR PRIDE; Q99P91; -.
DR ProteomicsDB; 271153; -.
DR Antibodypedia; 12086; 457 antibodies from 35 providers.
DR DNASU; 93695; -.
DR Ensembl; ENSMUST00000031840; ENSMUSP00000031840; ENSMUSG00000029816.
DR GeneID; 93695; -.
DR KEGG; mmu:93695; -.
DR UCSC; uc012elo.1; mouse.
DR CTD; 10457; -.
DR MGI; MGI:1934765; Gpnmb.
DR VEuPathDB; HostDB:ENSMUSG00000029816; -.
DR eggNOG; ENOG502QVWX; Eukaryota.
DR GeneTree; ENSGT00950000183188; -.
DR HOGENOM; CLU_017264_1_0_1; -.
DR InParanoid; Q99P91; -.
DR OMA; KRYKQYK; -.
DR OrthoDB; 833491at2759; -.
DR PhylomeDB; Q99P91; -.
DR TreeFam; TF334865; -.
DR Reactome; R-MMU-8857538; PTK6 promotes HIF1A stabilization.
DR BioGRID-ORCS; 93695; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Gpnmb; mouse.
DR PRO; PR:Q99P91; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q99P91; protein.
DR Bgee; ENSMUSG00000029816; Expressed in vault of skull and 107 other tissues.
DR ExpressionAtlas; Q99P91; baseline and differential.
DR Genevisible; Q99P91; MM.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008201; F:heparin binding; IDA:MGI.
DR GO; GO:0005178; F:integrin binding; IDA:MGI.
DR GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR GO; GO:0045545; F:syndecan binding; ISO:MGI.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
DR GO; GO:0001818; P:negative regulation of cytokine production; ISO:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:1901215; P:negative regulation of neuron death; ISO:MGI.
DR GO; GO:0050868; P:negative regulation of T cell activation; ISO:MGI.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:MGI.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:CACAO.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:ParkinsonsUK-UCL.
DR GO; GO:0034103; P:regulation of tissue remodeling; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007165; P:signal transduction; ISO:MGI.
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 Cell membrane; Endosome; Glycoprotein; Membrane; Phosphoprotein;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..574
FT /note="Transmembrane glycoprotein NMB"
FT /id="PRO_0000024710"
FT TOPO_DOM 23..502
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..574
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 250..338
FT /note="PKD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151"
FT REGION 320..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 558..560
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 320..351
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
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 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 312
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 463
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 471
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 36
FT /note="D -> N (in Ref. 1; AAK14240, 3; BAC32074 and 4;
FT AAH26375)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="P -> S (in Ref. 2; CAB65272)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..341
FT /note="SPP -> LPS (in Ref. 2; CAB65272)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="L -> M (in Ref. 3; BAC32074)"
FT /evidence="ECO:0000305"
FT CONFLICT 541
FT /note="K -> E (in Ref. 3; BAC32074)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 574 AA; 63676 MW; B6AE99DD5DB7C6D0 CRC64;
MESLCGVLGF LLLAAGLPLQ AAKRFRDVLG HEQYPDHMRE HNQLRGWSSD ENEWDEHLYP
VWRRGDGRWK DSWEGGRVQA VLTSDSPALV GSNITFVVNL VFPRCQKEDA NGNIVYEKNC
RNDLGLTSDL HVYNWTAGAD DGDWEDGTSR SQHLRFPDRR PFPRPHGWKK WSFVYVFHTL
GQYFQKLGRC SARVSINTVN LTAGPQVMEV TVFRRYGRAY IPISKVKDVY VITDQIPVFV
TMSQKNDRNL SDEIFLRDLP IVFDVLIHDP SHFLNDSAIS YKWNFGDNTG LFVSNNHTLN
HTYVLNGTFN LNLTVQTAVP GPCPPPSPST PPPPSTPPSP PPSPLPTLST PSPSLMPTGY
KSMELSDISN ENCRINRYGY FRATITIVEG ILEVSIMQIA DVPMPTPQPA NSLMDFTVTC
KGATPMEACT IISDPTCQIA QNRVCSPVAV DGLCLLSVRR AFNGSGTYCV NFTLGDDASL
ALTSTLISIP GKDPDSPLRA VNGVLISIGC LAVLVTMVTI LLYKKHKAYK PIGNCPRNTV
KGKGLSVLLS HAKAPFFRGD QEKDPLLQDK PRTL
