ID GPNMB_RAT Reviewed; 572 AA. AC Q6P7C7; DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 24-JAN-2024, entry version 107. DE RecName: Full=Transmembrane glycoprotein NMB; DE Flags: Precursor; GN Name=Gpnmb; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Prostate; 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). 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 -!- SIMILARITY: Belongs to the PMEL/NMB family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC061725; AAH61725.1; -; mRNA. DR AlphaFoldDB; Q6P7C7; -. DR STRING; 10116.ENSRNOP00000011945; -. DR GlyCosmos; Q6P7C7; 11 sites, No reported glycans. DR GlyGen; Q6P7C7; 11 sites. DR PhosphoSitePlus; Q6P7C7; -. DR PaxDb; 10116-ENSRNOP00000011945; -. DR Ensembl; ENSRNOT00000104789.1; ENSRNOP00000076498.1; ENSRNOG00000008816.5. DR Ensembl; ENSRNOT00055047069; ENSRNOP00055038686; ENSRNOG00055027200. DR Ensembl; ENSRNOT00060041093; ENSRNOP00060034022; ENSRNOG00060023675. DR Ensembl; ENSRNOT00065024342; ENSRNOP00065019010; ENSRNOG00065014717. DR UCSC; RGD:71008; rat. DR AGR; RGD:71008; -. DR RGD; 71008; Gpnmb. DR eggNOG; ENOG502QVWX; Eukaryota. DR GeneTree; ENSGT00950000183188; -. DR HOGENOM; CLU_017264_1_0_1; -. DR InParanoid; Q6P7C7; -. DR OMA; HGWRKWN; -. DR PhylomeDB; Q6P7C7; -. DR TreeFam; TF334865; -. DR Reactome; R-RNO-8857538; PTK6 promotes HIF1A stabilization. DR PRO; PR:Q6P7C7; -. DR Proteomes; UP000002494; Chromosome 4. DR Bgee; ENSRNOG00000008816; Expressed in lung and 20 other cell types or tissues. DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD. DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; ISO:RGD. DR GO; GO:0005886; C:plasma membrane; ISO:RGD. DR GO; GO:0008201; F:heparin binding; ISO:RGD. DR GO; GO:0005178; F:integrin binding; ISO:RGD. DR GO; GO:0048018; F:receptor ligand activity; ISO:RGD. DR GO; GO:0045545; F:syndecan binding; ISO:RGD. DR GO; GO:0030282; P:bone mineralization; IEP:RGD. DR GO; GO:0007155; P:cell adhesion; ISO:RGD. DR GO; GO:0007267; P:cell-cell signaling; ISO:RGD. DR GO; GO:0001818; P:negative regulation of cytokine production; ISO:RGD. DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:RGD. DR GO; GO:0050868; P:negative regulation of T cell activation; ISO:RGD. DR GO; GO:0042130; P:negative regulation of T cell proliferation; ISO:RGD. DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; ISO:RGD. DR GO; GO:0001649; P:osteoblast differentiation; IEP:RGD. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:RGD. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD. DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:RGD. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD. DR GO; GO:0034103; P:regulation of tissue remodeling; ISO:RGD. DR GO; GO:0007165; P:signal transduction; ISO:RGD. DR CDD; cd00146; PKD; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR045219; PKAT. DR InterPro; IPR046846; PKAT_KLD. DR InterPro; IPR022409; PKD/Chitinase_dom. DR InterPro; IPR000601; PKD_dom. DR InterPro; IPR035986; PKD_dom_sf. DR PANTHER; PTHR11861; MELANOCYTE PROTEIN PMEL 17-RELATED; 1. DR PANTHER; PTHR11861:SF11; TRANSMEMBRANE GLYCOPROTEIN NMB; 1. DR Pfam; PF20433; PKAT_KLD; 1. DR Pfam; PF18911; PKD_4; 1. DR SMART; SM00089; PKD; 1. DR SUPFAM; SSF49299; PKD domain; 1. DR PROSITE; PS50093; PKD; 1. DR Genevisible; Q6P7C7; RN. PE 2: Evidence at transcript 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..572 FT /note="Transmembrane glycoprotein NMB" FT /id="PRO_0000024711" FT TOPO_DOM 23..500 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 501..521 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 522..572 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DOMAIN 251..338 FT /note="PKD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00151" FT REGION 321..359 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 556..558 FT /note="Cell attachment site" FT /evidence="ECO:0000255" FT COMPBIAS 321..349 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 544 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 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 461 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 469 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" SQ SEQUENCE 572 AA; 63731 MW; 99854F7773FF946C CRC64; MESLCGVLVF LLLAAGLPLQ AAKRFRDVLG HEQYPDHMRE NNQLRGWSSD ENEWDEQLYP VWRRGEGRWK DSWEGGRVQA ALTSDSPALV GSNITFVVNL VFPRCQKEDA NGNIVYERNC RSDLELASDP YVYNWTTGAD DEDWEDSTSQ GQHLRFPDGK PFPRPHGRKK WNFVYVFHTL GQYFQKLGRC SARVSINTVN LTVGPQVMEV IVFRRHGRAY IPISKVKDVY VITDQIPIFV TMYQKNDRNS SDETFLRDLP IFFDVLIHDP SHFLNYSAIS YKWNFGDNTG LFVSNNHTLN HTYVLNGTFN FNLTVQTAVP GPCPSPTPSP SSSTSPSPAS SPSPTLSTPS PSLMPTGHKS MELSDISNEN CRINRYGYFR ATITIVDGIL EVNIIQVADV PIPTPQPDNS LMDFIVTCKG ATPTEACTII SDPTCQIAQN RVCSPVAVDE LCLLSVRRAF NGSGTYCVNF TLGDDASLAL TSALISIPGK DLGSPLRTVN GVLISIGCLA MFVTMVTILL YKKHKTYKPI GNCTRNVVKG KGLSVFLSHA KAPFSRGDRE KDPLLQDKPW ML //