GPNMB_RAT
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 03-AUG-2022, entry version 101.
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}.
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DR EMBL; BC061725; AAH61725.1; -; mRNA.
DR AlphaFoldDB; Q6P7C7; -.
DR STRING; 10116.ENSRNOP00000011945; -.
DR GlyGen; Q6P7C7; 11 sites.
DR PaxDb; Q6P7C7; -.
DR PRIDE; Q6P7C7; -.
DR Ensembl; ENSRNOT00000104789; ENSRNOP00000076498; ENSRNOG00000008816.
DR UCSC; RGD:71008; rat.
DR RGD; 71008; Gpnmb.
DR eggNOG; ENOG502QVWX; Eukaryota.
DR GeneTree; ENSGT00950000183188; -.
DR HOGENOM; CLU_017264_1_0_1; -.
DR InParanoid; Q6P7C7; -.
DR OMA; KRYKQYK; -.
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 tissues.
DR Genevisible; Q6P7C7; RN.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0033162; C:melanosome membrane; IEA:UniProtKB-SubCell.
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:1901215; P:negative regulation of neuron death; 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 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 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
