GP107_RAT
ID GP107_RAT Reviewed; 551 AA.
AC D3ZWZ9;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Protein GPR107;
DE Flags: Precursor;
GN Name=Gpr107;
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 GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22933024; DOI=10.1152/ajpregu.00336.2012;
RA Yosten G.L., Redlinger L.J., Samson W.K.;
RT "Evidence for an interaction of neuronostatin with the orphan G protein-
RT coupled receptor, GPR107.";
RL Am. J. Physiol. 303:R941-R949(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26561648; DOI=10.1152/ajpregu.00369.2014;
RA Elrick M.M., Samson W.K., Corbett J.A., Salvatori A.S., Stein L.M.,
RA Kolar G.R., Naatz A., Yosten G.L.;
RT "Neuronostatin acts via GPR107 to increase cAMP-independent PKA
RT phosphorylation and proglucagon mRNA accumulation in pancreatic alpha-
RT cells.";
RL Am. J. Physiol. 310:R143-R155(2016).
CC -!- FUNCTION: Has been proposed to act as a receptor for neuronostatin, a
CC peptide derived from the somatostatin/SST precursor (PubMed:22933024,
CC PubMed:26561648). Involved in blood sugar regulation through the
CC induction of glucagon in response to low glucose (PubMed:26561648).
CC {ECO:0000269|PubMed:22933024, ECO:0000269|PubMed:26561648}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:26561648};
CC Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000250|UniProtKB:Q5VW38}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:22933024,
CC PubMed:26561648). Not detected in the duodenum, nor in the exocrine
CC pancreas (PubMed:22933024). {ECO:0000269|PubMed:22933024,
CC ECO:0000269|PubMed:26561648}.
CC -!- PTM: Cleaved by FURIN to yield two fragments that remain associated via
CC a disulfide bond. {ECO:0000250|UniProtKB:Q5VW38}.
CC -!- SIMILARITY: Belongs to the LU7TM family. {ECO:0000305}.
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DR EMBL; AABR07051408; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474001; EDL93279.1; -; Genomic_DNA.
DR RefSeq; NP_001101298.1; NM_001107828.1.
DR AlphaFoldDB; D3ZWZ9; -.
DR STRING; 10116.ENSRNOP00000037572; -.
DR GlyGen; D3ZWZ9; 2 sites.
DR iPTMnet; D3ZWZ9; -.
DR PhosphoSitePlus; D3ZWZ9; -.
DR PaxDb; D3ZWZ9; -.
DR PeptideAtlas; D3ZWZ9; -.
DR PRIDE; D3ZWZ9; -.
DR Ensembl; ENSRNOT00000037742; ENSRNOP00000037572; ENSRNOG00000023589.
DR GeneID; 311857; -.
DR KEGG; rno:311857; -.
DR UCSC; RGD:1305882; rat.
DR CTD; 57720; -.
DR RGD; 1305882; Gpr107.
DR eggNOG; KOG2569; Eukaryota.
DR GeneTree; ENSGT00940000160451; -.
DR HOGENOM; CLU_020277_4_1_1; -.
DR InParanoid; D3ZWZ9; -.
DR OMA; PQGEWES; -.
DR OrthoDB; 1427067at2759; -.
DR PhylomeDB; D3ZWZ9; -.
DR TreeFam; TF314804; -.
DR PRO; PR:D3ZWZ9; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000023589; Expressed in skeletal muscle tissue and 20 other tissues.
DR GO; GO:0030136; C:clathrin-coated vesicle; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032050; F:clathrin heavy chain binding; ISO:RGD.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISO:RGD.
DR InterPro; IPR009637; GPR107/GPR108-like.
DR PANTHER; PTHR21229; PTHR21229; 1.
DR Pfam; PF06814; Lung_7-TM_R; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Golgi apparatus; Membrane;
KW Receptor; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..551
FT /note="Protein GPR107"
FT /evidence="ECO:0000255"
FT /id="PRO_5014087767"
FT TOPO_DOM 34..262
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..336
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..367
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 368..388
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 389..401
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 444..466
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 467..475
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 476..495
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 496..551
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 127..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 209
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 551 AA; 62002 MW; B7C9B432CC541DD5 CRC64;
MAVRVPLGCT GSFCPRLLPL LALLELLVDP SLGRVHHLAL KDDVRHKVHL NTFGFFKDGY
MVVNISSLSV NEPEGVKDKD TEIGFSLDRT KNDGFSSYLD EDVNYCILKK KSMSSVTLLI
LDISGSGVKV RSPPEAGKQL PEIVFSKDEK VPSRSQEPAV SSNPKDSKVQ RTPDGSKAQR
STVDSKTIAE KFFSIHKNDG AVSFQFFFNI STSDQEGLYS LYFHKCPSSK LRSGEQVSFS
LNIDITEKNP DSYLSAGEIP LPKLYVSMAL LFFLSGTVWI HILRKRRNDV FKIHWLMAAL
PFTKSLSLVF HAIDYHYISS QGFPIEGWAV VYYITHLLKG ALLFITIALI GTGWAFIKHI
LSDKDKKIFM IVIPLQVLAN VAYIIIESTE EGTTEYGLWK DSLFLVDLLC CGAILFPVVW
SIRHLQEASA TDGKAAINLA KLKLFRHYYV LIVCYIYFTR IIAFLLKFAV PFQWKWLYQL
LDETATLVFF VLTGYKFRPA SDNPYLQLSQ EEDDLEMESV VTTSGVMENM KKVKKVSNGA
VEPQGSWEGT A
