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GP107_MOUSE
ID   GP107_MOUSE             Reviewed;         551 AA.
AC   Q8BUV8; Q6ZPL4; Q8BM58; Q8BMN6; Q8BTW1;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Protein GPR107;
DE   Flags: Precursor;
GN   Name=Gpr107; Synonyms=Kiaa1624;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryoid bodies, Pituitary, and Thymus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-551.
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC   and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   SUBCELLULAR LOCATION.
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 (By similarity).
CC       Involved in blood sugar regulation through the induction of glucagon in
CC       response to low glucose (By similarity).
CC       {ECO:0000250|UniProtKB:D3ZWZ9}.
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   -!- 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; AK030433; BAC26961.1; -; mRNA.
DR   EMBL; AK034815; BAC28840.1; -; mRNA.
DR   EMBL; AK082237; BAC38445.1; -; mRNA.
DR   EMBL; AK088544; BAC40414.1; -; mRNA.
DR   EMBL; BC092231; AAH92231.1; -; mRNA.
DR   EMBL; AK129407; BAC98217.1; -; mRNA.
DR   CCDS; CCDS15895.1; -.
DR   RefSeq; NP_848875.2; NM_178760.4.
DR   AlphaFoldDB; Q8BUV8; -.
DR   BioGRID; 234940; 1.
DR   STRING; 10090.ENSMUSP00000056739; -.
DR   GlyGen; Q8BUV8; 2 sites.
DR   iPTMnet; Q8BUV8; -.
DR   PhosphoSitePlus; Q8BUV8; -.
DR   EPD; Q8BUV8; -.
DR   jPOST; Q8BUV8; -.
DR   MaxQB; Q8BUV8; -.
DR   PaxDb; Q8BUV8; -.
DR   PRIDE; Q8BUV8; -.
DR   ProteomicsDB; 271423; -.
DR   Antibodypedia; 31467; 153 antibodies from 26 providers.
DR   Ensembl; ENSMUST00000056433; ENSMUSP00000056739; ENSMUSG00000000194.
DR   GeneID; 277463; -.
DR   KEGG; mmu:277463; -.
DR   UCSC; uc008jdp.2; mouse.
DR   CTD; 57720; -.
DR   MGI; MGI:2139054; Gpr107.
DR   VEuPathDB; HostDB:ENSMUSG00000000194; -.
DR   eggNOG; KOG2569; Eukaryota.
DR   GeneTree; ENSGT00940000160451; -.
DR   HOGENOM; CLU_020277_4_1_1; -.
DR   InParanoid; Q8BUV8; -.
DR   OMA; PQGEWES; -.
DR   OrthoDB; 1427067at2759; -.
DR   PhylomeDB; Q8BUV8; -.
DR   TreeFam; TF314804; -.
DR   BioGRID-ORCS; 277463; 2 hits in 72 CRISPR screens.
DR   PRO; PR:Q8BUV8; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8BUV8; protein.
DR   Bgee; ENSMUSG00000000194; Expressed in spermatocyte and 224 other tissues.
DR   ExpressionAtlas; Q8BUV8; baseline and differential.
DR   Genevisible; Q8BUV8; MM.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IDA:MGI.
DR   GO; GO:0005769; C:early endosome; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032050; F:clathrin heavy chain binding; IDA:MGI.
DR   GO; GO:0072583; P:clathrin-dependent endocytosis; IMP:MGI.
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   Phosphoprotein; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..551
FT                   /note="Protein GPR107"
FT                   /id="PRO_0000021341"
FT   TOPO_DOM        40..262
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..292
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        293..313
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        314..336
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358..367
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        389..401
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        423..449
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        450..470
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        471..475
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        476..495
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        496..551
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         537
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
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"
FT   DISULFID        106..226
FT                   /evidence="ECO:0000250|UniProtKB:Q5VW38"
FT   CONFLICT        127
FT                   /note="I -> L (in Ref. 1; BAC38445)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="Q -> R (in Ref. 1; BAC40414 and 3; BAC98217)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        532
FT                   /note="K -> R (in Ref. 1; BAC28840)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  62056 MW;  B79DBE97D56BD2B6 CRC64;
     MAVPVPLGRF GSFCLRLLRL LALLELLVHP VLGRVHHLAL KDDVRHKVHL NTFGFFKDGY
     MVVNVSSLSV NEPEGATDKD AEIGFSLDRT KNDGFSSYLD EDVNYCILKK KSMSSVTLVI
     LDISGSIVKV RSPPEAGKQL PEIVFSKDEK ILSQSQEPAV SSNPKDSEAR RTLDGFKAGR
     STVDSKAITE RSFSIHKNDG VVSFQFFFNI STDDQEGLYS LYFHKCSGNN VKPGEQASFS
     LNIAITEKNP NSYLSAGEIP LPKLYVSMAL FFFLSGTIWI HILRKRRNDV FKIHWLMAAL
     PFTKSLSLVF HAIDYHYISS QGFPIEGWAV VYYITHLLKG ALLFITIALI GTGWAFIKHI
     LSDKDKKIFM IVIPLQVLAN VAYIIIESTE EGTTEYGLWK DSLFLVDLLC CGAILFPVVW
     SIRHLQEASA TDGKAAINLA KLRLFRHYYV LIVCYIYFTR IIAFLLKFAV PFQWKWLYQL
     LDETATLVFF VLTGYKFRPA SDNPYLQLSQ EDDDLEMESV VTTSGVMENM KKVKKVSNGA
     VEPQGSWEGT A
 
 
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