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GP174_MOUSE
ID   GP174_MOUSE             Reviewed;         335 AA.
AC   Q3U507;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Probable G-protein coupled receptor 174;
GN   Name=Gpr174; Synonyms=Gm376;
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, and NOD; TISSUE=Spleen, 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   TISSUE SPECIFICITY.
RX   PubMed=23178570; DOI=10.1016/j.bbrc.2012.11.046;
RA   Sugita K., Yamamura C., Tabata K., Fujita N.;
RT   "Expression of orphan G-protein coupled receptor GPR174 in CHO cells
RT   induced morphological changes and proliferation delay via increasing
RT   intracellular cAMP.";
RL   Biochem. Biophys. Res. Commun. 430:190-195(2013).
CC   -!- FUNCTION: Putative receptor for purines coupled to G-proteins.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Expressed in spleen and, at low levels, in brain.
CC       {ECO:0000269|PubMed:23178570}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR   EMBL; AK153611; BAE32116.1; -; mRNA.
DR   EMBL; AK153950; BAE32273.1; -; mRNA.
DR   EMBL; AK156069; BAE33570.1; -; mRNA.
DR   EMBL; AK171832; BAE42688.1; -; mRNA.
DR   CCDS; CCDS30348.1; -.
DR   RefSeq; NP_001028423.1; NM_001033251.4.
DR   RefSeq; NP_001171252.1; NM_001177781.1.
DR   RefSeq; NP_001171253.1; NM_001177782.1.
DR   AlphaFoldDB; Q3U507; -.
DR   SMR; Q3U507; -.
DR   STRING; 10090.ENSMUSP00000098852; -.
DR   ChEMBL; CHEMBL3813587; -.
DR   GlyGen; Q3U507; 3 sites.
DR   iPTMnet; Q3U507; -.
DR   PhosphoSitePlus; Q3U507; -.
DR   PaxDb; Q3U507; -.
DR   PRIDE; Q3U507; -.
DR   ProteomicsDB; 263387; -.
DR   Antibodypedia; 14113; 262 antibodies from 28 providers.
DR   Ensembl; ENSMUST00000101294; ENSMUSP00000098852; ENSMUSG00000073008.
DR   Ensembl; ENSMUST00000117310; ENSMUSP00000112808; ENSMUSG00000073008.
DR   Ensembl; ENSMUST00000118820; ENSMUSP00000113032; ENSMUSG00000073008.
DR   Ensembl; ENSMUST00000120971; ENSMUSP00000112974; ENSMUSG00000073008.
DR   Ensembl; ENSMUST00000178838; ENSMUSP00000137372; ENSMUSG00000073008.
DR   GeneID; 213439; -.
DR   KEGG; mmu:213439; -.
DR   UCSC; uc009ucd.2; mouse.
DR   CTD; 84636; -.
DR   MGI; MGI:2685222; Gpr174.
DR   VEuPathDB; HostDB:ENSMUSG00000073008; -.
DR   eggNOG; ENOG502QSC0; Eukaryota.
DR   GeneTree; ENSGT01030000234518; -.
DR   HOGENOM; CLU_009579_8_2_1; -.
DR   InParanoid; Q3U507; -.
DR   OMA; LYCSWKT; -.
DR   PhylomeDB; Q3U507; -.
DR   TreeFam; TF350009; -.
DR   BioGRID-ORCS; 213439; 3 hits in 72 CRISPR screens.
DR   ChiTaRS; Gpr174; mouse.
DR   PRO; PR:Q3U507; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q3U507; protein.
DR   Bgee; ENSMUSG00000073008; Expressed in peripheral lymph node and 41 other tissues.
DR   Genevisible; Q3U507; MM.
DR   GO; GO:0034451; C:centriolar satellite; ISO:MGI.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0045125; F:bioactive lipid receptor activity; IMP:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0051482; P:positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway; IBA:GO_Central.
DR   GO; GO:0035025; P:positive regulation of Rho protein signal transduction; IBA:GO_Central.
DR   GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00237; GPCRRHODOPSN.
DR   PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW   Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..335
FT                   /note="Probable G-protein coupled receptor 174"
FT                   /id="PRO_0000069655"
FT   TOPO_DOM        1..27
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..53
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        75..91
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..112
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..134
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        135..155
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        156..182
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        183..203
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        204..231
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        232..252
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        253..268
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..335
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        8
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        91..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ   SEQUENCE   335 AA;  38761 MW;  E1125388C0A7923D CRC64;
     MTDNFTCNKT DGDNTDFRYF IYAVTYTVIL VPGLIGNILA LWVFYGYMKE TKRAVVFMIN
     LAIADLLQIL SLPLRIFYYL NHDWPFGPGL CMFCFYLKYV NMYASIYFLV CISVRRFWFL
     MYPFRFNDCK QKYDLYISII GWLIICLACL LFPLLRTNDD TPGNRTKCFV DLPIRNVNLA
     QSVAMITIGE VVGFVTPLMI VLYCTWKTAL SLQNKYPISQ HLGEKKKALK MILTCAGVFL
     VCFVPYHFSF PLDFLVKSNE IKSCFARRVI LIFHSVALCL ASLNSCLDPV IYYFTTNEFR
     RRLSRQDLPD NIQLHTKSYK IASNHATSTV AAELC
 
 
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