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Database: UniProt
Entry: TPRA1_MOUSE
LinkDB: TPRA1_MOUSE
Original site: TPRA1_MOUSE 
ID   TPRA1_MOUSE             Reviewed;         369 AA.
AC   Q99MU1; Q80UD9; Q8C240; Q91Z36; Q9Z112;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Transmembrane protein adipocyte-associated 1;
DE   AltName: Full=Integral membrane protein GPR175;
DE   AltName: Full=TPRA40;
DE   AltName: Full=Transmembrane domain protein of 40 kDa regulated in adipocytes;
GN   Name=Tpra1; Synonyms=Gpr175, Tpra40;
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 [MRNA], INDUCTION, AND TISSUE SPECIFICITY.
RC   TISSUE=Adipocyte;
RX   PubMed=10342878; DOI=10.1210/endo.140.6.6830;
RA   Yang H., Egan J.M., Rodgers B.D., Bernier M., Montrose-Rafizadeh C.;
RT   "Differential expression of a novel seven transmembrane domain protein in
RT   epididymal fat from aged and diabetic mice.";
RL   Endocrinology 140:2859-2867(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Lung, and Spleen;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Mammary gland;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 25-148.
RX   PubMed=12679517; DOI=10.1073/pnas.0230374100;
RA   Vassilatis D.K., Hohmann J.G., Zeng H., Li F., Ranchalis J.E.,
RA   Mortrud M.T., Brown A., Rodriguez S.S., Weller J.R., Wright A.C.,
RA   Bergmann J.E., Gaitanaris G.A.;
RT   "The G protein-coupled receptor repertoires of human and mouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:4903-4908(2003).
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Ubiquitous, with higher levels in heart, brain,
CC       lung, liver and kidney. {ECO:0000269|PubMed:10342878}.
CC   -!- INDUCTION: Induced during adipocytes differentiation and in white fat
CC       from aged and diabetics mice. {ECO:0000269|PubMed:10342878}.
CC   -!- SIMILARITY: Belongs to the UPF0359 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD15788.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF051098; AAD15788.1; ALT_FRAME; mRNA.
DR   EMBL; AK089317; BAC40839.1; -; mRNA.
DR   EMBL; AK164913; BAE37962.1; -; mRNA.
DR   EMBL; AK172045; BAE42796.1; -; mRNA.
DR   EMBL; BC010244; AAH10244.1; -; mRNA.
DR   EMBL; BC028977; AAH28977.1; -; mRNA.
DR   EMBL; AY255531; AAO85043.1; -; mRNA.
DR   CCDS; CCDS39555.1; -.
DR   RefSeq; NP_036036.2; NM_011906.2.
DR   RefSeq; XP_006506124.1; XM_006506061.2.
DR   RefSeq; XP_006506125.1; XM_006506062.2.
DR   RefSeq; XP_006506126.1; XM_006506063.2.
DR   AlphaFoldDB; Q99MU1; -.
DR   STRING; 10090.ENSMUSP00000063042; -.
DR   GlyCosmos; Q99MU1; 2 sites, No reported glycans.
DR   GlyGen; Q99MU1; 2 sites.
DR   PhosphoSitePlus; Q99MU1; -.
DR   MaxQB; Q99MU1; -.
DR   PaxDb; 10090-ENSMUSP00000063042; -.
DR   ProteomicsDB; 259504; -.
DR   Antibodypedia; 17215; 306 antibodies from 30 providers.
DR   Ensembl; ENSMUST00000055022.15; ENSMUSP00000063042.9; ENSMUSG00000002871.15.
DR   Ensembl; ENSMUST00000203185.3; ENSMUSP00000145168.2; ENSMUSG00000002871.15.
DR   Ensembl; ENSMUST00000204765.3; ENSMUSP00000145050.2; ENSMUSG00000002871.15.
DR   GeneID; 24100; -.
DR   KEGG; mmu:24100; -.
DR   UCSC; uc009cvy.1; mouse.
DR   AGR; MGI:1345190; -.
DR   CTD; 131601; -.
DR   MGI; MGI:1345190; Tpra1.
DR   VEuPathDB; HostDB:ENSMUSG00000002871; -.
DR   eggNOG; KOG4536; Eukaryota.
DR   GeneTree; ENSGT00390000016807; -.
DR   HOGENOM; CLU_056255_0_0_1; -.
DR   InParanoid; Q99MU1; -.
DR   OMA; DRWKSIN; -.
DR   OrthoDB; 2916831at2759; -.
DR   PhylomeDB; Q99MU1; -.
DR   TreeFam; TF314072; -.
DR   BioGRID-ORCS; 24100; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Tpra1; mouse.
DR   PRO; PR:Q99MU1; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q99MU1; Protein.
DR   Bgee; ENSMUSG00000002871; Expressed in lip and 250 other cell types or tissues.
DR   ExpressionAtlas; Q99MU1; baseline and differential.
DR   Genevisible; Q99MU1; MM.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR   GO; GO:0040016; P:embryonic cleavage; IMP:MGI.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:1901991; P:negative regulation of mitotic cell cycle phase transition; IMP:MGI.
DR   InterPro; IPR018781; TPRA1/CAND2/CAND8.
DR   PANTHER; PTHR15876; TRANSMEMBRANE PROTEIN ADIPOCYTE-ASSOCIATED 1; 1.
DR   PANTHER; PTHR15876:SF8; TRANSMEMBRANE PROTEIN ADIPOCYTE-ASSOCIATED 1; 1.
DR   Pfam; PF10160; Tmemb_40; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..369
FT                   /note="Transmembrane protein adipocyte-associated 1"
FT                   /id="PRO_0000076100"
FT   TRANSMEM        45..65
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        237..257
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        329
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   369 AA;  40578 MW;  BACB74C431312443 CRC64;
     MASLQEANGS TAWPPPTASN ISEPHQCLLL LYEDIGSSRV RYWDLLLLIP NVLFFIFLLW
     KLPLARAKIR VTSSPIFITF YILVFVVALV GIARAVVSMT VSASDAATVA DKILWEITRF
     FLLAIELSVI ILGLAFGHLE SKSSIKRVLA ITTVLSLAYS VTQGTLEILY PDSHLSAEDF
     NIYGHGGRQF WLVSSCFFFL VYSLVVILPK TPLKERVSLP SRRSFYVYAG ILATLNLLQG
     LGSALLCANI IVGLCCVDAT TFLYFSFFAP LIYVAFLRGF FGSEPKILFS YKCQVDEAEE
     PDMHLPQPYA VARREGIESA GPACASAANY SSTQFDSAGV AYLDDIASMP CHTGSINSTD
     SERWKAINA
//
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