ATRAP_MOUSE
ID ATRAP_MOUSE Reviewed; 161 AA.
AC Q9WVK0; B2KFL8; Q3U7X6; Q9D8Z8; Q9D940;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Type-1 angiotensin II receptor-associated protein;
DE AltName: Full=AT1 receptor-associated protein;
GN Name=Agtrap; Synonyms=Atrap;
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], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH AGTR1.
RC STRAIN=DBA/2J; TISSUE=Kidney;
RX PubMed=10358057; DOI=10.1074/jbc.274.24.17058;
RA Daviet L., Lehtonen J.Y.A., Tamura K., Griese D.P., Horiuchi M., Dzau V.J.;
RT "Cloning and characterization of ATRAP, a novel protein that interacts with
RT the angiotensin II type 1 receptor.";
RL J. Biol. Chem. 274:17058-17062(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone, Bone marrow, and Pancreas;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor;
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 [6]
RP FUNCTION.
RX PubMed=15757644; DOI=10.1016/j.febslet.2005.01.068;
RA Tanaka Y., Tamura K., Koide Y., Sakai M., Tsurumi Y., Noda Y., Umemura M.,
RA Ishigami T., Uchino K., Kimura K., Horiuchi M., Umemura S.;
RT "The novel angiotensin II type 1 receptor (AT1R)-associated protein ATRAP
RT downregulates AT1R and ameliorates cardiomyocyte hypertrophy.";
RL FEBS Lett. 579:1579-1586(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, 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).
CC -!- FUNCTION: Appears to be a negative regulator of type-1 angiotensin II
CC receptor-mediated signaling by regulating receptor internalization as
CC well as mechanism of receptor desensitization such as phosphorylation.
CC Induces also a decrease in angiotensin II-stimulated transcriptional
CC activity. May play a role of negative regulator in cardiomyocyte
CC hypertrophy induced by angiotensin II through an inhibition of p38
CC mitogen-activated protein kinase pathway. {ECO:0000269|PubMed:10358057,
CC ECO:0000269|PubMed:15757644}.
CC -!- SUBUNIT: Interacts with RACK1 (By similarity), and with the C-terminal
CC region of AGTR1. {ECO:0000250, ECO:0000269|PubMed:10358057}.
CC -!- INTERACTION:
CC Q9WVK0; P29754: Agtr1a; NbExp=5; IntAct=EBI-645964, EBI-765178;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cytoplasmic
CC vesicle membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Note=Present in perinuclear vesicular membranes,
CC Endoplasmic reticulum, Golgi and endocytic vesicles. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous but more abundant in kidney, testis and
CC heart. {ECO:0000269|PubMed:10358057}.
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DR EMBL; AF102548; AAD25997.1; -; mRNA.
DR EMBL; AK007383; BAB25001.1; -; mRNA.
DR EMBL; AK007502; BAB25074.1; -; mRNA.
DR EMBL; AK036598; BAC29501.1; -; mRNA.
DR EMBL; AK152467; BAE31243.1; -; mRNA.
DR EMBL; CU207376; CAQ51920.1; -; Genomic_DNA.
DR EMBL; AL606929; CAM14899.1; -; Genomic_DNA.
DR EMBL; CH466594; EDL14800.1; -; Genomic_DNA.
DR EMBL; BC046820; AAH46820.1; -; mRNA.
DR EMBL; BC057196; AAH57196.1; -; mRNA.
DR CCDS; CCDS18930.1; -.
DR RefSeq; NP_033772.2; NM_009642.5.
DR AlphaFoldDB; Q9WVK0; -.
DR BioGRID; 198032; 2.
DR IntAct; Q9WVK0; 2.
DR MINT; Q9WVK0; -.
DR STRING; 10090.ENSMUSP00000030865; -.
DR iPTMnet; Q9WVK0; -.
DR PhosphoSitePlus; Q9WVK0; -.
DR MaxQB; Q9WVK0; -.
DR PaxDb; Q9WVK0; -.
DR PeptideAtlas; Q9WVK0; -.
DR PRIDE; Q9WVK0; -.
DR ProteomicsDB; 273581; -.
DR Antibodypedia; 28197; 237 antibodies from 27 providers.
DR DNASU; 11610; -.
DR Ensembl; ENSMUST00000030865; ENSMUSP00000030865; ENSMUSG00000029007.
DR GeneID; 11610; -.
DR KEGG; mmu:11610; -.
DR UCSC; uc008vtz.1; mouse.
DR CTD; 57085; -.
DR MGI; MGI:1339977; Agtrap.
DR VEuPathDB; HostDB:ENSMUSG00000029007; -.
DR eggNOG; ENOG502S36M; Eukaryota.
DR GeneTree; ENSGT00390000017402; -.
DR HOGENOM; CLU_126745_0_0_1; -.
DR InParanoid; Q9WVK0; -.
DR OMA; NINFGFP; -.
DR OrthoDB; 1325275at2759; -.
DR PhylomeDB; Q9WVK0; -.
DR TreeFam; TF324477; -.
DR BioGRID-ORCS; 11610; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Agtrap; mouse.
DR PRO; PR:Q9WVK0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9WVK0; protein.
DR Bgee; ENSMUSG00000029007; Expressed in right kidney and 204 other tissues.
DR Genevisible; Q9WVK0; MM.
DR GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IMP:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008217; P:regulation of blood pressure; IMP:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR InterPro; IPR009436; AGTRAP.
DR PANTHER; PTHR16521; PTHR16521; 1.
DR Pfam; PF06396; AGTRAP; 1.
DR SMART; SM00805; AGTRAP; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..161
FT /note="Type-1 angiotensin II receptor-associated protein"
FT /id="PRO_0000064736"
FT TOPO_DOM 1..26
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..53
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..86
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..161
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 110..122
FT /note="Interaction with AGTR1"
FT /evidence="ECO:0000250"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6RW13"
FT MOD_RES 135
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6RW13"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6RW13"
FT CONFLICT 35
FT /note="F -> L (in Ref. 2; BAB25074)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="V -> A (in Ref. 1; AAD25997, 3; CAQ51920 and 5;
FT AAH57196)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 161 AA; 17525 MW; 42094CBD40A2F97C CRC64;
MELPAVNLKV ILLVHWLLTT WGCLVFSSSY AWGNFTILAL GVWAVAQRDS IDAIGMFLGG
LVATIFLDII YISIFYSSVA TGDTGRFGAG MAILSLLLKP FSCCLVYHMH RERGGELPLR
PDFFGPSQEH SAYQTIDSSS DAAADPFASL ENKGQAVPRG Y
