ID   ATRAP_RAT               Reviewed;         160 AA.
AC   Q642A2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=Type-1 angiotensin II receptor-associated protein;
DE   AltName: Full=AT1 receptor-associated protein;
GN   Name=Agtrap; Synonyms=Atrap;
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 MRNA].
RC   TISSUE=Kidney;
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   [2]
RP   FUNCTION.
RX   PubMed=11162453; DOI=10.1006/bbrc.2000.4055;
RA   Cui T., Nakagami H., Iwai M., Takeda Y., Shiuchi T., Tamura K., Daviet L.,
RA   Horiuchi M.;
RT   "ATRAP, novel AT1 receptor associated protein, enhances internalization of
RT   AT1 receptor and inhibits vascular smooth muscle cell growth.";
RL   Biochem. Biophys. Res. Commun. 279:938-941(2000).
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).
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       May play a role of negative regulator in cardiomyocyte hypertrophy
CC       induced by angiotensin II through an inhibition of p38 mitogen-
CC       activated protein kinase pathway. Attenuates type-1 angiotensin II
CC       receptor growth promoting effect and angiotensin II-induced
CC       phosphorylation of protein kinase AKT and of STAT3.
CC       {ECO:0000269|PubMed:11162453}.
CC   -!- SUBUNIT: Interacts with RACK1, and with the carboxy-terminal region of
CC       AGTR1. {ECO:0000250}.
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}.
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DR   EMBL; BC082019; AAH82019.1; -; mRNA.
DR   RefSeq; NP_001007655.1; NM_001007654.1.
DR   AlphaFoldDB; Q642A2; -.
DR   STRING; 10116.ENSRNOP00000011747; -.
DR   PhosphoSitePlus; Q642A2; -.
DR   PaxDb; 10116-ENSRNOP00000011747; -.
DR   Ensembl; ENSRNOT00000011747.7; ENSRNOP00000011747.3; ENSRNOG00000008619.7.
DR   Ensembl; ENSRNOT00055038884; ENSRNOP00055031559; ENSRNOG00055022665.
DR   Ensembl; ENSRNOT00060049513; ENSRNOP00060041299; ENSRNOG00060028434.
DR   Ensembl; ENSRNOT00065017134; ENSRNOP00065013111; ENSRNOG00065010576.
DR   GeneID; 298646; -.
DR   KEGG; rno:298646; -.
DR   AGR; RGD:1359346; -.
DR   CTD; 57085; -.
DR   RGD; 1359346; Agtrap.
DR   eggNOG; ENOG502S36M; Eukaryota.
DR   GeneTree; ENSGT00390000017402; -.
DR   HOGENOM; CLU_126745_0_0_1; -.
DR   InParanoid; Q642A2; -.
DR   OMA; MHSKDSI; -.
DR   OrthoDB; 5401843at2759; -.
DR   PhylomeDB; Q642A2; -.
DR   TreeFam; TF324477; -.
DR   PRO; PR:Q642A2; -.
DR   Proteomes; UP000002494; Chromosome 5.
DR   Bgee; ENSRNOG00000008619; Expressed in adult mammalian kidney and 19 other cell types or tissues.
DR   GO; GO:0005938; C:cell cortex; ISO:RGD.
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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR   GO; GO:0004945; F:angiotensin type II receptor activity; ISO:RGD.
DR   GO; GO:0038166; P:angiotensin-activated signaling pathway; ISO:RGD.
DR   GO; GO:0008217; P:regulation of blood pressure; ISO:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   InterPro; IPR009436; AGTRAP.
DR   PANTHER; PTHR16521; TYPE-1 ANGIOTENSIN II RECEPTOR-ASSOCIATED PROTEIN; 1.
DR   PANTHER; PTHR16521:SF3; TYPE-1 ANGIOTENSIN II RECEPTOR-ASSOCIATED PROTEIN; 1.
DR   Pfam; PF06396; AGTRAP; 1.
DR   SMART; SM00805; AGTRAP; 1.
DR   Genevisible; Q642A2; RN.
PE   1: Evidence at protein level;
KW   Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..160
FT                   /note="Type-1 angiotensin II receptor-associated protein"
FT                   /id="PRO_0000064738"
FT   TOPO_DOM        1..9
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..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..160
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          110..122
FT                   /note="Interaction with AGTR1"
FT                   /evidence="ECO:0000250"
FT   REGION          128..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   160 AA;  17398 MW;  DEBD34E6F62CBB5A CRC64;
     MELPAVNLKV ILLVHWLLTT WGCLAFSGSY AWGNFTILAL GVWAVAQRDS VDAIGMFLGG
     LVATIFLDII YISIFYSSVA VGDTGRFSAG MAIFSLLLKP FSCCLVYHMH RERGGELPLR
     SDFFGPSQEH SAYQTIDSSD SPADPLASLE NKGQAAPRGY
//