ID   ATRAP_PONAB             Reviewed;         152 AA.
AC   Q5RER2;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Type-1 angiotensin II receptor-associated protein;
DE   AltName: Full=AT1 receptor-associated protein;
GN   Name=AGTRAP;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 cell proliferation and angiotensin II-
CC       stimulated transcriptional activity (By similarity). {ECO:0000250}.
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; CR857454; CAH89745.1; -; mRNA.
DR   RefSeq; NP_001127190.1; NM_001133718.1.
DR   AlphaFoldDB; Q5RER2; -.
DR   STRING; 9601.ENSPPYP00000002181; -.
DR   Ensembl; ENSPPYT00000048797; ENSPPYP00000045301; ENSPPYG00000001883.
DR   GeneID; 100174244; -.
DR   KEGG; pon:100174244; -.
DR   CTD; 57085; -.
DR   eggNOG; ENOG502S36M; Eukaryota.
DR   GeneTree; ENSGT00410000029218; -.
DR   HOGENOM; CLU_126745_0_0_1; -.
DR   InParanoid; Q5RER2; -.
DR   OrthoDB; 1325275at2759; -.
DR   Proteomes; UP000001595; Chromosome 1.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0038166; P:angiotensin-activated signaling pathway; IEA:InterPro.
DR   InterPro; IPR009436; AGTRAP.
DR   PANTHER; PTHR16521; PTHR16521; 1.
DR   Pfam; PF06396; AGTRAP; 1.
DR   SMART; SM00805; AGTRAP; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasmic vesicle; Endoplasmic reticulum; Golgi apparatus; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..152
FT                   /note="Type-1 angiotensin II receptor-associated protein"
FT                   /id="PRO_0000064737"
FT   TOPO_DOM        1..23
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..55
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        77..86
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        108..152
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         119
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RW13"
FT   MOD_RES         120
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RW13"
FT   MOD_RES         128
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RW13"
FT   MOD_RES         131
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6RW13"
SQ   SEQUENCE   152 AA;  16525 MW;  901A86B016A84003 CRC64;
     MELPAVNLKV ILLGHWLLTT WGCIVFSGSY AWANFTILAL GVWAVAQRDS IDAISMFLGG
     LLATIFLDIV HISIFYPRAG LTDTGRFGAG MAILSLLLKP LSCCFVYHMY RQRGGFLGSS
     QDRSAYQTID SAEAPANAFA VPEGRGQDAR GY