AGTR2_SHEEP
ID AGTR2_SHEEP Reviewed; 362 AA.
AC Q28929; W5PJB5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 03-AUG-2022, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Type-2 angiotensin II receptor;
DE AltName: Full=Angiotensin II type-2 receptor;
DE Short=AT2 receptor {ECO:0000303|PubMed:8618791};
GN Name=AGTR2;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20809919; DOI=10.1111/j.1365-2052.2010.02100.x;
RA Archibald A.L., Cockett N.E., Dalrymple B.P., Faraut T., Kijas J.W.,
RA Maddox J.F., McEwan J.C., Hutton Oddy V., Raadsma H.W., Wade C., Wang J.,
RA Wang W., Xun X.;
RT "The sheep genome reference sequence: a work in progress.";
RL Anim. Genet. 41:449-453(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 47-306.
RC TISSUE=Kidney;
RX PubMed=8618791; DOI=10.1203/00006450-199512000-00012;
RA Robillard J.E., Page W.V., Mathews M.S., Schutte B.C., Nuyt A.M.,
RA Segar J.L.;
RT "Differential gene expression and regulation of renal angiotensin II
RT receptor subtypes (AT1 and AT2) during fetal life in sheep.";
RL Pediatr. Res. 38:896-904(1995).
CC -!- FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide.
CC Signals primarily via a non-canonical G-protein- and beta-arrestin
CC independent pathways. Cooperates with MTUS1 to inhibit ERK2 activation
CC and cell proliferation. {ECO:0000250|UniProtKB:P50052}.
CC -!- SUBUNIT: Interacts with MTUS1. {ECO:0000250|UniProtKB:P50052}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35374};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P50052}.
CC -!- DOMAIN: Helix VIII may act as a gatekeeper for either suppression or
CC activation of the receptor, depending on post-translational
CC modifications and interactions with various receptor partners. Helix
CC VIII is found in a non-canonical position, stabilizing the active-like
CC state, but at the same time preventing the recruitment of G-proteins or
CC beta-arrestins. Upon switching to a membrane-bound conformation, helix
CC VIII can support the recruitment of G proteins and beta-arrestins.
CC {ECO:0000250|UniProtKB:P50052}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AMGL01118537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S81979; AAB36404.1; -; mRNA.
DR RefSeq; XP_011962878.1; XM_012107488.1.
DR RefSeq; XP_011962879.1; XM_012107489.1.
DR RefSeq; XP_014960561.1; XM_015105075.1.
DR AlphaFoldDB; Q28929; -.
DR SMR; Q28929; -.
DR STRING; 9940.ENSOARP00000010536; -.
DR Ensembl; ENSOART00000010692.1; ENSOARP00000010536.1; ENSOARG00000009828.1.
DR Ensembl; ENSOART00020037991; ENSOARP00020031452; ENSOARG00020024319.
DR KEGG; oas:443335; -.
DR CTD; 186; -.
DR eggNOG; KOG3656; Eukaryota.
DR Proteomes; UP000002356; Chromosome X.
DR Bgee; ENSOARG00000009828; Expressed in aortic valve and 28 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004945; F:angiotensin type II receptor activity; ISS:UniProtKB.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IEA:InterPro.
DR GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
DR InterPro; IPR000147; ATII_AT2_rcpt.
DR InterPro; IPR000248; ATII_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00241; ANGIOTENSINR.
DR PRINTS; PR00636; ANGIOTENSN2R.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
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..362
FT /note="Type-2 angiotensin II receptor"
FT /id="PRO_0000069171"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 45..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 70..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 80..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 104..113
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 114..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 140..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 159..180
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 181..205
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 206..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 232..256
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 257..280
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 281..293
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TRANSMEM 294..319
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT TOPO_DOM 320..362
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT REGION 323..332
FT /note="Helix VIII"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 102
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 103
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 181
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 203
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 214
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 278
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT BINDING 296
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 13
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..289
FT /evidence="ECO:0000250|UniProtKB:P50052"
FT DISULFID 116..194
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 54
FT /note="F -> W (in Ref. 2; AAB36404)"
FT CONFLICT 166
FT /note="V -> G (in Ref. 2; AAB36404)"
SQ SEQUENCE 362 AA; 41108 MW; 08A865093E712012 CRC64;
MKANFSLATI SKNITSSLHV GFVNISSNES TFNCSHKPSD KHLDAIPVLY YIIFGVGFLV
NTIVVTLFCC QKGPKKVSSI YIFNLAVADL LLLATLPLWA TYYSHRYDWI FGPVMCKVFG
SFLTLNMFAS IFFITCMSVD RYQSVIYPFL SQRRNPWQAS YIVPLVWCMA CLSSLPTFYF
RDVRTIEYLG VNACIMAFPP EKYAQWSAGI ALMKNILGFI IPLIFIATCY FGIRKHLLKT
NSYGKNRITR DQVLKMAAAV VLAFIICWLP FHVLTFLDAL AWMGVINSCE VIAVIDLALP
FAILLGFTNS CINPFLYCFV GNRFQQKLRR VFRVPITWLQ GKRENGSCGK SSSFREMETF
VS
