AGTR2_HUMAN
ID AGTR2_HUMAN Reviewed; 363 AA.
AC P50052; B2R9V1; Q13016; Q6FGY7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Type-2 angiotensin II receptor {ECO:0000303|PubMed:7733925};
DE AltName: Full=Angiotensin II type-2 receptor {ECO:0000303|PubMed:7790004};
DE Short=AT2 receptor {ECO:0000303|PubMed:7719706};
GN Name=AGTR2 {ECO:0000303|PubMed:7790004, ECO:0000312|HGNC:HGNC:338};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=7733925; DOI=10.1006/bbrc.1995.1537;
RA Martin M.M., Elton T.S.;
RT "The sequence and genomic organization of the human type 2 angiotensin II
RT receptor.";
RL Biochem. Biophys. Res. Commun. 209:554-562(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=7790004; DOI=10.1016/0888-7543(95)80072-t;
RA Chassagne C., Beatty B.G., Meloche S.;
RT "Assignment of the human angiotensin II type 2 receptor gene (AGTR2) to
RT chromosome Xq22-q23 by fluorescence in situ hybridization.";
RL Genomics 25:601-603(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=7945336; DOI=10.1006/bbrc.1994.2402;
RA Koike G., Horiuchi M., Yamada T., Szpirer C., Jacob H.J., Dzau V.J.;
RT "Human type 2 angiotensin II receptor gene: cloned, mapped to the X
RT chromosome, and its mRNA is expressed in the human lung.";
RL Biochem. Biophys. Res. Commun. 203:1842-1850(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC TISSUE=Placenta;
RX PubMed=8185599; DOI=10.1006/bbrc.1994.1613;
RA Tsuzuki S., Ichiki T., Nakakubo H., Kitami Y., Guo D.F., Shirai H.,
RA Inagami T.;
RT "Molecular cloning and expression of the gene encoding human angiotensin II
RT type 2 receptor.";
RL Biochem. Biophys. Res. Commun. 200:1449-1454(1994).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=7999093; DOI=10.1006/bbrc.1994.2714;
RA Martin M.M., Su B., Elton T.S.;
RT "Molecular cloning of the human angiotensin II type 2 receptor cDNA.";
RL Biochem. Biophys. Res. Commun. 205:645-651(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=7719706;
RA Lazard D., Briend-Sutren M.M., Villageois P., Mattei M.-G., Strosberg A.D.,
RA Nahmias C.;
RT "Molecular characterization and chromosome localization of a human
RT angiotensin II AT2 receptor gene highly expressed in fetal tissues.";
RL Recept. Channels 2:271-280(1994).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhang M., Ma H., Wang B., Zhao Y.;
RT "Sequence of the AGTR2 gene in Cantonese.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Kopatz S.A., Aronstam R.S., Sharma S.V.;
RT "Isolation of complete coding sequence for angiotensin II receptor, type 2
RT (AGTR2).";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D.,
RA Toth E.J., Nickerson D.A.;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [15]
RP NUCLEOTIDE SEQUENCE OF 1-22.
RC TISSUE=Blood;
RA Katsuya T., Dzau V.J.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [16]
RP NUCLEOTIDE SEQUENCE OF 1-16.
RC TISSUE=Uterus;
RA Warnecke C.H., Holzmeister J., Regitz-Zagrosek V., Fleck E.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP TISSUE SPECIFICITY, VARIANTS VAL-21; LYS-248; GLN-324 AND VAL-337, AND
RP POSSIBLE ASSOCIATION OF VARIANTS VAL-21; GLN-324 AND VAL-337 WITH X-LINKED
RP INTELLECTUAL DISABILITY.
RX PubMed=12089445; DOI=10.1126/science.1072191;
RA Vervoort V.S., Beachem M.A., Edwards P.S., Ladd S., Miller K.E.,
RA de Mollerat X., Clarkson K., DuPont B., Schwartz C.E., Stevenson R.E.,
RA Boyd E., Srivastava A.K.;
RT "AGTR2 mutations in X-linked mental retardation.";
RL Science 296:2401-2403(2002).
RN [18]
RP INTERACTION WITH MTUS1, AND FUNCTION.
RX PubMed=15123706; DOI=10.1074/jbc.m403880200;
RA Nouet S., Amzallag N., Li J.-M., Louis S., Seitz I., Cui T.-X.,
RA Alleaume A.-M., Di Benedetto M., Boden C., Masson M., Strosberg A.D.,
RA Horiuchi M., Couraud P.-O., Nahmias C.;
RT "Trans-inactivation of receptor tyrosine kinases by novel angiotensin II
RT AT2 receptor-interacting protein, ATIP.";
RL J. Biol. Chem. 279:28989-28997(2004).
RN [19]
RP LACK OF ASSOCIATION VARIANTS VAL-21; GLN-324 AND VAL-337 WITH X-LINKED
RP INTELLECTUAL DISABILITY.
RX PubMed=23871722; DOI=10.1016/j.ajhg.2013.06.013;
RA Piton A., Redin C., Mandel J.L.;
RT "XLID-causing mutations and associated genes challenged in light of data
RT from large-scale human exome sequencing.";
RL Am. J. Hum. Genet. 93:368-383(2013).
RN [20] {ECO:0007744|PDB:5UNF, ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 35-335, FUNCTION, DISULFIDE
RP BONDS, TOPOLOGY, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ARG-182 AND
RP LYS-215.
RX PubMed=28379944; DOI=10.1038/nature22035;
RA Zhang H., Han G.W., Batyuk A., Ishchenko A., White K.L., Patel N.,
RA Sadybekov A., Zamlynny B., Rudd M.T., Hollenstein K., Tolstikova A.,
RA White T.A., Hunter M.S., Weierstall U., Liu W., Babaoglu K., Moore E.L.,
RA Katz R.D., Shipman J.M., Garcia-Calvo M., Sharma S., Sheth P.,
RA Soisson S.M., Stevens R.C., Katritch V., Cherezov V.;
RT "Structural basis for selectivity and diversity in angiotensin II
RT receptors.";
RL Nature 544:327-332(2017).
RN [21] {ECO:0007744|PDB:5XJM}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 35-242 AND 246-346 IN COMPLEX
RP WITH ANGIOTENSIN II, FUNCTION, DISULFIDE BONDS, TOPOLOGY, SUBCELLULAR
RP LOCATION, AND MUTAGENESIS OF TYR-108; MET-128; ARG-182; LYS-215; TRP-269;
RP PHE-272 AND ASP-297.
RX PubMed=29967536; DOI=10.1038/s41594-018-0079-8;
RA Asada H., Horita S., Hirata K., Shiroishi M., Shiimura Y., Iwanari H.,
RA Hamakubo T., Shimamura T., Nomura N., Kusano-Arai O., Uemura T., Suno C.,
RA Kobayashi T., Iwata S.;
RT "Crystal structure of the human angiotensin II type 2 receptor bound to an
RT angiotensin II analog.";
RL Nat. Struct. Mol. Biol. 25:570-576(2018).
RN [22] {ECO:0007744|PDB:7C6A}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 35-242 AND 246-346, DISULFIDE
RP BONDS, TOPOLOGY, AND SUBCELLULAR LOCATION.
RX PubMed=32669569; DOI=10.1038/s41598-020-68355-x;
RA Miyagi H., Asada H., Suzuki M., Takahashi Y., Yasunaga M., Suno C.,
RA Iwata S., Saito J.I.;
RT "The discovery of a new antibody for BRIL-fused GPCR structure
RT determination.";
RL Sci. Rep. 10:11669-11669(2020).
RN [23] {ECO:0007744|PDB:6JOD}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 35-346 IN COMPLEX WITH
RP ANGIOTENSIN II, FUNCTION, DISULFIDE BONDS, TOPOLOGY, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF TYR-104; MET-128; ARG-182; LYS-215; TRP-269; PHE-272;
RP ASP-297 AND PHE-308.
RX PubMed=31899086; DOI=10.1016/j.str.2019.12.003;
RA Asada H., Inoue A., Ngako Kadji F.M., Hirata K., Shiimura Y., Im D.,
RA Shimamura T., Nomura N., Iwanari H., Hamakubo T., Kusano-Arai O.,
RA Hisano H., Uemura T., Suno C., Aoki J., Iwata S.;
RT "The crystal structure of angiotensin II type 2 receptor with endogenous
RT peptide hormone.";
RL Structure 28:418-425(2020).
CC -!- FUNCTION: Receptor for angiotensin II, a vasoconstricting peptide
CC (PubMed:8185599, PubMed:28379944, PubMed:29967536, PubMed:31899086).
CC Signals primarily via a non-canonical G-protein- and beta-arrestin
CC independent pathways (PubMed:28379944). Cooperates with MTUS1 to
CC inhibit ERK2 activation and cell proliferation (PubMed:15123706).
CC {ECO:0000269|PubMed:15123706, ECO:0000269|PubMed:28379944,
CC ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
CC ECO:0000269|PubMed:8185599}.
CC -!- SUBUNIT: Interacts with MTUS1. {ECO:0000269|PubMed:15123706}.
CC -!- INTERACTION:
CC P50052; PRO_0000032459 [P01019]: AGT; NbExp=2; IntAct=EBI-1748067, EBI-2927577;
CC P50052; P35625: TIMP3; NbExp=7; IntAct=EBI-1748067, EBI-1748085;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P35374};
CC Multi-pass membrane protein {ECO:0000269|PubMed:28379944,
CC ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
CC ECO:0000269|PubMed:32669569}.
CC -!- TISSUE SPECIFICITY: In adult, highly expressed in myometrium with lower
CC levels in adrenal gland and fallopian tube. Expressed in the
CC cerebellum. Very highly expressed in fetal kidney and intestine.
CC {ECO:0000269|PubMed:12089445}.
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
CC (PubMed:28379944). Helix VIII is found in a non-canonical position,
CC stabilizing the active-like state, but at the same time preventing the
CC recruitment of G-proteins or beta-arrestins (PubMed:28379944). Upon
CC switching to a membrane-bound conformation, helix VIII can support the
CC recruitment of G proteins and beta-arrestins (PubMed:28379944).
CC {ECO:0000269|PubMed:28379944}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- CAUTION: AGTR2 has been reported to be involved in X-linked
CC intellectual disability (PubMed:12089445). Its pathological role is
CC however questionable (PubMed:23871722). {ECO:0000305|PubMed:12089445,
CC ECO:0000305|PubMed:23871722}.
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DR EMBL; U20860; AAA85851.1; -; Genomic_DNA.
DR EMBL; L34579; AAA98990.1; -; Genomic_DNA.
DR EMBL; U10273; AAA61794.1; -; Genomic_DNA.
DR EMBL; U15592; AAA50762.1; -; Genomic_DNA.
DR EMBL; U16957; AAA67753.1; -; mRNA.
DR EMBL; U27478; AAA84900.1; -; Genomic_DNA.
DR EMBL; AY536522; AAS45437.1; -; Genomic_DNA.
DR EMBL; AY322542; AAP84355.1; -; Genomic_DNA.
DR EMBL; AY324607; AAP72969.1; -; Genomic_DNA.
DR EMBL; CR541969; CAG46767.1; -; mRNA.
DR EMBL; AK313927; BAG36648.1; -; mRNA.
DR EMBL; AL732602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471234; EAW51502.1; -; Genomic_DNA.
DR EMBL; BC095504; AAH95504.1; -; mRNA.
DR EMBL; X87723; CAA61022.1; -; mRNA.
DR CCDS; CCDS14569.1; -.
DR PIR; JC2543; JC2543.
DR RefSeq; NP_000677.2; NM_000686.4.
DR RefSeq; XP_011535835.1; XM_011537533.1.
DR PDB; 5UNF; X-ray; 2.80 A; A/B=35-335.
DR PDB; 5UNG; X-ray; 2.80 A; B=35-335.
DR PDB; 5UNH; X-ray; 2.90 A; A/B=35-335.
DR PDB; 5XJM; X-ray; 3.20 A; A=35-242, A=246-346.
DR PDB; 6JOD; X-ray; 3.20 A; A=35-346.
DR PDB; 7C6A; X-ray; 3.40 A; A=35-242, A=246-346.
DR PDB; 7JNI; X-ray; 3.00 A; A/B=35-335.
DR PDBsum; 5UNF; -.
DR PDBsum; 5UNG; -.
DR PDBsum; 5UNH; -.
DR PDBsum; 5XJM; -.
DR PDBsum; 6JOD; -.
DR PDBsum; 7C6A; -.
DR PDBsum; 7JNI; -.
DR AlphaFoldDB; P50052; -.
DR SMR; P50052; -.
DR BioGRID; 106692; 9.
DR IntAct; P50052; 3.
DR STRING; 9606.ENSP00000360973; -.
DR BindingDB; P50052; -.
DR ChEMBL; CHEMBL4607; -.
DR DrugBank; DB05739; CYT006-AngQb.
DR DrugBank; DB01349; Tasosartan.
DR DrugCentral; P50052; -.
DR GuidetoPHARMACOLOGY; 35; -.
DR GlyGen; P50052; 5 sites.
DR iPTMnet; P50052; -.
DR PhosphoSitePlus; P50052; -.
DR BioMuta; AGTR2; -.
DR DMDM; 1703214; -.
DR MassIVE; P50052; -.
DR PaxDb; P50052; -.
DR PeptideAtlas; P50052; -.
DR PRIDE; P50052; -.
DR ABCD; P50052; 1 sequenced antibody.
DR Antibodypedia; 29644; 266 antibodies from 36 providers.
DR DNASU; 186; -.
DR Ensembl; ENST00000371906.5; ENSP00000360973.4; ENSG00000180772.8.
DR Ensembl; ENST00000681852.1; ENSP00000505750.1; ENSG00000180772.8.
DR GeneID; 186; -.
DR KEGG; hsa:186; -.
DR MANE-Select; ENST00000371906.5; ENSP00000360973.4; NM_000686.5; NP_000677.2.
DR UCSC; uc004eqh.5; human.
DR CTD; 186; -.
DR DisGeNET; 186; -.
DR GeneCards; AGTR2; -.
DR HGNC; HGNC:338; AGTR2.
DR HPA; ENSG00000180772; Tissue enhanced (endometrium, lung, smooth muscle).
DR MalaCards; AGTR2; -.
DR MIM; 300034; gene.
DR neXtProt; NX_P50052; -.
DR OpenTargets; ENSG00000180772; -.
DR Orphanet; 777; X-linked non-syndromic intellectual disability.
DR PharmGKB; PA44; -.
DR VEuPathDB; HostDB:ENSG00000180772; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244888; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P50052; -.
DR OMA; STFNCSH; -.
DR OrthoDB; 685818at2759; -.
DR PhylomeDB; P50052; -.
DR TreeFam; TF330024; -.
DR PathwayCommons; P50052; -.
DR Reactome; R-HSA-375276; Peptide ligand-binding receptors.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; P50052; -.
DR SIGNOR; P50052; -.
DR BioGRID-ORCS; 186; 7 hits in 698 CRISPR screens.
DR GeneWiki; Angiotensin_II_receptor_type_2; -.
DR GenomeRNAi; 186; -.
DR Pharos; P50052; Tchem.
DR PRO; PR:P50052; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P50052; protein.
DR Bgee; ENSG00000180772; Expressed in adrenal tissue and 57 other tissues.
DR Genevisible; P50052; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004945; F:angiotensin type II receptor activity; IDA:UniProtKB.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IBA:GO_Central.
DR GO; GO:0048019; F:receptor antagonist activity; TAS:BHF-UCL.
DR GO; GO:0002033; P:angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure; IEA:Ensembl.
DR GO; GO:0001974; P:blood vessel remodeling; TAS:BHF-UCL.
DR GO; GO:0007420; P:brain development; NAS:BHF-UCL.
DR GO; GO:0002035; P:brain renin-angiotensin system; IEA:Ensembl.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IDA:BHF-UCL.
DR GO; GO:0035640; P:exploration behavior; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0007199; P:G protein-coupled receptor signaling pathway coupled to cGMP nucleotide second messenger; ISS:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:BHF-UCL.
DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; NAS:BHF-UCL.
DR GO; GO:0030308; P:negative regulation of cell growth; TAS:BHF-UCL.
DR GO; GO:0010459; P:negative regulation of heart rate; ISS:BHF-UCL.
DR GO; GO:0051387; P:negative regulation of neurotrophin TRK receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0007263; P:nitric oxide mediated signal transduction; TAS:BHF-UCL.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IMP:BHF-UCL.
DR GO; GO:0072300; P:positive regulation of metanephric glomerulus development; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IC:BHF-UCL.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISS:BHF-UCL.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0008217; P:regulation of blood pressure; TAS:ProtInc.
DR GO; GO:0035566; P:regulation of metanephros size; IEA:Ensembl.
DR GO; GO:0001991; P:regulation of systemic arterial blood pressure by circulatory renin-angiotensin; ISS:BHF-UCL.
DR GO; GO:0042311; P:vasodilation; IDA:BHF-UCL.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Disulfide bond; G-protein coupled receptor;
KW Glycoprotein; Membrane; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..363
FT /note="Type-2 angiotensin II receptor"
FT /id="PRO_0000069167"
FT TOPO_DOM 1..45
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TRANSMEM 46..70
FT /note="Helical; Name=1"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TOPO_DOM 71..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TRANSMEM 81..104
FT /note="Helical; Name=2"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TOPO_DOM 105..114
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TRANSMEM 115..140
FT /note="Helical; Name=3"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TOPO_DOM 141..159
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TRANSMEM 160..181
FT /note="Helical; Name=4"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TOPO_DOM 182..206
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TRANSMEM 207..232
FT /note="Helical; Name=5"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TOPO_DOM 233..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TRANSMEM 258..281
FT /note="Helical; Name=6"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TOPO_DOM 282..294
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TRANSMEM 295..320
FT /note="Helical; Name=7"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT TOPO_DOM 321..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT REGION 324..333
FT /note="Helix VIII"
FT /evidence="ECO:0000269|PubMed:28379944"
FT BINDING 103
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000305|PubMed:31899086,
FT ECO:0007744|PDB:6JOD"
FT BINDING 104
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000305|PubMed:31899086,
FT ECO:0007744|PDB:6JOD"
FT BINDING 182
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000305|PubMed:31899086,
FT ECO:0007744|PDB:6JOD"
FT BINDING 204
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000305|PubMed:31899086,
FT ECO:0007744|PDB:6JOD"
FT BINDING 215
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000269|PubMed:29967536,
FT ECO:0000305|PubMed:31899086, ECO:0007744|PDB:5XJM,
FT ECO:0007744|PDB:6JOD"
FT BINDING 279
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000269|PubMed:29967536,
FT ECO:0000305|PubMed:31899086, ECO:0007744|PDB:5XJM,
FT ECO:0007744|PDB:6JOD"
FT BINDING 297
FT /ligand="angiotensin II"
FT /ligand_id="ChEBI:CHEBI:58506"
FT /evidence="ECO:0000269|PubMed:29967536,
FT ECO:0007744|PDB:5XJM"
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 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..290
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT DISULFID 117..195
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086,
FT ECO:0000269|PubMed:32669569, ECO:0007744|PDB:5UNF,
FT ECO:0007744|PDB:5UNG, ECO:0007744|PDB:5UNH,
FT ECO:0007744|PDB:5XJM, ECO:0007744|PDB:6JOD,
FT ECO:0007744|PDB:7C6A"
FT VARIANT 21
FT /note="G -> V (rare variant found in patients with X-linked
FT intellectual disability; unknown pathological significance;
FT dbSNP:rs121917810)"
FT /evidence="ECO:0000269|PubMed:12089445,
FT ECO:0000269|PubMed:23871722"
FT /id="VAR_065946"
FT VARIANT 231
FT /note="Y -> H (in dbSNP:rs3729977)"
FT /id="VAR_049374"
FT VARIANT 248
FT /note="R -> K (in dbSNP:rs5191)"
FT /evidence="ECO:0000269|PubMed:12089445"
FT /id="VAR_011849"
FT VARIANT 268
FT /note="C -> W (in dbSNP:rs1042860)"
FT /id="VAR_011850"
FT VARIANT 324
FT /note="R -> Q (rare variant found in patients with X-linked
FT intellectual disability; unknown pathological significance;
FT dbSNP:rs35474657)"
FT /evidence="ECO:0000269|PubMed:12089445,
FT ECO:0000269|PubMed:23871722"
FT /id="VAR_065947"
FT VARIANT 337
FT /note="I -> V (rare variant found in patients with X-linked
FT intellectual disability; unknown pathological significance;
FT dbSNP:rs121917811)"
FT /evidence="ECO:0000269|PubMed:12089445"
FT /id="VAR_065948"
FT MUTAGEN 104
FT /note="Y->A: Abolished angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:31899086"
FT MUTAGEN 108
FT /note="Y->A: Abolished angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:29967536"
FT MUTAGEN 128
FT /note="M->A: Abolished angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:31899086"
FT MUTAGEN 128
FT /note="M->L: Does not affect angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:29967536,
FT ECO:0000269|PubMed:31899086"
FT MUTAGEN 182
FT /note="R->A: Abolished angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086"
FT MUTAGEN 215
FT /note="K->A,Q: Abolished angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:28379944,
FT ECO:0000269|PubMed:29967536, ECO:0000269|PubMed:31899086"
FT MUTAGEN 269
FT /note="W->A: Abolished angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:31899086"
FT MUTAGEN 272
FT /note="F->A: Abolished angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:29967536,
FT ECO:0000269|PubMed:31899086"
FT MUTAGEN 272
FT /note="F->H: Does not affect angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:31899086"
FT MUTAGEN 297
FT /note="D->A: Abolished angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:29967536,
FT ECO:0000269|PubMed:31899086"
FT MUTAGEN 308
FT /note="F->Y: Abolished angiotensin II-binding."
FT /evidence="ECO:0000269|PubMed:31899086"
FT CONFLICT 269
FT /note="W -> C (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 272
FT /note="F -> L (in Ref. 4; AAA50762)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="N -> G (in Ref. 4; AAA50762)"
FT /evidence="ECO:0000305"
FT TURN 39..42
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 46..71
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 79..94
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:5UNF"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:6JOD"
FT HELIX 113..147
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:5UNG"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6JOD"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:5UNF"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:5UNF"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:5UNF"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 205..219
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 221..240
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 246..283
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 290..318
FT /evidence="ECO:0007829|PDB:5UNF"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 322..333
FT /evidence="ECO:0007829|PDB:5UNF"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:6JOD"
SQ SEQUENCE 363 AA; 41184 MW; FDD7D4E6F9B43E60 CRC64;
MKGNSTLATT SKNITSGLHF GLVNISGNNE STLNCSQKPS DKHLDAIPIL YYIIFVIGFL
VNIVVVTLFC CQKGPKKVSS IYIFNLAVAD LLLLATLPLW ATYYSYRYDW LFGPVMCKVF
GSFLTLNMFA SIFFITCMSV DRYQSVIYPF LSQRRNPWQA SYIVPLVWCM ACLSSLPTFY
FRDVRTIEYL GVNACIMAFP PEKYAQWSAG IALMKNILGF IIPLIFIATC YFGIRKHLLK
TNSYGKNRIT RDQVLKMAAA VVLAFIICWL PFHVLTFLDA LAWMGVINSC EVIAVIDLAL
PFAILLGFTN SCVNPFLYCF VGNRFQQKLR SVFRVPITWL QGKRESMSCR KSSSLREMET
FVS
