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Renin receptor (ATPase H( )-transporting lysosomal accessory protein 2) (ATPase H( )-transporting lysosomal-interacting protein 2) (ER-localized type I transmembrane adaptor) (Embryonic liver differentiation factor 10) (N14F) (Renin/prorenin receptor) (Vacuolar ATP synthase membrane sector-associated protein M8-9) (ATP6M8-9) (V-ATPase M8.9 subunit)

 RENR_HUMAN              Reviewed;         350 AA.
O75787; B7Z9I3; Q5QTQ7; Q6T7F5; Q8NBP3; Q8NG15; Q96FV6; Q96LB5;
Q9H2P8; Q9UG89;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
10-MAY-2005, sequence version 2.
23-MAY-2018, entry version 162.
RecName: Full=Renin receptor;
AltName: Full=ATPase H(+)-transporting lysosomal accessory protein 2;
AltName: Full=ATPase H(+)-transporting lysosomal-interacting protein 2;
AltName: Full=ER-localized type I transmembrane adaptor;
AltName: Full=Embryonic liver differentiation factor 10;
AltName: Full=N14F;
AltName: Full=Renin/prorenin receptor;
AltName: Full=Vacuolar ATP synthase membrane sector-associated protein M8-9;
Short=ATP6M8-9;
Short=V-ATPase M8.9 subunit;
Flags: Precursor;
Name=ATP6AP2; Synonyms=ATP6IP2, CAPER, ELDF10;
ORFNames=HT028, MSTP009, PSEC0072;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH REN,
PHOSPHORYLATION, TISSUE SPECIFICITY, AND FUNCTION.
TISSUE=Mesangial cell;
PubMed=12045255; DOI=10.1172/JCI0214276;
Nguyen G., Delarue F., Burckle C., Bouzhir L., Giller T., Sraer J.-D.;
"Pivotal role of the renin/prorenin receptor in angiotensin II
production and cellular responses to renin.";
J. Clin. Invest. 109:1417-1427(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Cervix carcinoma;
Wang J., Kirby C., Herbst R.;
"Cell cycle-dependent subcellular localization of the protein tyrosine
phosphatase PTPCAAX1 and its implication in cell cycle regulation.";
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Aorta;
Hui R.T., Liu Y.Q., Liu B., Zhao B., Meng X.M., Sheng H., Xu Y.Y.,
Wang X.Y., Ye J., Song L., Gao Y., Wei Y.J., Zhang C.L., Zhang J.,
Chai M.Q., Chen J.Z., Sun Y.H., Zhou X.L., Jiang Y.X., Zhao X.W.,
Liu S., Cao H.Q., Zhao Y., Liu D.Q., Ding J.F., Liu L.S., Gao R.L.,
Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S.;
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hypothalamus;
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain cortex;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Teratocarcinoma;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 13-350 (ISOFORM 1).
TISSUE=Liver;
Zhang S., Yan H., Yang F.;
"The cloning of a novel gene related with erythroid differentiation.";
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-350 (ISOFORM 1).
TISSUE=Brain;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 188-350 (ISOFORM 1).
PubMed=9556572; DOI=10.1074/jbc.273.18.10939;
Ludwig J., Kerscher S., Brandt U., Pfeiffer K., Getlawi F., Apps D.K.,
Schaegger H.;
"Identification and characterization of a novel 9.2-kDa membrane
sector-associated protein of vacuolar proton-ATPase from chromaffin
granules.";
J. Biol. Chem. 273:10939-10947(1998).
[12]
INVOLVEMENT IN MRXE, TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
PubMed=15746149; DOI=10.1093/hmg/ddi094;
Ramser J., Abidi F.E., Burckle C.A., Lenski C., Toriello H., Wen G.,
Lubs H.A., Engert S., Stevenson R.E., Meindl A., Schwartz C.E.,
Nguyen G.;
"A unique exonic splice enhancer mutation in a family with X-linked
mental retardation and epilepsy points to a novel role of the renin
receptor.";
Hum. Mol. Genet. 14:1019-1027(2005).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
INVOLVEMENT IN XPDS.
PubMed=23595882; DOI=10.1093/hmg/ddt180;
Korvatska O., Strand N.S., Berndt J.D., Strovas T., Chen D.H.,
Leverenz J.B., Kiianitsa K., Mata I.F., Karakoc E., Greenup J.L.,
Bonkowski E., Chuang J., Moon R.T., Eichler E.E., Nickerson D.A.,
Zabetian C.P., Kraemer B.C., Bird T.D., Raskind W.H.;
"Altered splicing of ATP6AP2 causes X-linked parkinsonism with
spasticity (XPDS).";
Hum. Mol. Genet. 22:3259-3268(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- FUNCTION: Functions as a renin and prorenin cellular receptor. May
mediate renin-dependent cellular responses by activating ERK1 and
ERK2. By increasing the catalytic efficiency of renin in
AGT/angiotensinogen conversion to angiotensin I, it may also play
a role in the renin-angiotensin system (RAS).
{ECO:0000269|PubMed:12045255}.
-!- SUBUNIT: Interacts with renin and the vacuolar proton-ATPase.
{ECO:0000269|PubMed:12045255}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O75787-1; Sequence=Displayed;
Name=2;
IsoId=O75787-2; Sequence=VSP_056910;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in brain, heart, placenta, liver,
kidney and pancreas. Barely detectable in lung and skeletal
muscles. In the kidney cortex it is restricted to the mesangium of
glomeruli. In the coronary and kidney artery it is expressed in
the subendothelium, associated to smooth muscles where it
colocalizes with REN. Expressed in vascular structures and by
syncytiotrophoblast cells in the mature fetal placenta.
{ECO:0000269|PubMed:12045255, ECO:0000269|PubMed:15746149}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:12045255}.
-!- DISEASE: Mental retardation, X-linked, with epilepsy (MRXE)
[MIM:300423]: A disorder characterized by significantly below
average general intellectual functioning associated with
impairments in adaptive behavior and manifested during the
developmental period. MRXE patients manifest mild to moderate
mental retardation associated with epilepsy, delays in motor
milestones and speech acquisition in infancy.
{ECO:0000269|PubMed:15746149}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Parkinsonism with spasticity, X-linked (XPDS)
[MIM:300911]: A syndrome characterized by parkinsonian features,
such as cogwheel rigidity, resting tremor and bradykinesia, and
variably penetrant spasticity. {ECO:0000269|PubMed:23595882}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAH10395.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAQ13511.1; Type=Frameshift; Positions=155; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAA76984.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AF291814; AAM47531.1; -; mRNA.
EMBL; AY038990; AAK83467.1; -; mRNA.
EMBL; AF109363; AAQ13511.1; ALT_FRAME; mRNA.
EMBL; AF248966; AAG44564.1; -; mRNA.
EMBL; AK315948; BAH14319.1; -; mRNA.
EMBL; AK075382; BAC11582.1; -; mRNA.
EMBL; AC092473; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC010395; AAH10395.1; ALT_INIT; mRNA.
EMBL; BC084541; AAH84541.1; -; mRNA.
EMBL; AY429341; AAR06910.1; -; mRNA.
EMBL; AL049929; CAB43210.1; -; mRNA.
EMBL; Y17975; CAA76984.1; ALT_INIT; mRNA.
CCDS; CCDS14252.1; -. [O75787-1]
PIR; T08667; T08667.
RefSeq; NP_005756.2; NM_005765.2. [O75787-1]
UniGene; Hs.495960; -.
PDB; 3LBS; X-ray; 2.15 A; A/B=333-350.
PDB; 3LC8; X-ray; 2.00 A; A/B=333-350.
PDBsum; 3LBS; -.
PDBsum; 3LC8; -.
ProteinModelPortal; O75787; -.
SMR; O75787; -.
BioGrid; 115461; 112.
IntAct; O75787; 90.
STRING; 9606.ENSP00000367697; -.
TCDB; 8.A.80.1.1; the (pro)renin receptor (prr) family.
iPTMnet; O75787; -.
PhosphoSitePlus; O75787; -.
BioMuta; ATP6AP2; -.
EPD; O75787; -.
MaxQB; O75787; -.
PaxDb; O75787; -.
PeptideAtlas; O75787; -.
PRIDE; O75787; -.
TopDownProteomics; O75787-1; -. [O75787-1]
Ensembl; ENST00000636409; ENSP00000489819; ENSG00000182220. [O75787-2]
Ensembl; ENST00000636580; ENSP00000490083; ENSG00000182220. [O75787-1]
GeneID; 10159; -.
KEGG; hsa:10159; -.
UCSC; uc004det.4; human. [O75787-1]
CTD; 10159; -.
DisGeNET; 10159; -.
EuPathDB; HostDB:ENSG00000182220.13; -.
GeneCards; ATP6AP2; -.
HGNC; HGNC:18305; ATP6AP2.
HPA; HPA003156; -.
MalaCards; ATP6AP2; -.
MIM; 300423; phenotype.
MIM; 300556; gene.
MIM; 300911; phenotype.
neXtProt; NX_O75787; -.
OpenTargets; ENSG00000182220; -.
Orphanet; 93952; X-linked intellectual disability, Hedera type.
Orphanet; 363654; X-linked parkinsonism-spasticity syndrome.
PharmGKB; PA25148; -.
eggNOG; KOG4737; Eukaryota.
eggNOG; ENOG4111F0U; LUCA.
GeneTree; ENSGT00390000008856; -.
HOVERGEN; HBG056579; -.
KO; K19514; -.
OMA; FRDGNWP; -.
OrthoDB; EOG091G0HQ3; -.
PhylomeDB; O75787; -.
TreeFam; TF106137; -.
BioCyc; MetaCyc:MONOMER66-34369; -.
Reactome; R-HSA-2022377; Metabolism of Angiotensinogen to Angiotensins.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SIGNOR; O75787; -.
ChiTaRS; ATP6AP2; human.
GeneWiki; ATP6AP2; -.
GenomeRNAi; 10159; -.
PRO; PR:O75787; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000182220; -.
ExpressionAtlas; O75787; baseline and differential.
Genevisible; O75787; HS.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:HGNC.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0101003; C:ficolin-1-rich granule membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
GO; GO:0002003; P:angiotensin maturation; IDA:HGNC.
GO; GO:0048069; P:eye pigmentation; IMP:UniProtKB.
GO; GO:0060323; P:head morphogenesis; IMP:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; IDA:HGNC.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; IDA:HGNC.
GO; GO:0021903; P:rostrocaudal neural tube patterning; IMP:UniProtKB.
InterPro; IPR012493; Renin_rcpt.
PANTHER; PTHR13351; PTHR13351; 1.
Pfam; PF07850; Renin_r; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Epilepsy;
Membrane; Mental retardation; Neurodegeneration; Parkinsonism;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 16 {ECO:0000255}.
CHAIN 17 350 Renin receptor.
/FTId=PRO_0000022203.
TOPO_DOM 17 302 Extracellular. {ECO:0000255}.
TRANSMEM 303 323 Helical. {ECO:0000255}.
TOPO_DOM 324 350 Cytoplasmic. {ECO:0000255}.
VAR_SEQ 101 132 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056910.
VARIANT 90 90 P -> A (in dbSNP:rs9014).
/FTId=VAR_051313.
VARIANT 290 290 A -> P (in dbSNP:rs35798522).
/FTId=VAR_051314.
CONFLICT 138 138 G -> W (in Ref. 2; AAK83467).
{ECO:0000305}.
CONFLICT 153 154 QL -> HV (in Ref. 2; AAK83467).
{ECO:0000305}.
CONFLICT 258 258 N -> K (in Ref. 6; BAC11582).
{ECO:0000305}.
CONFLICT 285 285 Q -> R (in Ref. 4 and 10). {ECO:0000305}.
CONFLICT 287 287 Missing (in Ref. 8; AAH10395).
{ECO:0000305}.
TURN 334 337 {ECO:0000244|PDB:3LC8}.
HELIX 338 340 {ECO:0000244|PDB:3LBS}.
SEQUENCE 350 AA; 39008 MW; 84084A4ACE9C5DE8 CRC64;
MAVFVVLLAL VAGVLGNEFS ILKSPGSVVF RNGNWPIPGE RIPDVAALSM GFSVKEDLSW
PGLAVGNLFH RPRATVMVMV KGVNKLALPP GSVISYPLEN AVPFSLDSVA NSIHSLFSEE
TPVVLQLAPS EERVYMVGKA NSVFEDLSVT LRQLRNRLFQ ENSVLSSLPL NSLSRNNEVD
LLFLSELQVL HDISSLLSRH KHLAKDHSPD LYSLELAGLD EIGKRYGEDS EQFRDASKIL
VDALQKFADD MYSLYGGNAV VELVTVKSFD TSLIRKTRTI LEAKQAKNPA SPYNLAYKYN
FEYSVVFNMV LWIMIALALA VIITSYNIWN MDPGYDSIIY RMTNQKIRMD


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