RENR_BOVIN
ID RENR_BOVIN Reviewed; 351 AA.
AC P81134; A5D7N4;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Renin receptor;
DE AltName: Full=ATPase H(+)-transporting lysosomal accessory protein 2;
DE AltName: Full=ATPase H(+)-transporting lysosomal-interacting protein 2;
DE AltName: Full=Renin/prorenin receptor;
DE AltName: Full=Vacuolar ATP synthase membrane sector-associated protein M8-9;
DE Short=V-ATPase M8.9 subunit;
DE Contains:
DE RecName: Full=Renin receptor extracellular fragment {ECO:0000305};
DE Contains:
DE RecName: Full=Renin receptor cytoplasmic fragment {ECO:0000305};
DE Flags: Precursor;
GN Name=ATP6AP2; Synonyms=ATP6IP2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 283-312.
RC TISSUE=Adrenal medulla;
RX PubMed=9556572; DOI=10.1074/jbc.273.18.10939;
RA Ludwig J., Kerscher S., Brandt U., Pfeiffer K., Getlawi F., Apps D.K.,
RA Schaegger H.;
RT "Identification and characterization of a novel 9.2-kDa membrane sector-
RT associated protein of vacuolar proton-ATPase from chromaffin granules.";
RL J. Biol. Chem. 273:10939-10947(1998).
RN [3] {ECO:0007744|PDB:6XBW, ECO:0007744|PDB:6XBY}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.37 ANGSTROMS) IN COMPLEX WITH THE
RP V-ATPASE, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP TISSUE SPECIFICITY.
RX PubMed=32764564; DOI=10.1038/s41467-020-17762-9;
RA Wang R., Long T., Hassan A., Wang J., Sun Y., Xie X.S., Li X.;
RT "Cryo-EM structures of intact V-ATPase from bovine brain.";
RL Nat. Commun. 11:3921-3921(2020).
CC -!- FUNCTION: Multifunctional protein which functions as a renin, prorenin
CC cellular receptor and is involved in the assembly of the lysosomal
CC proton-transporting V-type ATPase (V-ATPase) and the acidification of
CC the endo-lysosomal system (By similarity). May mediate renin-dependent
CC cellular responses by activating ERK1 and ERK2 (By similarity). By
CC increasing the catalytic efficiency of renin in AGT/angiotensinogen
CC conversion to angiotensin I, may also play a role in the renin-
CC angiotensin system (RAS) (By similarity). Through its function in V-
CC type ATPase (v-ATPase) assembly and acidification of the lysosome it
CC regulates protein degradation and may control different signaling
CC pathways important for proper brain development, synapse morphology and
CC synaptic transmission (By similarity). {ECO:0000250|UniProtKB:O75787,
CC ECO:0000250|UniProtKB:Q9CYN9}.
CC -!- SUBUNIT: Interacts with renin (By similarity). Accessory component of
CC the multisubunit proton-transporting vacuolar (V)-ATPase protein pump
CC (PubMed:32764564). Interacts (via N-terminus) with ATP6AP1 (via N-
CC terminus) (By similarity). Interacts with ATP6V0D1; ATP6V0D1 is a V-
CC ATPase complex subunit and the interaction promotes V-ATPase complex
CC assembly (PubMed:32764564). Interacts with TMEM9; TMEM9 is a V-ATPase
CC assembly regulator and the interaction induces the interaction with
CC ATP6V0D1 (By similarity). Interacts with VMA21 (via N-terminus); VMA21
CC is a V-ATPase accessory component (By similarity).
CC {ECO:0000250|UniProtKB:O75787, ECO:0000269|PubMed:32764564}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein
CC {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9CYN9};
CC Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle,
CC autophagosome membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type
CC I membrane protein {ECO:0000305}. Cell projection, dendritic spine
CC membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane
CC protein {ECO:0000305}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9CYN9}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9CYN9}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000269|PubMed:32764564}; Single-pass type I
CC membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass
CC type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:32764564}.
CC -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:O75787}.
CC -!- PTM: Proteolytically cleaved by a furin-like convertase in the trans-
CC Golgi network to generate N- and C-terminal fragments.
CC {ECO:0000250|UniProtKB:O75787}.
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DR EMBL; BC140624; AAI40625.1; -; mRNA.
DR RefSeq; NP_001091491.1; NM_001098022.1.
DR PDB; 6XBW; EM; 3.37 A; r=1-351.
DR PDB; 6XBY; EM; 3.79 A; r=1-351.
DR PDB; 7KHR; EM; 3.62 A; r=1-351.
DR PDBsum; 6XBW; -.
DR PDBsum; 6XBY; -.
DR PDBsum; 7KHR; -.
DR AlphaFoldDB; P81134; -.
DR SMR; P81134; -.
DR CORUM; P81134; -.
DR STRING; 9913.ENSBTAP00000023668; -.
DR PaxDb; P81134; -.
DR PRIDE; P81134; -.
DR Ensembl; ENSBTAT00000023668; ENSBTAP00000023668; ENSBTAG00000017801.
DR GeneID; 513520; -.
DR KEGG; bta:513520; -.
DR CTD; 10159; -.
DR VEuPathDB; HostDB:ENSBTAG00000017801; -.
DR eggNOG; KOG4737; Eukaryota.
DR GeneTree; ENSGT00390000008856; -.
DR InParanoid; P81134; -.
DR OrthoDB; 1179410at2759; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000017801; Expressed in spermatocyte and 102 other tissues.
DR ExpressionAtlas; P81134; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0030665; C:clathrin-coated vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032591; C:dendritic spine membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:0045851; P:pH reduction; IC:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:1902600; P:proton transmembrane transport; IC:UniProtKB.
DR InterPro; IPR012493; Renin_rcpt.
DR PANTHER; PTHR13351; PTHR13351; 1.
DR Pfam; PF07850; Renin_r; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection;
KW Cleavage on pair of basic residues; Cytoplasmic vesicle;
KW Direct protein sequencing; Endoplasmic reticulum; Endosome; Lysosome;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..351
FT /note="Renin receptor"
FT /id="PRO_0000097247"
FT CHAIN 18..276
FT /note="Renin receptor extracellular fragment"
FT /evidence="ECO:0000305"
FT /id="PRO_0000447862"
FT CHAIN 279..351
FT /note="Renin receptor cytoplasmic fragment"
FT /evidence="ECO:0000305"
FT /id="PRO_0000447863"
FT TOPO_DOM 18..303
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 325..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 347..351
FT /note="Mediates retrograde transport to the ER"
FT /evidence="ECO:0000250|UniProtKB:O75787"
FT SITE 276..277
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:O75787"
FT SITE 278..279
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:O75787"
FT HELIX 304..330
FT /evidence="ECO:0007829|PDB:6XBW"
SQ SEQUENCE 351 AA; 39491 MW; 73C3F05415452922 CRC64;
MAVLVVFLSF LVADVFGNEF SILRSPGSVV FRNGNWPIPG ERIPDVAALS MGFSVKEDLS
WPGLAVGNLF HRPRATVMVM VKGVDKLALP PGSVISYPLE NAVPFSLDSV ANSIHSLFSE
ETPVVLQLAP SEERVYMVGK ANSVFEDLSV TLRQLRNRLF QENSVLTSLP LNSLSRNNEV
DLLFLSELQV LRDISSLLSR HKHLAKDHSP DLYSLELAGL DEIGKHYGED SEQFRDASKI
LIDALQKFAD DMYNLYGGNA VVELVTVRSF DTSLVRKTRN ILETKQVKDP STTYNLAYKY
NFEYPVVFNL VLWIMIGLAL TLIVTCYNIW NMDPGYDSII YRMTNQKIRM D
