RENR_PONAB
ID RENR_PONAB Reviewed; 350 AA.
AC Q5R563;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
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 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 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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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. May mediate renin-dependent cellular
CC responses by activating ERK1 and ERK2. By increasing the catalytic
CC efficiency of renin in AGT/angiotensinogen conversion to angiotensin I,
CC may also play a role in the renin-angiotensin system (RAS) (By
CC similarity). Through its function in V-type ATPase (v-ATPase) assembly
CC and acidification of the lysosome it regulates protein degradation and
CC may control different signaling pathways important for proper brain
CC development, synapse morphology and synaptic transmission (By
CC similarity). {ECO:0000250|UniProtKB:O75787,
CC ECO:0000250|UniProtKB:Q9CYN9}.
CC -!- SUBUNIT: Interacts with renin. Accessory component of the multisubunit
CC proton-transporting vacuolar (V)-ATPase protein pump. Interacts (via N-
CC terminus) with ATP6AP1 (via N-terminus). Interacts with ATP6V0D1;
CC ATP6V0D1 is a V-ATPase complex subunit and the interaction promotes V-
CC ATPase complex assembly. Interacts with TMEM9; TMEM9 is a V-ATPase
CC assembly regulator and the interaction induces the interaction with
CC ATP6V0D1. Interacts with VMA21 (via N-terminus); VMA21 is a V-ATPase
CC accessory component. {ECO:0000250|UniProtKB:O75787}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O75787}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:O75787}. Lysosome membrane
CC {ECO:0000250|UniProtKB:O75787}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:O75787}. Cytoplasmic vesicle, autophagosome
CC membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane
CC protein {ECO:0000250|UniProtKB:O75787}. Cell projection, dendritic
CC spine membrane {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:O75787}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9CYN9}. Endosome membrane
CC {ECO:0000250|UniProtKB:Q9CYN9}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:O75787}. Cytoplasmic vesicle, clathrin-coated
CC vesicle membrane {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:O75787}. Cytoplasmic vesicle,
CC secretory vesicle, synaptic vesicle membrane
CC {ECO:0000250|UniProtKB:Q6AXS4}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:O75787}.
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; CR861006; CAH93103.1; -; mRNA.
DR RefSeq; NP_001126837.1; NM_001133365.1.
DR AlphaFoldDB; Q5R563; -.
DR SMR; Q5R563; -.
DR STRING; 9601.ENSPPYP00000022663; -.
DR Ensembl; ENSPPYT00000023623; ENSPPYP00000022663; ENSPPYG00000020251.
DR GeneID; 100173844; -.
DR KEGG; pon:100173844; -.
DR CTD; 10159; -.
DR eggNOG; KOG4737; Eukaryota.
DR GeneTree; ENSGT00390000008856; -.
DR HOGENOM; CLU_065819_0_0_1; -.
DR InParanoid; Q5R563; -.
DR OMA; QYAVIFN; -.
DR OrthoDB; 1179410at2759; -.
DR TreeFam; TF106137; -.
DR Proteomes; UP000001595; Chromosome X.
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; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016471; C:vacuolar proton-transporting V-type ATPase complex; ISS:UniProtKB.
DR GO; GO:0000220; C:vacuolar proton-transporting V-type ATPase, V0 domain; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0002003; P:angiotensin maturation; IEA:Ensembl.
DR GO; GO:0021626; P:central nervous system maturation; ISS:UniProtKB.
DR GO; GO:0048069; P:eye pigmentation; IEA:Ensembl.
DR GO; GO:0060323; P:head morphogenesis; IEA:Ensembl.
DR GO; GO:0007042; P:lysosomal lumen acidification; ISS:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; IEA:Ensembl.
DR GO; GO:0043408; P:regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0021903; P:rostrocaudal neural tube patterning; IEA:Ensembl.
DR InterPro; IPR012493; Renin_rcpt.
DR PANTHER; PTHR13351; PTHR13351; 1.
DR Pfam; PF07850; Renin_r; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cleavage on pair of basic residues;
KW Cytoplasmic vesicle; Endoplasmic reticulum; Endosome; Lysosome; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..350
FT /note="Renin receptor"
FT /id="PRO_0000022205"
FT CHAIN 17..275
FT /note="Renin receptor extracellular fragment"
FT /evidence="ECO:0000305"
FT /id="PRO_0000447868"
FT CHAIN 278..350
FT /note="Renin receptor cytoplasmic fragment"
FT /evidence="ECO:0000305"
FT /id="PRO_0000447869"
FT TOPO_DOM 17..302
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..350
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOTIF 346..350
FT /note="Mediates retrograde transport to the ER"
FT /evidence="ECO:0000250|UniProtKB:O75787"
FT SITE 275..276
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:O75787"
FT SITE 277..278
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:O75787"
SQ 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
