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O75787 (RENR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Renin receptor
Alternative name(s):
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
Short name=ATP6M8-9
Short name=V-ATPase M8.9 subunit
Gene names
Name:ATP6AP2
Synonyms:ATP6IP2, CAPER, ELDF10
ORF Names:HT028, MSTP009, PSEC0072
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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). Ref.1

Subunit structure

Interacts with renin and the vacuolar proton-ATPase. Ref.1

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

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. Ref.1 Ref.10

Post-translational modification

Phosphorylated. Ref.1

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12

Sequence caution

The sequence AAH10395.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAQ13511.1 differs from that shown. Reason: Frameshift at position 155. Translation N-terminally extended.

The sequence CAA76984.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseEpilepsy
Mental retardation
Neurodegeneration
Parkinsonism
   DomainSignal
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiotensin maturation

Inferred from direct assay Ref.1Ref.10. Source: HGNC

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein metabolic process

Traceable author statement. Source: Reactome

positive regulation of transforming growth factor beta1 production

Inferred from direct assay PubMed 16374430. Source: HGNC

proteolysis

Inferred from experiment. Source: GOC

regulation of MAPK cascade

Inferred from direct assay Ref.1Ref.10. Source: HGNC

   Cellular_componentcell body

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from direct assay Ref.1Ref.10. Source: HGNC

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708PubMed 23376485. Source: UniProt

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionaspartic-type endopeptidase activity

Inferred from experiment. Source: Reactome

protein binding

Inferred from physical interaction Ref.1. Source: HGNC

receptor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 350334Renin receptor
PRO_0000022203

Regions

Topological domain17 – 302286Extracellular Potential
Transmembrane303 – 32321Helical; Potential
Topological domain324 – 35027Cytoplasmic Potential

Natural variations

Natural variant901P → A.
Corresponds to variant rs9014 [ dbSNP | Ensembl ].
VAR_051313
Natural variant2901A → P.
Corresponds to variant rs35798522 [ dbSNP | Ensembl ].
VAR_051314

Experimental info

Sequence conflict1381G → W in AAK83467. Ref.2
Sequence conflict153 – 1542QL → HV in AAK83467. Ref.2
Sequence conflict2581N → K in BAC11582. Ref.5
Sequence conflict2851Q → R Ref.4
Sequence conflict2851Q → R Ref.8
Sequence conflict2871Missing in AAH10395. Ref.6

Secondary structure

.... 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75787 [UniParc].

Last modified May 10, 2005. Version 2.
Checksum: 84084A4ACE9C5DE8

FASTA35039,008
        10         20         30         40         50         60 
MAVFVVLLAL VAGVLGNEFS ILKSPGSVVF RNGNWPIPGE RIPDVAALSM GFSVKEDLSW 

        70         80         90        100        110        120 
PGLAVGNLFH RPRATVMVMV KGVNKLALPP GSVISYPLEN AVPFSLDSVA NSIHSLFSEE 

       130        140        150        160        170        180 
TPVVLQLAPS EERVYMVGKA NSVFEDLSVT LRQLRNRLFQ ENSVLSSLPL NSLSRNNEVD 

       190        200        210        220        230        240 
LLFLSELQVL HDISSLLSRH KHLAKDHSPD LYSLELAGLD EIGKRYGEDS EQFRDASKIL 

       250        260        270        280        290        300 
VDALQKFADD MYSLYGGNAV VELVTVKSFD TSLIRKTRTI LEAKQAKNPA SPYNLAYKYN 

       310        320        330        340        350 
FEYSVVFNMV LWIMIALALA VIITSYNIWN MDPGYDSIIY RMTNQKIRMD 

« Hide

References

« Hide 'large scale' references
[1]"Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin."
Nguyen G., Delarue F., Burckle C., Bouzhir L., Giller T., Sraer J.-D.
J. Clin. Invest. 109:1417-1427(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH REN, PHOSPHORYLATION, TISSUE SPECIFICITY, FUNCTION.
Tissue: Mesangial cell.
[2]"Cell cycle-dependent subcellular localization of the protein tyrosine phosphatase PTPCAAX1 and its implication in cell cycle regulation."
Wang J., Kirby C., Herbst R.
Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Cervix carcinoma.
[3]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Aorta.
[4]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
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. expand/collapse author list , 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.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hypothalamus.
[5]"Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
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. expand/collapse author list , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Teratocarcinoma.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain and Prostate.
[7]"The cloning of a novel gene related with erythroid differentiation."
Zhang S., Yan H., Yang F.
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-350.
Tissue: Liver.
[8]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 21-350.
Tissue: Brain.
[9]"Identification and characterization of a novel 9.2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules."
Ludwig J., Kerscher S., Brandt U., Pfeiffer K., Getlawi F., Apps D.K., Schaegger H.
J. Biol. Chem. 273:10939-10947(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 188-350.
[10]"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."
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.
Hum. Mol. Genet. 14:1019-1027(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRXE, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Altered splicing of ATP6AP2 causes X-linked parkinsonism with spasticity (XPDS)."
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.
Hum. Mol. Genet. 22:3259-3268(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN XPDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF291814 mRNA. Translation: AAM47531.1.
AY038990 mRNA. Translation: AAK83467.1.
AF109363 mRNA. Translation: AAQ13511.1. Frameshift.
AF248966 mRNA. Translation: AAG44564.1.
AK075382 mRNA. Translation: BAC11582.1.
BC010395 mRNA. Translation: AAH10395.1. Different initiation.
BC084541 mRNA. Translation: AAH84541.1.
AY429341 mRNA. Translation: AAR06910.1.
AL049929 mRNA. Translation: CAB43210.1.
Y17975 mRNA. Translation: CAA76984.1. Different initiation.
CCDSCCDS14252.1.
PIRT08667.
RefSeqNP_005756.2. NM_005765.2.
UniGeneHs.495960.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3LBSX-ray2.15A/B333-350[»]
3LC8X-ray2.00A/B333-350[»]
ProteinModelPortalO75787.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115461. 8 interactions.
IntActO75787. 3 interactions.

PTM databases

PhosphoSiteO75787.

Proteomic databases

MaxQBO75787.
PaxDbO75787.
PRIDEO75787.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378438; ENSP00000367697; ENSG00000182220.
GeneID10159.
KEGGhsa:10159.
UCSCuc004det.3. human.

Organism-specific databases

CTD10159.
GeneCardsGC0XP040440.
HGNCHGNC:18305. ATP6AP2.
HPAHPA003156.
MIM300423. phenotype.
300556. gene.
300911. phenotype.
neXtProtNX_O75787.
Orphanet93952. X-linked intellectual disability, Hedera type.
363654. X-linked parkinsonism-spasticity syndrome.
PharmGKBPA25148.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG296465.
HOVERGENHBG056579.
InParanoidO75787.
OMAFRDGNWP.
OrthoDBEOG7R56VH.
PhylomeDBO75787.
TreeFamTF106137.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER66-34369.
ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressO75787.
BgeeO75787.
GenevestigatorO75787.

Family and domain databases

InterProIPR012493. Renin_rcpt.
[Graphical view]
PANTHERPTHR13351. PTHR13351. 1 hit.
PfamPF07850. Renin_r. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSATP6AP2. human.
GeneWikiATP6AP2.
GenomeRNAi10159.
NextBio38460.
PROO75787.
SOURCESearch...

Entry information

Entry nameRENR_HUMAN
AccessionPrimary (citable) accession number: O75787
Secondary accession number(s): Q5QTQ7 expand/collapse secondary AC list , Q6T7F5, Q8NBP3, Q8NG15, Q96FV6, Q96LB5, Q9H2P8, Q9UG89
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 10, 2005
Last modified: July 9, 2014
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM