O75787 (RENR_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Defects in ATP6AP2 are a cause of mental retardation X-linked with epilepsy (MRXE) [MIM:300423]. MRXE is a syndromic mental retardation. Patients manifest mild to moderate mental retardation associated with epilepsy, delays in motor milestones and speech acquisition in infancy. Ref.10
Sequence caution	The sequence AAH10395.1 differs from that shown. Reason: Erroneous initiation. The sequence AAQ13511.1 differs from that shown. Reason: Frameshift at position 155. The sequence CAA76984.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Epilepsy Mental retardation
Domain	Signal Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	angiotensin maturation Inferred from direct assay Ref.1Ref.10. Source: HGNC positive regulation of transforming growth factor beta1 production Inferred from direct assay. Source: HGNC regulation of MAPKKK cascade Inferred from direct assay Ref.1Ref.10. Source: HGNC
Cellular component	external side of plasma membrane Inferred from direct assay Ref.1Ref.10. Source: HGNC integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from physical interaction Ref.1. Source: HGNC receptor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Potential

Chain

17 – 350

334

Renin receptor

PRO_0000022203

Regions

Topological domain

17 – 302

286

Extracellular Potential

Transmembrane

303 – 323

21

Helical; Potential

Topological domain

324 – 350

27

Cytoplasmic Potential

Natural variations

Natural variant

90

1

P → A.
Corresponds to variant rs9014 [ dbSNP | Ensembl ].

VAR_051313

Natural variant

290

1

A → P.
Corresponds to variant rs35798522 [ dbSNP | Ensembl ].

VAR_051314

Experimental info

Sequence conflict

138

1

G → W in AAK83467. Ref.2

Sequence conflict

153 – 154

2

QL → HV in AAK83467. Ref.2

Sequence conflict

258

1

N → K in BAC11582. Ref.5

Sequence conflict

285

1

Q → R Ref.4

Sequence conflict

285

1

Q → R Ref.8

Sequence conflict

287

1

Missing in AAH10395. Ref.6

Secondary structure

1

.

.

.

350

Helix Strand Turn

Details...

Turn

334 – 337

4

Sequences

	Sequence		Length	Mass (Da)
	O75787 [UniParc]. Last modified May 10, 2005. Version 2. Checksum: 84084A4ACE9C5DE8	FASTA	350	39,008
	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

References

	« Hide 'large scale' referencesShow '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: 12045255] [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. , 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. , 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: 10931946] [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. , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T. DNA Res. 12:117-126(2005) [PubMed: 16303743] [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: 15489334] [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: 17974005] [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: 9556572] [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: 15746149] [Abstract] Cited for: INVOLVEMENT IN MRXE, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
+	Additional computationally mapped references.

Web resources

GeneReviews

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.

IPI

IPI00168884.

PIR

T08667.

RefSeq

NP_005756.2. NM_005765.2.

UniGene

Hs.495960.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3LBS	X-ray	2.15	A/B	333-349	[»]
3LC8	X-ray	2.00	A/B	333-349	[»]

ProteinModelPortal

O75787.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75787. 2 interactions.

STRING

O75787.

PTM databases

PhosphoSite

O75787.

Proteomic databases

PRIDE

O75787.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000378438; ENSP00000367697; ENSG00000182220.

GeneID

10159.

KEGG

hsa:10159.

UCSC

uc004det.1. human.

Organism-specific databases

CTD

10159.

GeneCards

GC0XP040440.

H-InvDB

HIX0016733.

HGNC

HGNC:18305. ATP6AP2.

HPA

HPA003156.

MIM

300423. phenotype.
300556. gene.

neXtProt

NX_O75787.

Orphanet

2076. X-linked intellectual deficit - epilepsy.

PharmGKB

PA25148.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG08935.

GeneTree

ENSGT00390000008856.

HOVERGEN

HBG056579.

InParanoid

O75787.

OMA

FRDGNWP.

OrthoDB

EOG4R7VB4.

PhylomeDB

O75787.

Gene expression databases

ArrayExpress

O75787.

Bgee

O75787.

Genevestigator

O75787.

GermOnline

ENSG00000182220. Homo sapiens.

Family and domain databases

InterPro

IPR012493. Renin_rcpt.
[Graphical view]

PANTHER

PTHR13351. Renin_rcpt. 1 hit.

Pfam

PF07850. Renin_r. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

38460.

SOURCE

Search...

Entry information

Entry name

RENR_HUMAN

Accession

Primary (citable) accession number: O75787
Secondary accession number(s): Q5QTQ7 , 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:	January 25, 2012
This is version 103 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.