Apelin receptor A - Xenopus laevis (African clawed frog)

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P79960 (APJA_XENLA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Apelin receptor A

Alternative name(s):
Angiotensin receptor-like 1a
Short name=xAngio1
Angiotensin receptor-related protein A
G-protein coupled receptor APJ-A
Short name=APJa
Mesenchyme-associated serpentine receptor
Short name=x-MSR

Gene names

Name:	aplnr-a
Synonyms:	agtrl1, agtrl1-a, agtrl1a, angio1, msr

Organism

Xenopus laevis (African clawed frog)

Taxonomic identifier

8355 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for an apelin-like peptide coupled to G proteins that inhibit adenylate cyclase activity. Required for cardiovascular development, particularly for intersomitic vein angiogenesis. Acts upstream of the i/o type of G-alpha proteins in the differentiation of endothelium, erythroid cells, myeloid cells and cardiomyocytes. Ref.3 Ref.5 Ref.6
Subcellular location	Cell membrane; Multi-pass membrane protein. Note: Internalized to the cytoplasm after exposure to apelin. Ref.3
Tissue specificity	Expressed in all blood vessels including the posterior cardinal vein, intersomitic veins and the vitelline vein network. At the gastrula stage, exclusively expressed in the mesodermal layer and at the neurula stage in the lateral plate mesoderm. Larval expression is observed in the endothelium of the primary blood vessels and the forming heart. Ref.1 Ref.3 Ref.5 Ref.6
Developmental stage	Expression starts in the late blastula (stage 8), increases during gastrulation and remains constant between neurula and larva stages. Ref.1
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.
Sequence caution	The sequence AAB17004.1 differs from that shown. Reason: Erroneous termination at position 304. Translated as Tyr. The sequence AAI39487.1 differs from that shown. Reason: Frameshift at position 330. The sequence CAA63612.1 differs from that shown. Reason: Frameshift at position 330.

Ontologies

Keywords
Biological process	Angiogenesis Differentiation
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Developmental protein G-protein coupled receptor Receptor Transducer
PTM	Glycoprotein
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW patterning of blood vessels Inferred from mutant phenotype Ref.5. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay Ref.3. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	angiotensin type II receptor activity Inferred from electronic annotation. Source: InterPro apelin receptor activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 362

362

Apelin receptor A

PRO_0000069177

Regions

Topological domain

1 – 37

Extracellular Potential

Transmembrane

38 – 58

Helical; Name=1; Potential

Topological domain

59 – 76

Cytoplasmic Potential

Transmembrane

77 – 97

Helical; Name=2; Potential

Topological domain

98 – 110

Extracellular Potential

Transmembrane

111 – 131

Helical; Name=3; Potential

Topological domain

132 – 151

Cytoplasmic Potential

Transmembrane

152 – 172

Helical; Name=4; Potential

Topological domain

173 – 199

Extracellular Potential

Transmembrane

200 – 220

Helical; Name=5; Potential

Topological domain

221 – 248

Cytoplasmic Potential

Transmembrane

249 – 269

Helical; Name=6; Potential

Topological domain

270 – 296

Extracellular Potential

Transmembrane

297 – 317

Helical; Name=7; Potential

Topological domain

318 – 362

Cytoplasmic Potential

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Glycosylation

181

N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis

D → N: No phenotype when overexpressed. Ref.1

Sequence conflict

150

S → P in CAA63612. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P79960 [UniParc].

Last modified November 13, 2007. Version 2.
Checksum: 33B80895612B3B5D
Show »

FASTA

362

40,858

        10         20         30         40         50         60 
METEGLSPML YEDDYYYGNE TGLQPCDETD WDFSYSLLPV FYMIVFVLGL SGNGVVIFTV 

        70         80         90        100        110        120 
WKSKPKRRSA DTYIGNLALA DLAFVVTLPL WATYTALGFH WPFGSALCKL SSYLVLLNMF 

       130        140        150        160        170        180 
ASVFCLTCLS FDRYLAIVHS LSSAKLRSRS SIIVSLAVIW LFSGLLALPS LILRDTRVEG 

       190        200        210        220        230        240 
NNTICDLDFS GVSSKENENF WIGGLSILTT VPGFLLPLLL MTIFYCFIGG KVTMHFQNLK 

       250        260        270        280        290        300 
KEEQKKKRLL KIIITLVVVF AICWLPFHIL KTIHFLDLMG FLELSCSTQN IIVSLHPYAT 

       310        320        330        340        350        360 
CLAYVNSCLN PFLYAFFDLR FRSQCFFFFG FKKVLQGHLS NTSSSLSAQT QKSEIHSLAT 


KV

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression of a new G protein-coupled receptor X-msr is associated with an endothelial lineage in Xenopus laevis." Devic E., Paquereau L., Vernier P., Knibiehler B., Audigier Y. Mech. Dev. 59:129-140(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF ASP-81. Tissue: Gastrula.
[2]	"XAngio1, a novel Xenopus gene, is expressed in vascular precursor cells." Saha M.S., Oakes J.A., Miles R.R. Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Paracrine and autocrine mechanisms of apelin signaling govern embryonic and tumor angiogenesis." Kaelin R.E., Kretz M.P., Meyer A.M., Kispert A., Heppner F.L., Braendli A.W. Dev. Biol. 305:599-614(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Embryo.
[4]	NIH - Xenopus Gene Collection (XGC) project Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Neurula.
[5]	"Apelin, the ligand for the endothelial G-protein-coupled receptor, APJ, is a potent angiogenic factor required for normal vascular development of the frog embryo." Cox C.M., D'Agostino S.L., Miller M.K., Heimark R.L., Krieg P.A. Dev. Biol. 296:177-189(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[6]	"Xapelin and Xmsr are required for cardiovascular development in Xenopus laevis." Inui M., Fukui A., Ito Y., Asashima M. Dev. Biol. 298:188-200(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X93045 mRNA. Translation: CAA63612.1. Frameshift. U72029 mRNA. Translation: AAB17004.1. Sequence problems. DQ473441 mRNA. Translation: ABF19731.1. BC139486 mRNA. Translation: AAI39487.1. Frameshift.
RefSeq	NP_001084106.1. NM_001090637.1.
UniGene	Xl.23649.
3D structure databases
ProteinModelPortal	P79960.
ModBase	Search...
Protein family/group databases
GPCRDB	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	399306.
KEGG	xla:399306.
Organism-specific databases
CTD	399306.
Xenbase	XB-GENE-6254056. aplnr.
Phylogenomic databases
HOVERGEN	HBG104998.
KO	K04174.
Family and domain databases
InterPro	IPR000248. ATII_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00241. ANGIOTENSINR. PR00237. GPCRRHODOPSN.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

APJA_XENLA

Accession

Primary (citable) accession number: P79960
Secondary accession number(s): A1XP42, A4QNR6, P70058

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	November 13, 2007
Last modified:	April 3, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents