APJB_XENLA
ID APJB_XENLA Reviewed; 363 AA.
AC Q2TAD5; A1XP43; Q05BH5; Q7T0X4;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Apelin receptor B;
DE AltName: Full=Angiotensin receptor-like 1b;
DE AltName: Full=Angiotensin receptor-related protein B;
DE AltName: Full=G-protein coupled receptor APJ-B;
DE Short=APJb;
GN Name=aplnr-b; Synonyms=agtrl1-b, agtrl1b {ECO:0000312|EMBL:AAI10979.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:ABF19732.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryo {ECO:0000312|EMBL:ABF19732.1};
RX PubMed=17412318; DOI=10.1016/j.ydbio.2007.03.004;
RA Kaelin R.E., Kretz M.P., Meyer A.M., Kispert A., Heppner F.L.,
RA Braendli A.W.;
RT "Paracrine and autocrine mechanisms of apelin signaling govern embryonic
RT and tumor angiogenesis.";
RL Dev. Biol. 305:599-614(2007).
RN [2] {ECO:0000312|EMBL:AAI10979.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH46659.1}, and
RC Spleen {ECO:0000312|EMBL:AAI10979.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor for apelin receptor early endogenous ligand (apela)
CC and apelin (apln) hormones coupled to G proteins that inhibit adenylate
CC cyclase activity (PubMed:17412318). Plays a key role in early
CC development such as gastrulation, blood vessels formation and heart
CC morphogenesis by acting as a receptor for apela hormone, promoting
CC endoderm and mesendoderm cell migration and regulating the migration of
CC cells fated to become myocardial progenitors, respectively (By
CC similarity). Promotes angioblast migration toward the embryonic
CC midline, i.e. the position of the future vessel formation, during
CC vasculogenesis (By similarity). May promote sinus venosus (SV)-derived
CC endothelial cells migration into the developing heart to promote
CC coronary blood vessel development (By similarity). Required for
CC cardiovascular development, particularly for intersomitic vein
CC angiogenesis by acting as a receptor for apln hormone
CC (PubMed:17412318). Also plays a role in various processes in adults
CC such as regulation of blood vessel formation, blood pressure, heart
CC contractility, and heart failure. Acts upstream of the i/o type of G-
CC alpha proteins in the differentiation of endothelium, erythroid cells,
CC myeloid cells and cardiomyocytes (By similarity).
CC {ECO:0000250|UniProtKB:P35414, ECO:0000250|UniProtKB:P79960,
CC ECO:0000250|UniProtKB:Q7SZP9, ECO:0000250|UniProtKB:Q9WV08,
CC ECO:0000269|PubMed:17412318}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17412318};
CC Multi-pass membrane protein {ECO:0000269|PubMed:17412318}.
CC Note=Internalized to the cytoplasm after exposure to apelin (apln)
CC (PubMed:17412318). After exposure to apelin receptor early endogenous
CC ligand (apela), internalized from the cell surface into an endosomal
CC recycling compartment, from where it is recycled to the cell membrane
CC (By similarity). {ECO:0000250|UniProtKB:P35414,
CC ECO:0000269|PubMed:17412318}.
CC -!- TISSUE SPECIFICITY: Expressed in all blood vessels including the
CC posterior cardinal vein, intersomitic veins and the vitelline vein
CC network. {ECO:0000269|PubMed:17412318}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH55998.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ473442; ABF19732.1; -; mRNA.
DR EMBL; BC046659; AAH46659.1; -; mRNA.
DR EMBL; BC055998; AAH55998.1; ALT_FRAME; mRNA.
DR EMBL; BC110978; AAI10979.1; -; mRNA.
DR RefSeq; NP_001079847.1; NM_001086378.1.
DR AlphaFoldDB; Q2TAD5; -.
DR SMR; Q2TAD5; -.
DR DNASU; 379537; -.
DR GeneID; 379537; -.
DR KEGG; xla:379537; -.
DR CTD; 379537; -.
DR Xenbase; XB-GENE-6255483; aplnr.S.
DR OrthoDB; 788659at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 379537; Expressed in lung and 16 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0060182; F:apelin receptor activity; IDA:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB.
DR GO; GO:0060183; P:apelin receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0001568; P:blood vessel development; ISS:UniProtKB.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007369; P:gastrulation; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0043951; P:negative regulation of cAMP-mediated signaling; ISS:UniProtKB.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:1904325; P:positive regulation of inhibitory G protein-coupled receptor phosphorylation; ISS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR InterPro; IPR003904; Apelin_rcpt.
DR InterPro; IPR000248; ATII_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR24228:SF31; PTHR24228:SF31; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00241; ANGIOTENSINR.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Angiogenesis; Cell membrane; Developmental protein; Differentiation;
KW G-protein coupled receptor; Gastrulation; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..363
FT /note="Apelin receptor B"
FT /id="PRO_0000311701"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 60..77
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..152
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..249
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 250..270
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..297
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 14
FT /note="E -> D (in Ref. 1; ABF19732 and 2; AAH46659)"
FT /evidence="ECO:0000305"
FT CONFLICT 244
FT /note="E -> D (in Ref. 1; ABF19732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 363 AA; 40920 MW; 833D915AB777E9F9 CRC64;
MESEGFSATT EQYEYYDYAN ETGLQPCDET DWDFSYSLLP VFYMIVFVLG LSGNGVVIFT
VWKAKPKRRS ADTYIGNLAL ADLAFVVTLP LWATYTALGF HWPFGSALCK LSSYLVLLNM
FASVFCLTCL SFDRYLAIVH SLSSAKLRSR SSILVSLAVI WLFSGLLALP SLILRDTRVE
GNNTICDLDF SGVSSKENEN FWIGGLSILT TVPGFLLPLL LMTIFYCFIG GKVTMHFQNL
KKEEQKKKRL LKIIITLVVV FAICWLPFHI LKTIHFLDLM GFLELSCSAQ NIIVSLHPYA
TCLAYVNSCL NPFLYAFFDL RFRSQCFFFF GFKKVLQGHL SNTSSSLSAQ TQKSEIHSLA
TKV
