CXR4A_XENLA
ID CXR4A_XENLA Reviewed; 358 AA.
AC Q9YGC3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=C-X-C chemokine receptor type 4-A;
DE Short=CXC-R4-A;
DE Short=CXCR-4-A;
DE Short=xCXCR4 {ECO:0000303|PubMed:11069075};
DE AltName: Full=Stromal cell-derived factor 1 receptor A;
DE Short=SDF-1 receptor A;
GN Name=cxcr4-a; Synonyms=cxcr4 {ECO:0000312|EMBL:CAA76924.1};
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:CAA76923.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:11069075};
RX PubMed=11069075;
RX DOI=10.1002/1521-4141(200010)30:10<2924::aid-immu2924>3.0.co;2-y;
RA Moepps B., Braun M., Knoepfle K., Dillinger K., Knoechel W., Gierschik P.;
RT "Characterization of a Xenopus laevis CXC chemokine receptor 4:
RT implications for hematopoietic cell development in the vertebrate embryo.";
RL Eur. J. Immunol. 30:2924-2934(2000).
RN [2] {ECO:0000312|EMBL:AAH73603.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:AAH73603.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION.
RX PubMed=11859124; DOI=10.4049/jimmunol.168.5.2340;
RA Braun M., Wunderlin M., Spieth K., Knoechel W., Gierschik P., Moepps B.;
RT "Xenopus laevis stromal cell-derived factor 1: conservation of structure
RT and function during vertebrate development.";
RL J. Immunol. 168:2340-2347(2002).
RN [4] {ECO:0000305}
RP PUTATIVE FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15740585; DOI=10.1111/j.1440-169x.2004.00777.x;
RA Nishiumi F., Komiya T., Ikenishi K.;
RT "The mode and molecular mechanisms of the migration of presumptive PGC in
RT the endoderm cell mass of Xenopus embryos.";
RL Dev. Growth Differ. 47:37-48(2005).
RN [5] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=17239342; DOI=10.1016/j.bbrc.2007.01.007;
RA Fukui A., Goto T., Kitamoto J., Homma M., Asashima M.;
RT "SDF-1 alpha regulates mesendodermal cell migration during frog
RT gastrulation.";
RL Biochem. Biophys. Res. Commun. 354:472-477(2007).
CC -!- FUNCTION: Receptor for the C-X-C chemokine cxcl12/sdf-1. Transduces a
CC signal by increasing the intracellular level of calcium ions. Signaling
CC with cxcl12/sdf-1 mediates the directional movement of mesodermal cells
CC during gastrulation. May play a role in the migration of embryonic
CC presumptive primordial germ cells (pPGCs). May also be involved in
CC regulating the migration of hematopoietic stem cells into the larval
CC liver. {ECO:0000269|PubMed:11069075, ECO:0000269|PubMed:11859124,
CC ECO:0000269|PubMed:17239342}.
CC -!- SUBUNIT: Monomer. Can form dimers (By similarity).
CC {ECO:0000250|UniProtKB:P61073}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15740585}. Nucleus
CC {ECO:0000269|PubMed:15740585}. Early endosome {ECO:0000250}. Late
CC endosome {ECO:0000250}. Lysosome {ECO:0000250}. Note=Expressed in the
CC cytoplasm of a small number of embryonic pPGCs from stage 24. Expressed
CC in the nucleus of 3 lateral pPGCs. {ECO:0000255,
CC ECO:0000269|PubMed:15740585}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the embryonic nervous system
CC including forebrain, hindbrain and sensory organs (including eye), and
CC in neural crest cells. Also expressed in the dorsal lateral plate, the
CC first site of definitive hematopoiesis in the embryo. Appears in
CC migrating presumptive primordial germ cells (pPGCs) from stage 24.
CC Expressed in the epidermis at stage 40. In the adult, highly expressed
CC in the spleen with lower levels of expression in the liver and very low
CC levels in kidney, heart, skin and brain. {ECO:0000269|PubMed:11069075,
CC ECO:0000269|PubMed:15740585}.
CC -!- DEVELOPMENTAL STAGE: Expression is up-regulated between stages 14-18
CC (early neurula stages) and remains high until stage 30, decreasing only
CC at stage 45. {ECO:0000269|PubMed:11069075,
CC ECO:0000269|PubMed:17239342}.
CC -!- PTM: Sulfation is required for efficient binding of cxcl12/sdf-1alpha
CC and promotes its dimerization. {ECO:0000250|UniProtKB:P61073}.
CC -!- PTM: O- and N-glycosylated. {ECO:0000250|UniProtKB:P61073}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Y17894; CAA76923.1; -; mRNA.
DR EMBL; Y17895; CAA76924.1; -; Genomic_DNA.
DR EMBL; BC073603; AAH73603.1; -; mRNA.
DR RefSeq; NP_001131053.1; NM_001137581.1.
DR AlphaFoldDB; Q9YGC3; -.
DR SMR; Q9YGC3; -.
DR DNASU; 100192360; -.
DR GeneID; 100192360; -.
DR KEGG; xla:100192360; -.
DR CTD; 100192360; -.
DR Xenbase; XB-GENE-489921; cxcr4.L.
DR OrthoDB; 773026at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 100192360; Expressed in spleen and 18 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IC:UniProtKB.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016494; F:C-X-C chemokine receptor activity; IDA:UniProtKB.
DR GO; GO:0019955; F:cytokine binding; IEA:InterPro.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0060216; P:definitive hemopoiesis; IEP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; IEP:UniProtKB.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; IMP:UniProtKB.
DR InterPro; IPR022726; Chemokine_CXCR4_N_dom.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR001277; CXCR4/ACKR2.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF12109; CXCR4_N; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR00645; CXCCHMKINER4.
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 Cell membrane; Cytoplasm; Developmental protein; Disulfide bond; Endosome;
KW G-protein coupled receptor; Gastrulation; Glycoprotein; Lysosome; Membrane;
KW Nucleus; Receptor; Reference proteome; Sulfation; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..358
FT /note="C-X-C chemokine receptor type 4-A"
FT /id="PRO_0000379452"
FT TOPO_DOM 1..44
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 45..67
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250"
FT TOPO_DOM 68..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 82..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250"
FT TOPO_DOM 104..114
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 115..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250"
FT TOPO_DOM 135..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 159..178
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250"
FT TOPO_DOM 179..202
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 203..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250"
FT TOPO_DOM 224..248
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 249..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250"
FT TOPO_DOM 269..289
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 290..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250"
FT TOPO_DOM 310..358
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 1..25
FT /note="Important for chemokine binding and signaling"
FT /evidence="ECO:0000250"
FT REGION 98..101
FT /note="Chemokine binding"
FT /evidence="ECO:0000250"
FT REGION 117..121
FT /note="Chemokine binding"
FT /evidence="ECO:0000250"
FT REGION 139..151
FT /note="Involved in dimerization; when bound to chemokine"
FT /evidence="ECO:0000250"
FT REGION 190..194
FT /note="Chemokine binding, important for signaling"
FT /evidence="ECO:0000250"
FT REGION 338..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 175
FT /note="Chemokine binding"
FT /evidence="ECO:0000250"
FT SITE 295
FT /note="Chemokine binding"
FT /evidence="ECO:0000250"
FT CARBOHYD 16
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 20
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..281
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 113..190
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 358 AA; 40079 MW; 2E9EB448AE40ECB1 CRC64;
MDGFSGGIDI NIFDGNSTEN GSGDFEDFIE PCFMHENSDF NRIFLPTIYS FIFLLGIIGN
GLVVVVMGYQ KKSRTMTDKY RLHLSVADLL FVFTLPFWSV DAAIGWYFKE FLCKAVHVIY
TVNLYSSVLI LAFISLDRYL AIVHATNSQG SRKMLADKVV YAGVWLPALL LTVPDLVFAR
VSDENGQFVC DRIYPIENRE TWTVGFRFLH ITVGLILPGL IILICYCVII SKLSHSKGHQ
KRKALKTTVI LILAFFACWL PYYVCLTTDT FMLLGLVKGD CIWENTLHMA ISITEALAFF
HCCLNPILYA FLGAKFKTSA QNAFTSVSRG SSLKILSKKR AGLSSVSTES ESSSFHSS
