CXR4B_XENLA
ID CXR4B_XENLA Reviewed; 358 AA.
AC Q7ZXJ7;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=C-X-C chemokine receptor type 4-B;
DE Short=CXC-R4-B;
DE Short=CXCR-4-B;
DE AltName: Full=Stromal cell-derived factor 1 receptor B;
DE Short=SDF-1 receptor B;
GN Name=cxcr4-b; Synonyms=cxcr4;
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:0000312|EMBL:AAH44963.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH44963.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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 migration of hematopoietic stem cells into the larval liver
CC (By similarity). {ECO:0000250}.
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:0000250|UniProtKB:Q9YGC3,
CC ECO:0000255}. Nucleus {ECO:0000250|UniProtKB:Q9YGC3, ECO:0000255}.
CC Early endosome {ECO:0000250}. Late endosome {ECO:0000250}. Lysosome
CC {ECO:0000250}. Note=Expressed in the cytoplasm of a small number of
CC embryonic pPGCs from stage 24. Expressed in the nucleus of 3 lateral
CC pPGCs (By similarity). {ECO:0000250|UniProtKB:Q9YGC3, ECO:0000255}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC044963; AAH44963.1; -; mRNA.
DR EMBL; BC110721; AAI10722.1; -; mRNA.
DR RefSeq; NP_001080681.1; NM_001087212.1.
DR AlphaFoldDB; Q7ZXJ7; -.
DR SMR; Q7ZXJ7; -.
DR DNASU; 380373; -.
DR GeneID; 380373; -.
DR KEGG; xla:380373; -.
DR CTD; 380373; -.
DR Xenbase; XB-GENE-6256540; cxcr4.S.
DR OMA; TIVHKWI; -.
DR OrthoDB; 773026at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 380373; Expressed in gastrula and 19 other tissues.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0016494; F:C-X-C chemokine receptor activity; ISS: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; ISS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; ISS:UniProtKB.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; ISS: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-B"
FT /id="PRO_0000379453"
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; 40028 MW; 7FBBB508DB9CCD01 CRC64;
MDGFSGGIDI NIFDGNSTEN GSGDFEDFIE PCFMQENSDF NRIFLPTIYS FIFLLGIIGN
GLVVVVMGYQ KKSRTMTDKY RLHLSVADLL FVFTLPFWSV DAAIGWYFKE FLCKAVHVIY
TVNLYSSVLI LAFISLDRYL AIVHATNSQG SRKMLADKVV YAGVWLPALL LTVPDLVFAS
VSNENGQFVC DRIYPIDNRE TWTVGFRFLH ITVGLILPGL IILVCYCVII SKLSHSKGHQ
KRKALKTTVI LILAFFACWL PYYVCLTTDT FMMLGLVKAD CIWENTLHKA ISITEALAFF
HCCLNPILYA FLGAKFKKSA QNAFTSVSRG SSLKILSKKR AGLSSVSTES ESSSFHSS
