Cxcr4
entrez
12767
canonical
uniprot
P70658
canonical
ensembl
ENSMUSG00000045382
resolver
ensp
ENSMUSP00000053489
resolver
enst
ENSMUST00000052172
resolver
genesymbol
Cxcr4
resolver
genesymbol_syn
Cmkar4
resolver
genesymbol_syn
Lestr
resolver
genesymbol_syn
Sdf1r
resolver
uniprot
A0A0R4J0N8
resolver
uniprot
O09059
resolver
uniprot
O09062
resolver
uniprot
P70233
resolver
uniprot
P70346
resolver
uniprot
Q4KMW1
resolver
uniprot_entry
A0A0R4J0N8_MOUSE
resolver
uniprot_entry
CXCR4_MOUSE
resolver
uniprot_sec
O09059
resolver
uniprot_sec
O09062
resolver
uniprot_sec
P70233
resolver
uniprot_sec
P70346
resolver
uniprot_sec
Q4KMW1
resolver
amino_acid_sequence
MEPISVSIYTSDNYSEEVGSGDYDSNKEPCFRDENVHFNRIFLPTIYFIIFLTGIVGNGLVILVMGYQKKLRSMTDKYRLHLSVADLLFVITLPFWAVDAMADWYFGKFLCKAVHIIYTVNLYSSVLILAFISLDRYLAIVHATNSQRPRKLLAEKAVYVGVWIPALLLTIPDFIFADVSQGDISQGDDRYICDRLYPDSLWMVVFQFQHIMVGLILPGIVILSCYCIIISKLSHSKGHQKRKALKTTVILILAFFACWLPYYVGISIDSFILLGVIKQGCDFESIVHKWISITEALAFFHCCLNPILYAFLGAKFKSSAQHALNSMSRGSSLKILSKGKRGGHSSVSTESESSSFHSS
uniprot
proteins
function
FUNCTION: Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation (PubMed:8962122, PubMed:9103415, PubMed:9295051). Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase (By similarity). CXCR4 is coupled to G(i) G alpha proteins and mediates inhibition of adenylate cyclase (By similarity). Involved in the AKT signaling cascade (By similarity). Plays a role in regulation of cell migration, e.g. during wound healing (By similarity). Also acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels (By similarity). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (By similarity). Involved in hematopoiesis and in cardiac ventricular septum formation (PubMed:9634237, PubMed:9634238, PubMed:9689100). Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells (PubMed:9634237). Involved in cerebellar development; in the CNS, could mediate hippocampal-neuron surviva (PubMed:9634238, PubMed:9689100). {ECO:0000250|UniProtKB:P61073, ECO:0000269|PubMed:8962122, ECO:0000269|PubMed:9103415, ECO:0000269|PubMed:9295051, ECO:0000269|PubMed:9634237, ECO:0000269|PubMed:9634238, ECO:0000269|PubMed:9689100}.
uniprot
proteins
mass_dalton
40426
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on agonist stimulation. Phosphorylation of the P-X-P-P motif promotes association with beta-arrestin ARRB1, leading to receptor desensitization and negative regulation of G protein-coupled receptor signaling. Phosphorylation at Ser-331 and Ser-332 leads to recruitment of ITCH, ubiquitination and protein degradation. {ECO:0000250|UniProtKB:P61073}.; PTM: Ubiquitinated after ligand binding, leading to its degradation. Ubiquitinated by ITCH at the cell membrane on agonist stimulation. The ubiquitin-dependent mechanism, endosomal sorting complex required for transport (ESCRT), then targets CXCR4 for lysosomal degradation. This process is dependent also on prior Ser-/Thr-phosphorylation in the C-terminal of CXCR4. Also binding of ARRB1 to STAM negatively regulates CXCR4 sorting to lysosomes though modulating ubiquitination of SFR5S. {ECO:0000250|UniProtKB:P61073}.; PTM: Sulfation is required for efficient binding of CXCL12/SDF-1alpha and promotes its dimerization. {ECO:0000250|UniProtKB:P61073}.; PTM: O- and N-glycosylated. N-glycosylation can mask coreceptor function. The O-glycosylation chondroitin sulfate attachment does not affect interaction with CXCL12/SDF-1alpha nor its coreceptor activity. {ECO:0000250|UniProtKB:P61073}.
uniprot
proteins
protein_family
G protein-coupled receptor 1 family
uniprot
proteins
pubmed
10479460
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18227060
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8955194
uniprot
proteins
pubmed
8962122
uniprot
proteins
pubmed
9103415
uniprot
proteins
pubmed
9295051
uniprot
proteins
pubmed
9634237
uniprot
proteins
pubmed
9634238
uniprot
proteins
pubmed
9689100
uniprot
proteins
pubmed
9879064
uniprot
proteins
sequence_length
359
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8962122, ECO:0000269|PubMed:9295051}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P61073}. Cell junction {ECO:0000250|UniProtKB:P61073}. Early endosome {ECO:0000250|UniProtKB:P61073}. Late endosome {ECO:0000250|UniProtKB:P61073}. Lysosome {ECO:0000250|UniProtKB:P61073}. Note=In unstimulated cells, diffuse pattern on plasma membrane. On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated. In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation cluster (SMAC). {ECO:0000250|UniProtKB:P61073}.
uniprot
proteins
transmembrane_region
TRANSMEM 41..65; /note="Helical; Name=1"; /evidence="ECO:0000250|UniProtKB:P61073"; TRANSMEM 80..101; /note="Helical; Name=2"; /evidence="ECO:0000250|UniProtKB:P61073"; TRANSMEM 113..132; /note="Helical; Name=3"; /evidence="ECO:0000250|UniProtKB:P61073"; TRANSMEM 157..176; /note="Helical; Name=4"; /evidence="ECO:0000250|UniProtKB:P61073"; TRANSMEM 203..223; /note="Helical; Name=5"; /evidence="ECO:0000250|UniProtKB:P61073"; TRANSMEM 249..268; /note="Helical; Name=6"; /evidence="ECO:0000250|UniProtKB:P61073"; TRANSMEM 290..309; /note="Helical; Name=7"; /evidence="ECO:0000250|UniProtKB:P61073
uniprot
proteins