CXCL12
entrez
6387
canonical
uniprot
P48061
canonical
ensembl
ENSG00000107562
resolver
ensp
ENSP00000339913
resolver
ensp
ENSP00000363548
resolver
ensp
ENSP00000363551
resolver
ensp
ENSP00000379139
resolver
ensp
ENSP00000379140
resolver
genesymbol
CXCL12
resolver
genesymbol_syn
SDF1
resolver
genesymbol_syn
SDF1A
resolver
genesymbol_syn
SDF1B
resolver
hgnc
HGNC:10672
resolver
uniprot
B2R4G0
resolver
uniprot
E7EVL0
resolver
uniprot
H7BYN8
resolver
uniprot
Q2L985
resolver
uniprot
Q2L986
resolver
uniprot
Q2L988
resolver
uniprot
Q5IT36
resolver
uniprot
Q6ICW0
resolver
uniprot
Q9H554
resolver
uniprot_entry
SDF1_HUMAN
resolver
uniprot_sec
B2R4G0
resolver
uniprot_sec
E7EVL0
resolver
uniprot_sec
H7BYN8
resolver
uniprot_sec
Q2L985
resolver
uniprot_sec
Q2L986
resolver
uniprot_sec
Q2L988
resolver
uniprot_sec
Q5IT36
resolver
uniprot_sec
Q6ICW0
resolver
uniprot_sec
Q9H554
resolver
amino_acid_sequence
MNAKVVVVLVLVLTALCLSDGKPVSLSYRCPCRFFESHVARANVKHLKILNTPNCALQIVARLKNNNRQVCIDPKLKWIQEYLEKALNKRFKM
uniprot
proteins
function
FUNCTION: Chemoattractant active on T-lymphocytes and monocytes but not neutrophils (PubMed:18802065, PubMed:39093700). Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis (PubMed:8752281, PubMed:18802065, PubMed:39093700). Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for CXCL12/SDF-1 (PubMed:16107333, PubMed:19255243). Binds to the allosteric site (site 2) of integrins and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 in a CXCR4-independent manner (PubMed:29301984). Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase (PubMed:18802065). Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins (PubMed:16107333, PubMed:18802065, PubMed:19255243, PubMed:39093700). CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase (PubMed:18802065). Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1 (PubMed:8752281). Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation (By similarity). Stimulates the proliferation of bone marrow-derived B-cell progenitors in the presence of IL7 as well as growth of stromal cell-dependent pre-B-cells (By similarity). {ECO:0000250|UniProtKB:P40224, ECO:0000269|PubMed:11069075, ECO:0000269|PubMed:11859124, ECO:0000269|PubMed:16107333, ECO:0000269|PubMed:18802065, ECO:0000269|PubMed:19255243, ECO:0000269|PubMed:29301984, ECO:0000269|PubMed:39093700, ECO:0000269|PubMed:8752281}.; FUNCTION: [SDF-1-beta(3-72)]: Shows a reduced chemotactic activity. {ECO:0000269|PubMed:14525775}.; FUNCTION: [SDF-1-alpha(3-67)]: Shows a reduced chemotactic activity (PubMed:14525775). Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites (PubMed:14525775). {ECO:0000269|PubMed:14525775}.
uniprot
proteins
mass_dalton
10666
uniprot
proteins
mutagenesis
MUTAGEN 22..23; /note="Missing: Abolished CXCR4 activation ability, but only slightly impaired binding to the receptor."; /evidence="ECO:0000269|PubMed:9384579"; MUTAGEN 22; /note="K->A: Loss of chemotactic activity."; /evidence="ECO:0000269|PubMed:17357154, ECO:0000269|PubMed:9384579"; MUTAGEN 22; /note="K->R: Abolished CXCR4 activation ability, but only slightly impaired binding to the receptor."; /evidence="ECO:0000269|PubMed:17357154, ECO:0000269|PubMed:9384579"; MUTAGEN 22; /note="Missing: Abolished CXCR4 activation ability, but only slightly impaired binding to the receptor."; /evidence="ECO:0000269|PubMed:17357154, ECO:0000269|PubMed:9384579"; MUTAGEN 23; /note="P->G: Abolished CXCR4 activation ability, but only slightly impaired binding to the receptor."; /evidence="ECO:0000269|PubMed:9384579"; MUTAGEN 25..27; /note="SLS->AQA: Significantly impaired CXCR4 activation ability, but only slightly impaired binding to the receptor."; /evidence="ECO:0000269|PubMed:9384579"; MUTAGEN 28; /note="Y->A: Impaired CXCR4 activation ability, but only slightly impaired binding to the receptor."; /evidence="ECO:0000269|PubMed:9384579"; MUTAGEN 28; /note="Y->H: No significant effect on CXCR4 binding or activation."; /evidence="ECO:0000269|PubMed:9384579"; MUTAGEN 29; /note="R->K: Slightly impaired binding and activation of CXCR4."; /evidence="ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:9384579"; MUTAGEN 29; /note="R->Q: Greatly impaired chemotactic activity and enhanced inhibition by heparin."; /evidence="ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:9384579"; MUTAGEN 33..38; /note="RFFESH->AAAAAA: Significantly decreased chemotactic activity."; /evidence="ECO:0000269|PubMed:10954912"; MUTAGEN 33; /note="R->A: Significantly decreased anti-HIV-1 and chemotactic activities."; /evidence="ECO:0000269|PubMed:10954912, ECO:0000269|PubMed:17264079"; MUTAGEN 33; /note="R->Q: Slightly impaired chemotactic activity and enhanced inhibition by heparin. Greatly impaired chemotactic activity; when associated with Q-29."; /evidence="ECO:0000269|PubMed:10954912, ECO:0000269|PubMed:17264079"; MUTAGEN 34; /note="F->A: No effect on anti-HIV-1 and chemotactic activities. Slightly impaired chemotactic activity and no effect on inhibition by heparin; when associated with A-35."; /evidence="ECO:0000269|PubMed:10954912"; MUTAGEN 35; /note="F->A: No effect on anti-HIV-1 and chemotactic activities. Slightly impaired chemotactic activity and no effect on inhibition by heparin; when associated with A-34."; /evidence="ECO:0000269|PubMed:10954912"; MUTAGEN 36..38; /note="ESH->QSN: Slightly impaired chemotactic activity, no effect on inhibition by heparin."; /evidence="ECO:0000269|PubMed:17264079"; MUTAGEN 36; /note="E->A: No effect on anti-HIV-1 and chemotactic activities."; /evidence="ECO:0000269|PubMed:10954912"; MUTAGEN 37; /note="S->A: No effect on anti-HIV-1 and chemotactic activities."; /evidence="ECO:0000269|PubMed:10954912"; MUTAGEN 38; /note="H->A: No effect on anti-HIV-1 and chemotactic activities."; /evidence="ECO:0000269|PubMed:10954912"; MUTAGEN 41; /note="R->A: No effect on CXCR4 activation."; /evidence="ECO:0000269|PubMed:18799424"; MUTAGEN 45..48; /note="KHLK->SSLS: Loss of heparin-binding capacity."; /evidence="ECO:0000269|PubMed:10446158"; MUTAGEN 45; /note="K->E: Loss of integrin activation; when associated with E-48 or E-64."; /evidence="ECO:0000269|PubMed:29301984"; MUTAGEN 45; /note="K->S: 55-fold reduction in binding affinity for Link domain of TNFAIP6; when associated with S-46 and S-48."; /evidence="ECO:0000269|PubMed:27044744"; MUTAGEN 46; /note="H->A: Reduced dimerization in neutral pH. Eliminates the pH dependence of dimerization."; /evidence="ECO:0000269|PubMed:15741341, ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 46; /note="H->L: No significant effect on dimerization in neutral pH. Eliminates the pH dependence of dimerization."; /evidence="ECO:0000269|PubMed:15741341, ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 46; /note="H->N: Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with Q-48; Q-62; Q-68 and N-69."; /evidence="ECO:0000269|PubMed:15741341, ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 46; /note="H->R: No effect on CXCR4 activation. Impaired dimer formation, leading to increased chemotactic activity. Eliminates the pH dependence of dimerization."; /evidence="ECO:0000269|PubMed:15741341, ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 46; /note="H->S: 55-fold reduction in binding affinity for Link domain of TNFAIP6; when associated with S-45 and S-48."; /evidence="ECO:0000269|PubMed:27044744"; MUTAGEN 48; /note="K->A: Impaired CXCR4 activation."; /evidence="ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 48; /note="K->E: Impaired CXCR4 activation. Loss of integrin activation; when associated with E-45 or E-64."; /evidence="ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424, ECO:0000269|PubMed:29301984"; MUTAGEN 48; /note="K->Q: Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-62; Q-68 and N-69."; /evidence="ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 48; /note="K->S: 55-fold reduction in binding affinity for Link domain of TNFAIP6; when associated with S-45 and S-46."; /evidence="ECO:0000269|PubMed:27044744"; MUTAGEN 52..56; /note="TPNCA->GPGCG: Slightly impaired chemotactic activity, no effect on inhibition by heparin."; /evidence="ECO:0000269|PubMed:17264079"; MUTAGEN 57; /note="L->C: Formation of an intermolecular disulfide bond, leading to a locked dimer; when associated with C-86. No effect on CXCR4 activation, but loss of chemotactic activity; when associated with C-86."; MUTAGEN 60; /note="V->A: Impaired CXCR4 activation."; /evidence="ECO:0000269|PubMed:18799424"; MUTAGEN 62; /note="R->A: No effect on CXCR4 activation."; /evidence="ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 62; /note="R->Q: Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-48; Q-68 and N-69."; /evidence="ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 64; /note="K->E: Loss of integrin activation; when associated with E-45 or E-48."; /evidence="ECO:0000269|PubMed:29301984"; MUTAGEN 68; /note="R->A: Impaired CXCR4 activation."; /evidence="ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 68; /note="R->E: Greatly impaired CXCR4 activation."; /evidence="ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 68; /note="R->Q: Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-48; Q-62 and N-69."; /evidence="ECO:0000269|PubMed:17264079, ECO:0000269|PubMed:18799424"; MUTAGEN 69; /note="Q->N: Slightly impaired CXCR4 activation and clear resistance to inhibition by heparin; when associated with N-46; Q-48; Q-62 and Q-68."; /evidence="ECO:0000269|PubMed:17264079"; MUTAGEN 70; /note="V->A: Impaired CXCR4 activation."; /evidence="ECO:0000269|PubMed:18799424"; MUTAGEN 81; /note="E->A: No effect on CXCR4 activation."; /evidence="ECO:0000269|PubMed:18799424"; MUTAGEN 84; /note="E->A: No effect on CXCR4 activation."; /evidence="ECO:0000269|PubMed:18799424"; MUTAGEN 85; /note="K->A: No effect on CXCR4 activation."; /evidence="ECO:0000269|PubMed:18799424"; MUTAGEN 86; /note="A->C: Formation of an intermolecular disulfide bond, leading to a locked dimer; when associated with C-57. No effect on CXCR4 activation, but loss of chemotactic activity; when associated with C-57.
uniprot
proteins
post_translational_modification
PTM: Processed forms SDF-1-beta(3-72) and SDF-1-alpha(3-67) are produced after secretion by proteolytic cleavage of isoforms Beta and Alpha, respectively. The N-terminal processing is probably achieved by DPP4. Isoform Alpha is first cleaved at the C-terminus to yield a SDF-1-alpha(1-67) intermediate before being processed at the N-terminus. The C-terminal processing of isoform Alpha is reduced by binding to heparin and, probably, cell surface proteoglycans. {ECO:0000269|PubMed:14525775}.
uniprot
proteins
protein_family
Intercrine alpha (chemokine CxC) family
uniprot
proteins
pubmed
10446158
uniprot
proteins
pubmed
10954912
uniprot
proteins
pubmed
11069075
uniprot
proteins
pubmed
11859124
uniprot
proteins
pubmed
14525775
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15588815
uniprot
proteins
pubmed
15741341
uniprot
proteins
pubmed
16107333
uniprot
proteins
pubmed
16344560
uniprot
proteins
pubmed
16626895
uniprot
proteins
pubmed
16725153
uniprot
proteins
pubmed
17264079
uniprot
proteins
pubmed
17357154
uniprot
proteins
pubmed
18799424
uniprot
proteins
pubmed
18802065
uniprot
proteins
pubmed
19255243
uniprot
proteins
pubmed
19551879
uniprot
proteins
pubmed
20077567
uniprot
proteins
pubmed
21802105
uniprot
proteins
pubmed
22457824
uniprot
proteins
pubmed
27044744
uniprot
proteins
pubmed
29301984
uniprot
proteins
pubmed
39093700
uniprot
proteins
pubmed
7490086
uniprot
proteins
pubmed
8752281
uniprot
proteins
pubmed
9384579
uniprot
proteins
pubmed
9427609
uniprot
proteins
pubmed
9618518
uniprot
proteins
sequence_length
93
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14525775, ECO:0000269|PubMed:8752281}.
uniprot
proteins