SDF1_XENTR
ID SDF1_XENTR Reviewed; 93 AA.
AC Q5EBF6;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Stromal cell-derived factor 1 {ECO:0000312|EMBL:AAH89703.1};
DE Short=SDF-1 {ECO:0000250|UniProtKB:Q8UUJ9};
DE AltName: Full=C-X-C motif chemokine 12 {ECO:0000312|EMBL:AAH89703.1};
DE Flags: Precursor;
GN Name=cxcl12 {ECO:0000312|EMBL:AAH89703.1};
GN Synonyms=sdf1 {ECO:0000250|UniProtKB:Q8UUJ9};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH89703.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=F6 {ECO:0000312|EMBL:AAH89703.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Chemoattractant. Activates the C-X-C chemokine receptor cxcr4
CC to induce a rapid and transient rise in the level of intracellular
CC calcium ions, and chemotaxis. Signaling with cxcr4 mediates the
CC directional movement of mesodermal cells during gastrulation. Binds to
CC the allosteric site (site 2) of integrins and activates them in a
CC cxcr4-independent manner. {ECO:0000250|UniProtKB:P48061,
CC ECO:0000250|UniProtKB:Q8UUJ9}.
CC -!- SUBUNIT: Monomer or homodimer; in equilibrium. Dimer formation is
CC induced by non acidic pH and the presence of multivalent anions, and by
CC binding to cxcr4 or heparin (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000255}.
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DR EMBL; BC089703; AAH89703.1; -; mRNA.
DR RefSeq; NP_001015764.1; NM_001015764.1.
DR AlphaFoldDB; Q5EBF6; -.
DR SMR; Q5EBF6; -.
DR PaxDb; Q5EBF6; -.
DR DNASU; 548481; -.
DR Ensembl; ENSXETT00000068483; ENSXETP00000064951; ENSXETG00000003570.
DR GeneID; 548481; -.
DR KEGG; xtr:548481; -.
DR CTD; 6387; -.
DR Xenbase; XB-GENE-919853; cxcl12.
DR eggNOG; ENOG502S54U; Eukaryota.
DR InParanoid; Q5EBF6; -.
DR OrthoDB; 1444515at2759; -.
DR Reactome; R-XTR-376176; Signaling by ROBO receptors.
DR Reactome; R-XTR-380108; Chemokine receptors bind chemokines.
DR Reactome; R-XTR-418594; G alpha (i) signalling events.
DR Proteomes; UP000008143; Chromosome 7.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000003570; Expressed in liver and 12 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0008009; F:chemokine activity; ISS:UniProtKB.
DR GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; ISS:UniProtKB.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
DR GO; GO:0033622; P:integrin activation; ISS:UniProtKB.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central.
DR CDD; cd00273; Chemokine_CXC; 1.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR033899; CXC_Chemokine_domain.
DR InterPro; IPR039813; CXCL12.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR18837; PTHR18837; 1.
DR Pfam; PF00048; IL8; 1.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
PE 3: Inferred from homology;
KW Chemotaxis; Cytokine; Developmental protein; Disulfide bond; Gastrulation;
KW Growth factor; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..93
FT /note="Stromal cell-derived factor 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000378621"
FT REGION 29..33
FT /note="Receptor and heparin binding"
FT /evidence="ECO:0000250"
FT REGION 48..50
FT /note="Receptor binding"
FT /evidence="ECO:0000250"
FT REGION 60..64
FT /note="Receptor binding"
FT /evidence="ECO:0000250"
FT MOTIF 22..23
FT /note="Receptor activation motif"
FT /evidence="ECO:0000250"
FT BINDING 41..51
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 69
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT SITE 45
FT /note="Important for integrin interaction and activation"
FT /evidence="ECO:0000250|UniProtKB:P48061"
FT SITE 46
FT /note="Important for dimer formation"
FT /evidence="ECO:0000250"
FT SITE 48
FT /note="Important for integrin interaction and activation"
FT /evidence="ECO:0000250|UniProtKB:P48061"
FT SITE 64
FT /note="Important for integrin interaction and activation"
FT /evidence="ECO:0000250|UniProtKB:P48061"
FT DISULFID 30..55
FT /evidence="ECO:0000250|UniProtKB:P48061"
FT DISULFID 32..71
FT /evidence="ECO:0000250|UniProtKB:P48061"
SQ SEQUENCE 93 AA; 10607 MW; 8BEA67CF754031D5 CRC64;
MDIRTLALFS ILLGSLCLSE GKPVSLVYRC PCRYFESNVP KSNIKHLKIL STSNCSLQIV
ARLKHNGKQI CLDPKTKWIQ EYLEKALNKK VKT
