SDF1_XENLA
ID SDF1_XENLA Reviewed; 94 AA.
AC Q8UUJ9; Q498K3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Stromal cell-derived factor 1 {ECO:0000250|UniProtKB:P48061};
DE Short=xSDF-1 {ECO:0000303|PubMed:11859124};
DE AltName: Full=C-X-C motif chemokine 12 {ECO:0000250|UniProtKB:P48061};
DE Flags: Precursor;
GN Name=cxcl12; Synonyms=sdf1 {ECO:0000312|EMBL:AAH61945.1};
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:CAC82196.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Spleen {ECO:0000312|EMBL:CAC82196.1};
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAH61945.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA).
RC TISSUE=Spleen {ECO:0000312|EMBL:AAH61945.1}, and
RC Tail bud {ECO:0000312|EMBL:AAI00185.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, 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: Chemoattractant (PubMed:11859124). Activates the C-X-C
CC chemokine receptor cxcr4 to induce a rapid and transient rise in the
CC level of intracellular calcium ions, and chemotaxis (PubMed:11859124).
CC Signaling with cxcr4 mediates the directional movement of mesodermal
CC cells during gastrulation (Ref.2). Binds to the allosteric site (site
CC 2) of integrins and activates them in a cxcr4-independent manner (By
CC similarity). {ECO:0000250|UniProtKB:P48061,
CC ECO:0000269|PubMed:11859124, ECO:0000269|PubMed:17239342}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta {ECO:0000269|PubMed:11859124}; Synonyms=xSDF-1
CC {ECO:0000269|PubMed:17239342};
CC IsoId=Q8UUJ9-1; Sequence=Displayed;
CC Name=Alpha; Synonyms=xSDF-1alpha {ECO:0000269|PubMed:17239342};
CC IsoId=Q8UUJ9-2; Sequence=VSP_053125;
CC -!- TISSUE SPECIFICITY: Isoform alpha is expressed throughout the inner
CC deep cells of the blastocoel roof during gastrula stage embryos.
CC Isoform beta is expressed in the developing central nervous system
CC (CNS) of embryos; at stages 21-23, up-regulated in the anterior of the
CC embryo where neural tube segregation occurs. At stages 32-34, expressed
CC in the mid- and hindbrain, otic vesicles and eye, and the dorsal fin,
CC and the embryonic heart at stage 32. At stages 39-40, isoform beta is
CC highly expressed in the proctodeum in the posterior embryo. In the
CC adult, isoform beta is highly expressed in the spleen, kidney, lung,
CC stomach, testis and skeletal muscle. Lower levels are expressed in
CC adult liver and heart. Expression is present at a very low level in
CC adult brain and skin. {ECO:0000269|PubMed:11859124,
CC ECO:0000269|PubMed:17239342}.
CC -!- DEVELOPMENTAL STAGE: Isoform alpha is expressed from the gastrula
CC stage, whereas isoform beta is not expressed until the tailbud stage.
CC {ECO:0000269|PubMed:17239342}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000255}.
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DR EMBL; AJ278857; CAC82196.1; -; mRNA.
DR EMBL; BC061945; AAH61945.1; -; mRNA.
DR EMBL; BC073527; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC100184; AAI00185.1; -; mRNA.
DR RefSeq; NP_001083632.1; NM_001090163.1. [Q8UUJ9-1]
DR AlphaFoldDB; Q8UUJ9; -.
DR SMR; Q8UUJ9; -.
DR DNASU; 399030; -.
DR GeneID; 399030; -.
DR KEGG; xla:399030; -.
DR CTD; 399030; -.
DR Xenbase; XB-GENE-6077780; cxcl12.L.
DR OMA; STPNCAL; -.
DR OrthoDB; 1537838at2759; -.
DR Proteomes; UP000186698; Chromosome 7L.
DR Bgee; 399030; Expressed in spleen and 18 other tissues.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0006952; P:defense response; IEA:InterPro.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0033622; P:integrin activation; ISS:UniProtKB.
DR GO; GO:0007509; P:mesoderm migration involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:UniProtKB.
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 2: Evidence at transcript level;
KW Alternative splicing; Chemotaxis; Cytokine; Developmental protein;
KW Disulfide bond; Gastrulation; Growth factor; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255, ECO:0000312|EMBL:CAC82196.1"
FT CHAIN 22..94
FT /note="Stromal cell-derived factor 1"
FT /evidence="ECO:0000250|UniProtKB:P48061"
FT /id="PRO_5000066132"
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"
FT VAR_SEQ 90..94
FT /note="Missing (in isoform Alpha)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_053125"
SQ SEQUENCE 94 AA; 10701 MW; 8C8325D152F326E7 CRC64;
MDIRTLALLS ILLGTLCLTE GKPVSLVYRC PCRYFESNVP KSNIKHLKIL STSNCSLQIV
ARLKHNGKQI CLDPKTKWIQ EYLEKALNKK AKKT
