ID SDF1_FELCA Reviewed; 93 AA. AC O62657; Q54AJ3; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 06-JUL-2016, entry version 94. DE RecName: Full=Stromal cell-derived factor 1; DE Short=SDF-1; DE AltName: Full=C-X-C motif chemokine 12; DE Flags: Precursor; GN Name=CXCL12; Synonyms=SDF1; OS Felis catus (Cat) (Felis silvestris catus). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; OC Felinae; Felis. OX NCBI_TaxID=9685; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA). RC TISSUE=Thymus; RX PubMed=9777331; DOI=10.1046/j.1365-2370.1998.00107.x; RA Nishimura Y., Miyazawa T., Ikeda Y., Izumiya Y., Nakamura K., RA Cai J.S., Sato E., Kohmoto M., Mikami T.; RT "Molecular cloning and sequencing of feline stromal cell-derived RT factor-1 alpha and beta."; RL Eur. J. Immunogenet. 25:303-305(1998). CC -!- FUNCTION: Chemoattractant active on T-lymphocytes, monocytes, but CC not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to CC induce a rapid and transient rise in the level of intracellular CC calcium ions and chemotaxis. Also binds to atypical chemokine CC receptor ACKR3, which activates the beta-arrestin pathway and acts CC as a scavenger receptor for SDF-1. Acts as a positive regulator of CC monocyte migration and a negative regulator of monocyte adhesion CC via the LYN kinase. Stimulates migration of monocytes and T- CC lymphocytes through its receptors, CXCR4 and ACKR3, and decreases CC monocyte adherence to surfaces coated with ICAM-1, a ligand for CC beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 CC integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through CC LYN kinase. Plays a protective role after myocardial infarction. CC Has several critical functions during embryonic development; CC required for B-cell lymphopoiesis, myelopoiesis in bone marrow and CC heart ventricular septum formation (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Monomer or homodimer; in equilibrium. Dimer formation is CC induced by non acidic pH and the presence of multivalent anions, CC and by binding to CXCR4 or heparin. Monomeric form is required for CC full chemotactic activity and resistance to ischemia/reperfusion CC injury, whereas the dimeric form acts as a partial agonist of CC CXCR4, stimulating Ca2+ mobilization but with no chemotactic CC activity and instead acts as a selective antagonist that blocks CC chemotaxis induced by the monomeric form. Interacts with the N- CC terminus of ACKR3 (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Beta; Synonyms=SDF-1b; CC IsoId=O62657-1; Sequence=Displayed; CC Name=Alpha; Synonyms=SDF-1a; CC IsoId=O62657-2; Sequence=VSP_001055; CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) CC family. {ECO:0000305}. 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; AB011965; BAA28601.1; -; mRNA. DR EMBL; AB011966; BAA28602.1; -; mRNA. DR RefSeq; NP_001009847.1; NM_001009847.1. [O62657-1] DR ProteinModelPortal; O62657; -. DR SMR; O62657; 22-89. DR STRING; 9685.ENSFCAP00000007102; -. DR Ensembl; ENSFCAT00000007670; ENSFCAP00000007102; ENSFCAG00000007670. [O62657-2] DR GeneID; 493806; -. DR KEGG; fca:493806; -. DR CTD; 6387; -. DR eggNOG; ENOG410J1S5; Eukaryota. DR eggNOG; ENOG4112BS6; LUCA. DR GeneTree; ENSGT00390000014056; -. DR HOVERGEN; HBG107437; -. DR InParanoid; O62657; -. DR KO; K10031; -. DR OMA; STPNCAL; -. DR OrthoDB; EOG7C5MBS; -. DR Proteomes; UP000011712; Chromosome D2. DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; IEA:Ensembl. DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW. DR GO; GO:0042056; F:chemoattractant activity; IBA:GO_Central. DR GO; GO:0008009; F:chemokine activity; IBA:GO_Central. DR GO; GO:0042379; F:chemokine receptor binding; ISS:UniProtKB. DR GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central. DR GO; GO:0007411; P:axon guidance; IBA:GO_Central. DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0006955; P:immune response; IEA:InterPro. DR GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central. DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl. DR GO; GO:2000107; P:negative regulation of leukocyte apoptotic process; IEA:Ensembl. DR GO; GO:1903237; P:negative regulation of leukocyte tethering or rolling; IEA:Ensembl. DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl. DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central. DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; IEA:Ensembl. DR GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl. DR InterPro; IPR001811; Chemokine_IL8-like_dom. DR Pfam; PF00048; IL8; 1. DR SMART; SM00199; SCY; 1. DR SUPFAM; SSF54117; SSF54117; 1. PE 3: Inferred from homology; KW Alternative splicing; Chemotaxis; Complete proteome; Cytokine; KW Disulfide bond; Growth factor; Reference proteome; Secreted; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 93 Stromal cell-derived factor 1. FT /FTId=PRO_0000005108. FT REGION 29 33 Receptor and heparin binding. FT {ECO:0000250}. FT REGION 39 41 Receptor binding. {ECO:0000250}. FT REGION 41 51 Heparin binding. {ECO:0000250}. FT REGION 48 50 Receptor binding. {ECO:0000250}. FT REGION 60 70 Receptor binding. {ECO:0000250}. FT MOTIF 22 23 Receptor activation motif. {ECO:0000250}. FT BINDING 62 62 Heparin. {ECO:0000250}. FT BINDING 69 69 Heparin. {ECO:0000250}. FT BINDING 85 85 Heparin. {ECO:0000250}. FT SITE 46 46 Important for dimer formation. FT {ECO:0000250}. FT DISULFID 30 55 {ECO:0000250}. FT DISULFID 32 71 {ECO:0000250}. FT VAR_SEQ 90 93 Missing (in isoform Alpha). FT {ECO:0000303|PubMed:9777331}. FT /FTId=VSP_001055. SQ SEQUENCE 93 AA; 10581 MW; 44FC763711E9BE37 CRC64; MDAKVVAVLA LVLAALCLSD GKPVSLSYRC PCRFFESHVA RANVKHLKIL NTPNCALQIV ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR FKM //