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   02-NOV-2016, entry version 97.
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}.
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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   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; EOG091G14JB; -.
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:0006954; P:inflammatory response; IEA:InterPro.
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
//