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   07-NOV-2018, entry version 109.
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 and monocytes
CC       but not neutrophils. 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. 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. Binds to the allosteric site (site 2) of
CC       integrins and activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and
CC       ITGA5:ITGB1 in a CXCR4-independent manner. Stimulates migration of
CC       monocytes and T-lymphocytes through its receptors, CXCR4 and
CC       ACKR3, and decreases monocyte adherence to surfaces coated with
CC       ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis
CC       inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to
CC       ICAM-1 through LYN kinase. Plays a protective role after
CC       myocardial infarction. Has several critical functions during
CC       embryonic development; required for B-cell lymphopoiesis,
CC       myelopoiesis in bone marrow and heart ventricular septum
CC       formation. Stimulates the proliferation of bone marrow-derived B-
CC       cell progenitors in the presence of IL7 as well as growth of
CC       stromal cell-dependent pre-B-cells. {ECO:0000250|UniProtKB:P40224,
CC       ECO:0000250|UniProtKB:P48061}.
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. Interacts with integrin subunit ITGB3 (via the
CC       allosteric site (site 2)). {ECO:0000250|UniProtKB:P48061}.
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   SMR; O62657; -.
DR   STRING; 9685.ENSFCAP00000007102; -.
DR   Ensembl; ENSFCAT00000058624; ENSFCAP00000044453; ENSFCAG00000036777. [O62657-1]
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   Bgee; ENSFCAG00000007670; Expressed in 3 organ(s), highest expression level in liver.
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; 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:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006952; P:defense response; IEA:InterPro.
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: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   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         45     45       Important for integrin interaction and
FT                                activation.
FT                                {ECO:0000250|UniProtKB:P48061}.
FT   SITE         46     46       Important for dimer formation.
FT                                {ECO:0000250}.
FT   SITE         48     48       Important for integrin interaction and
FT                                activation.
FT                                {ECO:0000250|UniProtKB:P48061}.
FT   SITE         64     64       Important for integrin interaction and
FT                                activation.
FT                                {ECO:0000250|UniProtKB:P48061}.
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
//