ID   SDF1_MOUSE              Reviewed;          93 AA.
AC   P40224; Q4FJL5; Q543V6;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 190.
DE   RecName: Full=Stromal cell-derived factor 1;
DE            Short=SDF-1;
DE   AltName: Full=12-O-tetradecanoylphorbol 13-acetate repressed protein 1;
DE            Short=TPAR1;
DE   AltName: Full=C-X-C motif chemokine 12;
DE   AltName: Full=Pre-B cell growth-stimulating factor;
DE            Short=PBSF;
DE   AltName: Full=Thymic lymphoma cell-stimulating factor;
DE            Short=TLSF;
DE   Flags: Precursor;
GN   Name=Cxcl12; Synonyms=Sdf1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RX   PubMed=8342023; DOI=10.1126/science.8342023;
RA   Tashiro K., Tada H., Heilker R., Shirozu M., Nakano T., Honjo T.;
RT   "Signal sequence trap: a cloning strategy for secreted proteins and type I
RT   membrane proteins.";
RL   Science 261:600-603(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), ALTERNATIVE SPLICING, TISSUE
RP   SPECIFICITY, AND INDUCTION.
RX   PubMed=7982471; DOI=10.1006/excr.1994.1344;
RA   Jiang W., Zhou P., Kahn S.M., Tomita N., Johnson M.D., Weinstein I.B.;
RT   "Molecular cloning of TPAR1, a gene whose expression is repressed by the
RT   tumor promoter 12-O-tetradecanoylphorbol 13-acetate (TPA).";
RL   Exp. Cell Res. 215:284-293(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND FUNCTION.
RX   PubMed=8134392; DOI=10.1073/pnas.91.6.2305;
RA   Nagasawa T., Kikutani H., Kishimoto T.;
RT   "Molecular cloning and structure of a pre-B-cell growth-stimulating
RT   factor.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:2305-2309(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND BETA).
RC   STRAIN=AKR/J;
RA   Nomura M., Nakata Y., Uzawa A., Nose M., Akashi M., Suzuki G.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS ALPHA AND BETA).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Kidney, and Spleen;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
RA   Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA   Wiemann S., Schick M., Korn B.;
RT   "Cloning of mouse full open reading frames in Gateway(R) system entry
RT   vector (pDONR201).";
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=8757135; DOI=10.1038/382635a0;
RA   Nagasawa T., Hirota S., Tachibana K., Takakura N., Nishikawa S.,
RA   Kitamura Y., Yoshida N., Kikutani H., Kishimoto T.;
RT   "Defects of B-cell lymphopoiesis and bone-marrow myelopoiesis in mice
RT   lacking the CXC chemokine PBSF/SDF-1.";
RL   Nature 382:635-638(1996).
CC   -!- FUNCTION: Chemoattractant active on T-lymphocytes and monocytes but not
CC       neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a
CC       rapid and transient rise in the level of intracellular calcium ions and
CC       chemotaxis. Also binds to atypical chemokine receptor ACKR3, which
CC       activates the beta-arrestin pathway and acts as a scavenger receptor
CC       for SDF-1. Binds to the allosteric site (site 2) of integrins and
CC       activates integrins ITGAV:ITGB3, ITGA4:ITGB1 and ITGA5:ITGB1 in a
CC       CXCR4-independent manner (By similarity). Acts as a positive regulator
CC       of monocyte migration and a negative regulator of monocyte adhesion via
CC       the LYN kinase. Stimulates migration of monocytes and T-lymphocytes
CC       through its receptors, CXCR4 and ACKR3, and decreases monocyte
CC       adherence to surfaces coated with ICAM-1, a ligand for beta-2
CC       integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1
CC       mediated adhesion of monocytes to ICAM-1 through LYN kinase. Plays a
CC       protective role after myocardial infarction. Induces down-regulation
CC       and internalization of ACKR3 expressed in various cells (By
CC       similarity). Has several critical functions during embryonic
CC       development; required for B-cell lymphopoiesis, myelopoiesis in bone
CC       marrow and heart ventricular septum formation. Stimulates the
CC       proliferation of bone marrow-derived B-cell progenitors in the presence
CC       of IL7 as well as growth of stromal cell-dependent pre-B-cells
CC       (PubMed:8134392). {ECO:0000250|UniProtKB:P48061,
CC       ECO:0000269|PubMed:8134392, ECO:0000269|PubMed:8757135}.
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. Monomeric form is required for full
CC       chemotactic activity and resistance to ischemia/reperfusion injury,
CC       whereas the dimeric form acts as a partial agonist of CXCR4,
CC       stimulating Ca2+ mobilization but with no chemotactic activity and
CC       instead acts as a selective antagonist that blocks chemotaxis induced
CC       by the monomeric form. Interacts with the N-terminus of ACKR3.
CC       Interacts with integrin subunit ITGB3 (via the allosteric site (site
CC       2)). Interacts with TNFAIP6 (via Link domain).
CC       {ECO:0000250|UniProtKB:P48061}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Beta;
CC         IsoId=P40224-2; Sequence=Displayed;
CC       Name=Alpha;
CC         IsoId=P40224-1; Sequence=VSP_037607;
CC   -!- TISSUE SPECIFICITY: Highest expression levels detected in kidney,
CC       liver, spleen and muscle. Isoform Alpha is expressed ubiquitously but
CC       at varying levels, while isoform Beta displays tissue-specific
CC       expression, with expression detected in kidney, liver, heart, spleen
CC       and muscle but not in lung, colon, brain, skin and stomach.
CC       {ECO:0000269|PubMed:7982471}.
CC   -!- INDUCTION: Down-regulated by 12-O-tetradecanoylphorbol 13-acetate
CC       (TPA), with 5-fold decrease in expression levels at 1 hour after TPA
CC       treatment, 12-fold decrease at 4 hours, undetectable levels after 8
CC       hours and low-level expression returning at 24 hours after treatment.
CC       Down-regulated by serum stimulation, with expression levels reaching
CC       their minimum at 4 hours after stimulation and returning back to normal
CC       levels at 16 hours after stimulation. {ECO:0000269|PubMed:7982471}.
CC   -!- DISRUPTION PHENOTYPE: Half of the embryos die by 18.5 dpc, and neonates
CC       die within an hour. Mutants display defective B-lymphopoiesis,
CC       defective myelopoiesis in the bone marrow but not in the liver, and
CC       defective formation of the heart ventricular septum.
CC       {ECO:0000269|PubMed:8757135}.
CC   -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC       {ECO:0000305}.
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DR   EMBL; L12029; AAA40100.1; -; mRNA.
DR   EMBL; L12030; AAA40101.1; -; mRNA.
DR   EMBL; S74318; AAB32650.1; -; mRNA.
DR   EMBL; D21072; BAA04648.1; -; mRNA.
DR   EMBL; D43804; BAA07862.1; -; mRNA.
DR   EMBL; D43805; BAA07863.1; -; mRNA.
DR   EMBL; AK045092; BAC32216.1; -; mRNA.
DR   EMBL; AK075596; BAC35845.1; -; mRNA.
DR   EMBL; AK157553; BAE34120.1; -; mRNA.
DR   EMBL; CT010389; CAJ18596.1; -; mRNA.
DR   EMBL; CH466523; EDK99572.1; -; Genomic_DNA.
DR   EMBL; BC006640; AAH06640.1; -; mRNA.
DR   CCDS; CCDS39605.1; -. [P40224-2]
DR   CCDS; CCDS39606.1; -. [P40224-1]
DR   PIR; A53497; A53497.
DR   PIR; I81182; I81182.
DR   RefSeq; NP_038683.1; NM_013655.4. [P40224-2]
DR   RefSeq; NP_068350.1; NM_021704.3. [P40224-1]
DR   AlphaFoldDB; P40224; -.
DR   BMRB; P40224; -.
DR   SMR; P40224; -.
DR   DIP; DIP-61153N; -.
DR   IntAct; P40224; 3.
DR   STRING; 10090.ENSMUSP00000072800; -.
DR   iPTMnet; P40224; -.
DR   PhosphoSitePlus; P40224; -.
DR   MaxQB; P40224; -.
DR   PaxDb; 10090-ENSMUSP00000072800; -.
DR   ProteomicsDB; 256759; -. [P40224-2]
DR   ProteomicsDB; 256760; -. [P40224-1]
DR   Pumba; P40224; -.
DR   ABCD; P40224; 2 sequenced antibodies.
DR   Antibodypedia; 4314; 1004 antibodies from 44 providers.
DR   DNASU; 20315; -.
DR   Ensembl; ENSMUST00000112866.8; ENSMUSP00000108487.2; ENSMUSG00000061353.12. [P40224-1]
DR   Ensembl; ENSMUST00000112871.8; ENSMUSP00000108492.2; ENSMUSG00000061353.12. [P40224-2]
DR   GeneID; 20315; -.
DR   KEGG; mmu:20315; -.
DR   UCSC; uc009dks.2; mouse. [P40224-2]
DR   AGR; MGI:103556; -.
DR   CTD; 6387; -.
DR   MGI; MGI:103556; Cxcl12.
DR   VEuPathDB; HostDB:ENSMUSG00000061353; -.
DR   eggNOG; ENOG502S54U; Eukaryota.
DR   GeneTree; ENSGT00390000014056; -.
DR   HOGENOM; CLU_154284_2_0_1; -.
DR   InParanoid; P40224; -.
DR   OMA; LSTPNCA; -.
DR   OrthoDB; 5350863at2759; -.
DR   PhylomeDB; P40224; -.
DR   Reactome; R-MMU-376176; Signaling by ROBO receptors.
DR   Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR   Reactome; R-MMU-418594; G alpha (i) signalling events.
DR   BioGRID-ORCS; 20315; 0 hits in 82 CRISPR screens.
DR   ChiTaRS; Cxcl12; mouse.
DR   PRO; PR:P40224; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P40224; Protein.
DR   Bgee; ENSMUSG00000061353; Expressed in stroma of bone marrow and 329 other cell types or tissues.
DR   ExpressionAtlas; P40224; baseline and differential.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0008009; F:chemokine activity; IDA:MGI.
DR   GO; GO:0042379; F:chemokine receptor binding; ISS:UniProtKB.
DR   GO; GO:0045236; F:CXCR chemokine receptor binding; ISO:MGI.
DR   GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0008344; P:adult locomotory behavior; ISO:MGI.
DR   GO; GO:0031100; P:animal organ regeneration; ISO:MGI.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR   GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR   GO; GO:0043534; P:blood vessel endothelial cell migration; IMP:MGI.
DR   GO; GO:0007420; P:brain development; IDA:MGI.
DR   GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IMP:MGI.
DR   GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
DR   GO; GO:0098609; P:cell-cell adhesion; IDA:MGI.
DR   GO; GO:1990869; P:cellular response to chemokine; ISO:MGI.
DR   GO; GO:0038146; P:chemokine (C-X-C motif) ligand 12 signaling pathway; ISO:MGI.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0038160; P:CXCL12-activated CXCR4 signaling pathway; ISO:MGI.
DR   GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISO:MGI.
DR   GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISO:MGI.
DR   GO; GO:0071542; P:dopaminergic neuron differentiation; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0007281; P:germ cell development; IDA:MGI.
DR   GO; GO:0008354; P:germ cell migration; IDA:MGI.
DR   GO; GO:0050930; P:induction of positive chemotaxis; IDA:MGI.
DR   GO; GO:0033622; P:integrin activation; ISS:UniProtKB.
DR   GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR   GO; GO:0008045; P:motor neuron axon guidance; IMP:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IGI:MGI.
DR   GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; ISO:MGI.
DR   GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI.
DR   GO; GO:1903237; P:negative regulation of leukocyte tethering or rolling; ISO:MGI.
DR   GO; GO:0001764; P:neuron migration; ISO:MGI.
DR   GO; GO:0048842; P:positive regulation of axon extension involved in axon guidance; ISO:MGI.
DR   GO; GO:0090280; P:positive regulation of calcium ion import; IDA:MGI.
DR   GO; GO:0045785; P:positive regulation of cell adhesion; ISO:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0050921; P:positive regulation of chemotaxis; IGI:MGI.
DR   GO; GO:0033603; P:positive regulation of dopamine secretion; ISO:MGI.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IGI:MGI.
DR   GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISO:MGI.
DR   GO; GO:1901741; P:positive regulation of myoblast fusion; IMP:MGI.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IGI:MGI.
DR   GO; GO:2000406; P:positive regulation of T cell migration; ISO:MGI.
DR   GO; GO:1904018; P:positive regulation of vasculature development; ISO:MGI.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR   GO; GO:0030334; P:regulation of cell migration; IDA:MGI.
DR   GO; GO:0010818; P:T cell chemotaxis; ISO:MGI.
DR   GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR   GO; GO:0022029; P:telencephalon cell migration; ISO:MGI.
DR   CDD; cd00273; Chemokine_CXC; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   InterPro; IPR039809; Chemokine_b/g/d.
DR   InterPro; IPR001811; Chemokine_IL8-like_dom.
DR   InterPro; IPR033899; CXC_Chemokine_domain.
DR   InterPro; IPR036048; Interleukin_8-like_sf.
DR   PANTHER; PTHR12015; SMALL INDUCIBLE CYTOKINE A; 1.
DR   PANTHER; PTHR12015:SF206; STROMAL CELL-DERIVED FACTOR 1; 1.
DR   Pfam; PF00048; IL8; 1.
DR   PRINTS; PR00436; INTERLEUKIN8.
DR   SMART; SM00199; SCY; 1.
DR   SUPFAM; SSF54117; Interleukin 8-like chemokines; 1.
DR   Genevisible; P40224; MM.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chemotaxis; Cytokine; Disulfide bond; Growth factor;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..93
FT                   /note="Stromal cell-derived factor 1"
FT                   /id="PRO_0000005112"
FT   REGION          29..33
FT                   /note="Receptor and heparin binding"
FT                   /evidence="ECO:0000250"
FT   REGION          39..41
FT                   /note="Receptor binding"
FT                   /evidence="ECO:0000250"
FT   REGION          48..50
FT                   /note="Receptor binding"
FT                   /evidence="ECO:0000250"
FT   REGION          60..70
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"
FT   DISULFID        32..71
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         90..93
FT                   /note="Missing (in isoform Alpha)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7982471,
FT                   ECO:0000303|PubMed:8134392, ECO:0000303|PubMed:8342023,
FT                   ECO:0000303|Ref.4"
FT                   /id="VSP_037607"
SQ   SEQUENCE   93 AA;  10561 MW;  625367D344B8AD69 CRC64;
     MDAKVVAVLA LVLAALCISD GKPVSLSYRC PCRFFESHIA RANVKHLKIL NTPNCALQIV
     ARLKNNNRQV CIDPKLKWIQ EYLEKALNKR LKM
//