PLF4_PIG
ID PLF4_PIG Reviewed; 90 AA.
AC P30034;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Platelet factor 4;
DE Short=PF-4;
DE AltName: Full=C-X-C motif chemokine 4;
GN Name=PF4; Synonyms=CXCL4, SCYB4;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP PROTEIN SEQUENCE, PYROGLUTAMATE FORMATION AT GLN-1, AND GLYCOSYLATION AT
RP THR-8.
RC TISSUE=Platelet;
RX PubMed=7737160; DOI=10.1111/j.1432-1033.1995.0658m.x;
RA Proudfoot A.E.I., Magnenat E., Haley T.M., Maione T.E., Wells T.N.C.;
RT "The complete primary structure of glycosylated porcine platelet factor
RT 4.";
RL Eur. J. Biochem. 228:658-664(1995).
RN [2]
RP PROTEIN SEQUENCE OF 18-86.
RC TISSUE=Platelet;
RX PubMed=1788836; DOI=10.1016/0049-3848(91)90351-v;
RA Shigeta O., Lu W., Holt J.C., Edmunds L.H. Jr., Niewiarowski S.;
RT "Ovine platelet factor 4: purification, amino acid sequence,
RT radioimmunoassay and comparison with platelet factor 4 of other species.";
RL Thromb. Res. 64:509-520(1991).
CC -!- FUNCTION: Released during platelet aggregation. Neutralizes the
CC anticoagulant effect of heparin because it binds more strongly to
CC heparin than to the chondroitin-4-sulfate chains of the carrier
CC molecule. Chemotactic for neutrophils and monocytes. Inhibits
CC endothelial cell proliferation.
CC -!- SUBUNIT: Homotetramer. Interacts with TNFAIP6 (via Link domain).
CC {ECO:0000250|UniProtKB:P02776}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: O-linked glycan consists of Gal-GalNAc disaccharide which is
CC modified with sialic acid residues (microheterogeneity).
CC {ECO:0000269|PubMed:7737160}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
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DR PIR; S69133; S69133.
DR AlphaFoldDB; P30034; -.
DR SMR; P30034; -.
DR STRING; 9823.ENSSSCP00000000258; -.
DR iPTMnet; P30034; -.
DR PaxDb; P30034; -.
DR PeptideAtlas; P30034; -.
DR eggNOG; ENOG502TF57; Eukaryota.
DR HOGENOM; CLU_143902_1_2_1; -.
DR InParanoid; P30034; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P30034; SS.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
DR GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0048248; F:CXCR3 chemokine receptor binding; ISS:UniProtKB.
DR GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0030595; P:leukocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR CDD; cd00273; Chemokine_CXC; 1.
DR InterPro; IPR001089; Chemokine_CXC.
DR InterPro; IPR018048; Chemokine_CXC_CS.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR033899; CXC_Chemokine_domain.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR InterPro; IPR027222; PF4.
DR PANTHER; PTHR10179; PTHR10179; 1.
DR PANTHER; PTHR10179:SF43; PTHR10179:SF43; 1.
DR Pfam; PF00048; IL8; 1.
DR PRINTS; PR00437; SMALLCYTKCXC.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
DR PROSITE; PS00471; SMALL_CYTOKINES_CXC; 1.
PE 1: Evidence at protein level;
KW Chemotaxis; Cytokine; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heparin-binding; Phosphoprotein; Pyrrolidone carboxylic acid;
KW Reference proteome; Secreted.
FT CHAIN 1..90
FT /note="Platelet factor 4"
FT /id="PRO_0000144299"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 76..82
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:7737160"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06765"
FT CARBOHYD 8
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:7737160"
FT DISULFID 25..51
FT /evidence="ECO:0000250"
FT DISULFID 27..67
FT /evidence="ECO:0000250"
FT CONFLICT 43
FT /note="E -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 85..86
FT /note="SQ -> PE (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 90 AA; 9644 MW; 108F15AC828FDE6F CRC64;
QEWSLPGTRV PPPADPEGGD ANLRCVCVKT ISGVSPKHIS SLEVIGAGPH CPSPQLIATL
KKGHKICLDP QNLLYKKIIK KLLKSQLLTA
