PLF4_RAT
ID PLF4_RAT Reviewed; 105 AA.
AC P06765;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Platelet factor 4;
DE Short=PF-4;
DE AltName: Full=C-X-C motif chemokine 4;
DE Flags: Precursor;
GN Name=Pf4; Synonyms=Cxcl4, Scyb4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3821732; DOI=10.1128/mcb.7.2.898-904.1987;
RA Doi T., Greenberg S.M., Rosenberg R.D.;
RT "Structure of the rat platelet factor 4 gene: a marker for megakaryocyte
RT differentiation.";
RL Mol. Cell. Biol. 7:898-904(1987).
RN [2]
RP GLYCOSYLATION AT THR-31.
RX PubMed=8033893; DOI=10.1111/j.1432-1033.1994.tb18984.x;
RA Ravanat C., Gachet C., Herbert J.-M., Schuhler S., Guillemot J.-C.,
RA Uzabiaga F., Picard C., Ferrara P., Freund M., Cazenave J.-P.;
RT "Rat platelets contain glycosylated and non-glycosylated forms of platelet
RT factor 4. Identification and characterization by mass spectrometry.";
RL Eur. J. Biochem. 223:203-210(1994).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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:8033893}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
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DR EMBL; M15254; AAA41832.1; -; Genomic_DNA.
DR PIR; A26774; A26774.
DR RefSeq; NP_001007730.1; NM_001007729.1.
DR AlphaFoldDB; P06765; -.
DR SMR; P06765; -.
DR BioGRID; 262303; 1.
DR IntAct; P06765; 1.
DR STRING; 10116.ENSRNOP00000032276; -.
DR GlyGen; P06765; 1 site.
DR iPTMnet; P06765; -.
DR PhosphoSitePlus; P06765; -.
DR PaxDb; P06765; -.
DR PRIDE; P06765; -.
DR Ensembl; ENSRNOT00000033406; ENSRNOP00000032276; ENSRNOG00000028015.
DR GeneID; 360918; -.
DR KEGG; rno:360918; -.
DR UCSC; RGD:3305; rat.
DR CTD; 5196; -.
DR RGD; 3305; Pf4.
DR eggNOG; ENOG502TF57; Eukaryota.
DR GeneTree; ENSGT00940000163368; -.
DR HOGENOM; CLU_143902_1_2_1; -.
DR InParanoid; P06765; -.
DR OMA; CAVPQLI; -.
DR OrthoDB; 1617719at2759; -.
DR PhylomeDB; P06765; -.
DR TreeFam; TF333433; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-380108; Chemokine receptors bind chemokines.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:P06765; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000028015; Expressed in spleen and 18 other tissues.
DR Genevisible; P06765; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031091; C:platelet alpha granule; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
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; ISO:RGD.
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:0042832; P:defense response to protozoan; ISO:RGD.
DR GO; GO:0006955; P:immune response; IDA:RGD.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0051873; P:killing by host of symbiont cells; ISO:RGD.
DR GO; GO:0030595; P:leukocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; ISO:RGD.
DR GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; ISO:RGD.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0030168; P:platelet activation; ISS:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:RGD.
DR GO; GO:0045651; P:positive regulation of macrophage differentiation; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IPI:RGD.
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; Disulfide bond; Glycoprotein; Heparin-binding;
KW Phosphoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT CHAIN 30..105
FT /note="Platelet factor 4"
FT /id="PRO_0000005070"
FT BINDING 96..102
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 31
FT /note="O-linked (GalNAc...) threonine; partial"
FT /evidence="ECO:0000269|PubMed:8033893"
FT DISULFID 44..71
FT /evidence="ECO:0000250"
FT DISULFID 46..87
FT /evidence="ECO:0000250"
SQ SEQUENCE 105 AA; 11287 MW; D9CCAD2B6A284496 CRC64;
MSAAAVFRGL RPSPELLLLG LLLLPAVVAV TRASPEESDG DLSCVCVKTS SSRIHLKRIT
SLEVIKAGPH CAVPQLIATL KNGSKICLDR QVPLYKKIIK KLLES
