PLF4_BOVIN
ID PLF4_BOVIN Reviewed; 88 AA.
AC P02777;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 133.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=3767377; DOI=10.1016/0003-9861(86)90723-x;
RA Ciaglowski R.E., Snow J., Walz D.A.;
RT "Isolation and amino acid sequence of bovine platelet factor 4.";
RL Arch. Biochem. Biophys. 250:249-256(1986).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=2065087; DOI=10.1016/0167-4838(91)99011-g;
RA Talpas C.J., Walz D.A., Lee L.;
RT "1H-NMR studies of bovine platelet factor 4: histidine assignments and
RT interactions with heparin.";
RL Biochim. Biophys. Acta 1078:208-218(1991).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), AND GLYCOSYLATION.
RX PubMed=2914894; DOI=10.1016/s0021-9258(18)94146-3;
RA St Charles R., Walz D.A., Edwards B.F.P.;
RT "The three-dimensional structure of bovine platelet factor 4 at 3.0-A
RT resolution.";
RL J. Biol. Chem. 264:2092-2099(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX PubMed=1409574; DOI=10.1002/prot.340140213;
RA Stuckey J.A., St Charles R., Edwards B.F.P.;
RT "A model of the platelet factor 4 complex with heparin.";
RL Proteins 14:277-287(1992).
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:2914894}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR PIR; A03242; PFBO4.
DR PDB; 1PLF; X-ray; 2.20 A; A/B/C/D=14-83.
DR PDBsum; 1PLF; -.
DR AlphaFoldDB; P02777; -.
DR SMR; P02777; -.
DR STRING; 9913.ENSBTAP00000015874; -.
DR iPTMnet; P02777; -.
DR PRIDE; P02777; -.
DR eggNOG; ENOG502TF57; Eukaryota.
DR InParanoid; P02777; -.
DR EvolutionaryTrace; P02777; -.
DR Proteomes; UP000009136; Unplaced.
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 3D-structure; Chemotaxis; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Heparin-binding; Phosphoprotein;
KW Proteoglycan; Reference proteome; Secreted.
FT CHAIN 1..88
FT /note="Platelet factor 4"
FT /id="PRO_0000144298"
FT BINDING 76..82
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT /evidence="ECO:0000250"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06765"
FT CARBOHYD 7
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:2914894"
FT DISULFID 25..51
FT DISULFID 27..67
FT HELIX 36..38
FT /evidence="ECO:0007829|PDB:1PLF"
FT STRAND 39..45
FT /evidence="ECO:0007829|PDB:1PLF"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:1PLF"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:1PLF"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1PLF"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1PLF"
SQ SEQUENCE 88 AA; 9523 MW; 9288E16455250FFB CRC64;
ESSFPATFVP LPADSEGGED EDLQCVCLKT TSGINPRHIS SLEVIGAGTH CPSPQLLATK
KTGRKICLDQ QRPLYKKILK KLLDGDES
