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Platelet factor 4 (PF-4) (C-X-C motif chemokine 4) (Iroplact) (Oncostatin-A) [Cleaved into: Platelet factor 4, short form (Endothelial cell growth inhibitor)]

 PLF4_HUMAN              Reviewed;         101 AA.
P02776; Q53X61; Q9UC64; Q9UC65;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 2.
27-SEP-2017, entry version 176.
RecName: Full=Platelet factor 4;
Short=PF-4;
AltName: Full=C-X-C motif chemokine 4;
AltName: Full=Iroplact;
AltName: Full=Oncostatin-A;
Contains:
RecName: Full=Platelet factor 4, short form;
AltName: Full=Endothelial cell growth inhibitor {ECO:0000303|PubMed:7644496};
Flags: Precursor;
Name=PF4; Synonyms=CXCL4, SCYB4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3098319;
Poncz M., Surrey S., Larocco P., Weiss M.J., Rappaport E.F.,
Conway T.M., Schwartz E.;
"Cloning and characterization of platelet factor 4 cDNA derived from a
human erythroleukemic cell line.";
Blood 69:219-223(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1695112;
Eisman R., Surrey S., Ramachandran B., Schwartz E., Poncz M.;
"Structural and functional comparison of the genes for human platelet
factor 4 and PF4alt.";
Blood 76:336-344(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11468158; DOI=10.1182/blood.V98.3.610;
Zhang C., Thornton M.A., Kowalska M.A., Sachis B.S., Feldman M.,
Poncz M., McKenzie S.E., Reilly M.P.;
"Localization of distal regulatory domains in the megakaryocyte-
specific platelet basic protein/platelet factor 4 gene locus.";
Blood 98:610-617(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 32-101.
PubMed=893407;
Hermodson M., Schmer G., Kurachi K.;
"Isolation, crystallization, and primary amino acid sequence of human
platelet factor 4.";
J. Biol. Chem. 252:6276-6279(1977).
[8]
PROTEIN SEQUENCE OF 32-101.
PubMed=267922; DOI=10.1073/pnas.74.6.2256;
Deuel T.F., Keim P.S., Farmer M., Heinrikson R.L.;
"Amino acid sequence of human platelet factor 4.";
Proc. Natl. Acad. Sci. U.S.A. 74:2256-2258(1977).
[9]
PROTEIN SEQUENCE OF 32-101.
PubMed=601757; DOI=10.1016/0049-3848(77)90117-7;
Walz D.A., Wu V.Y., de Lamo R., Dene H., McCoy L.E.;
"Primary structure of human platelet factor 4.";
Thromb. Res. 11:893-898(1977).
[10]
PROTEIN SEQUENCE OF 32-101.
PubMed=6445090;
Morgan F.J., Begg G.S., Chesterman C.N.;
"Complete covalent structure of human platelet factor 4.";
Thromb. Haemost. 42:1652-1660(1980).
[11]
PROTEIN SEQUENCE OF 32-101, IDENTIFICATION OF PF4 SHORT FORM,
FUNCTION, MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
TISSUE=Leukocyte;
PubMed=7644496; DOI=10.1073/pnas.92.17.7799;
Gupta S.K., Hassel T., Singh J.P.;
"A potent inhibitor of endothelial cell proliferation is generated by
proteolytic cleavage of the chemokine platelet factor 4.";
Proc. Natl. Acad. Sci. U.S.A. 92:7799-7803(1995).
[12]
HEPARIN-BINDING REGION.
PubMed=23536183; DOI=10.1074/jbc.M113.455329;
Kuo J.H., Chen Y.P., Liu J.S., Dubrac A., Quemener C., Prats H.,
Bikfalvi A., Wu W.G., Sue S.C.;
"Alternative C-terminal helix orientation alters chemokine function:
Structure of the Anti-angiogenic Chemokine, CXCL4L1.";
J. Biol. Chem. 288:13522-13533(2013).
[13]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), SUBUNIT, AND DISULFIDE BONDS.
PubMed=8031770; DOI=10.1021/bi00193a025;
Zhang X., Chen L., Bancroft D.P., Lai C.K., Maione T.E.;
"Crystal structure of recombinant human platelet factor 4.";
Biochemistry 33:8361-8366(1994).
[14]
STRUCTURE BY NMR OF 43-101, SUBUNIT, AND DISULFIDE BONDS.
PubMed=7547867; DOI=10.1021/bi00036a012;
Mayo K.H., Roongta V., Ilyina E., Milius R., Barker S., Quinlan C.,
La Rosa G., Daly T.J.;
"NMR solution structure of the 32-kDa platelet factor 4 ELR-motif N-
terminal chimera: a symmetric tetramer.";
Biochemistry 34:11399-11409(1995).
-!- FUNCTION: Released during platelet aggregation. Neutralizes the
anticoagulant effect of heparin because it binds more strongly to
heparin than to the chondroitin-4-sulfate chains of the carrier
molecule. Chemotactic for neutrophils and monocytes. Inhibits
endothelial cell proliferation, the short form is a more potent
inhibitor than the longer form. {ECO:0000269|PubMed:7644496}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7547867,
ECO:0000269|PubMed:8031770}.
-!- INTERACTION:
P02749:APOH; NbExp=2; IntAct=EBI-2565740, EBI-2114682;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7644496}.
-!- MASS SPECTROMETRY: Mass=7765; Method=Electrospray; Range=32-101;
Evidence={ECO:0000269|PubMed:7644496};
-!- MASS SPECTROMETRY: Mass=6033; Method=Electrospray; Range=48-101;
Note=Short form.; Evidence={ECO:0000269|PubMed:7644496};
-!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC)
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=CXCL4 entry;
URL="https://en.wikipedia.org/wiki/CXCL4";
-----------------------------------------------------------------------
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EMBL; M25897; AAA60066.1; -; mRNA.
EMBL; AF349466; AAK29643.1; -; Genomic_DNA.
EMBL; CR407677; CAG28605.1; -; mRNA.
EMBL; AC097709; AAY41003.1; -; Genomic_DNA.
EMBL; BC093965; AAH93965.1; -; mRNA.
EMBL; BC112093; AAI12094.1; -; mRNA.
CCDS; CCDS3562.1; -.
PIR; A60161; PFHU4.
RefSeq; NP_002610.1; NM_002619.3.
UniGene; Hs.81564; -.
PDB; 1DN3; NMR; -; A=59-73.
PDB; 1F9Q; X-ray; 2.00 A; A/B/C/D=32-101.
PDB; 1F9R; X-ray; 2.00 A; A/B/C/D=32-101.
PDB; 1F9S; X-ray; 2.38 A; A/B/C/D=32-101.
PDB; 1PFM; NMR; -; A/B/C/D=39-101.
PDB; 1PFN; NMR; -; A/B/C/D=39-101.
PDB; 1RHP; X-ray; 2.40 A; A/B/C/D=32-101.
PDB; 4R9W; X-ray; 2.50 A; A/B=32-101.
PDB; 4R9Y; X-ray; 4.11 A; A/B/C/D=32-101.
PDB; 4RAU; X-ray; 3.74 A; C/F/I/L/O/R/U/X=32-101.
PDBsum; 1DN3; -.
PDBsum; 1F9Q; -.
PDBsum; 1F9R; -.
PDBsum; 1F9S; -.
PDBsum; 1PFM; -.
PDBsum; 1PFN; -.
PDBsum; 1RHP; -.
PDBsum; 4R9W; -.
PDBsum; 4R9Y; -.
PDBsum; 4RAU; -.
ProteinModelPortal; P02776; -.
SMR; P02776; -.
BioGrid; 111219; 9.
DIP; DIP-56941N; -.
IntAct; P02776; 4.
STRING; 9606.ENSP00000296029; -.
BindingDB; P02776; -.
ChEMBL; CHEMBL3286075; -.
DrugBank; DB00055; Drotrecogin alfa.
PhosphoSitePlus; P02776; -.
BioMuta; PF4; -.
DMDM; 130304; -.
OGP; P02776; -.
PaxDb; P02776; -.
PeptideAtlas; P02776; -.
PRIDE; P02776; -.
TopDownProteomics; P02776; -.
Ensembl; ENST00000296029; ENSP00000296029; ENSG00000163737.
GeneID; 5196; -.
KEGG; hsa:5196; -.
UCSC; uc003hhi.4; human.
CTD; 5196; -.
DisGeNET; 5196; -.
EuPathDB; HostDB:ENSG00000163737.3; -.
GeneCards; PF4; -.
HGNC; HGNC:8861; PF4.
HPA; CAB026008; -.
HPA; HPA052485; -.
MIM; 173460; gene.
neXtProt; NX_P02776; -.
OpenTargets; ENSG00000163737; -.
PharmGKB; PA33203; -.
eggNOG; ENOG410J314; Eukaryota.
eggNOG; ENOG4111556; LUCA.
GeneTree; ENSGT00530000062901; -.
HOGENOM; HOG000220915; -.
HOVERGEN; HBG107789; -.
InParanoid; P02776; -.
KO; K05407; -.
OMA; GAGLHCP; -.
OrthoDB; EOG091G14JD; -.
PhylomeDB; P02776; -.
TreeFam; TF333433; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
EvolutionaryTrace; P02776; -.
GeneWiki; Platelet_factor_4; -.
GenomeRNAi; 5196; -.
PMAP-CutDB; P02776; -.
PRO; PR:P02776; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163737; -.
CleanEx; HS_PF4; -.
Genevisible; P02776; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0097679; C:other organism cytoplasm; IDA:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0020005; C:symbiont-containing vacuole membrane; IDA:UniProtKB.
GO; GO:0008009; F:chemokine activity; TAS:UniProtKB.
GO; GO:0048248; F:CXCR3 chemokine receptor binding; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0042832; P:defense response to protozoan; IDA:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0051873; P:killing by host of symbiont cells; IDA:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0030595; P:leukocyte chemotaxis; IDA:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0045918; P:negative regulation of cytolysis; IDA:BHF-UCL.
GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IDA:BHF-UCL.
GO; GO:0045653; P:negative regulation of megakaryocyte differentiation; IDA:UniProtKB.
GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IDA:BHF-UCL.
GO; GO:0030168; P:platelet activation; IDA:UniProtKB.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0030816; P:positive regulation of cAMP metabolic process; IDA:UniProtKB.
GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; IDA:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IDA:BHF-UCL.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IDA:BHF-UCL.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0042127; P:regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0032496; P:response to lipopolysaccharide; IBA:GO_Central.
CDD; cd00273; Chemokine_CXC; 1.
InterPro; IPR001089; Chemokine_CXC.
InterPro; IPR018048; Chemokine_CXC_CS.
InterPro; IPR001811; Chemokine_IL8-like_dom.
InterPro; IPR033899; CXC_Chemokine_domain.
InterPro; IPR027222; PF4.
PANTHER; PTHR10179; PTHR10179; 1.
PANTHER; PTHR10179:SF53; PTHR10179:SF53; 1.
Pfam; PF00048; IL8; 1.
PRINTS; PR00437; SMALLCYTKCXC.
SMART; SM00199; SCY; 1.
SUPFAM; SSF54117; SSF54117; 1.
PROSITE; PS00471; SMALL_CYTOKINES_CXC; 1.
1: Evidence at protein level;
3D-structure; Chemotaxis; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Heparin-binding;
Phosphoprotein; Reference proteome; Secreted; Signal.
SIGNAL 1 31 {ECO:0000269|PubMed:267922,
ECO:0000269|PubMed:601757,
ECO:0000269|PubMed:6445090,
ECO:0000269|PubMed:7644496,
ECO:0000269|PubMed:893407}.
CHAIN 32 101 Platelet factor 4.
/FTId=PRO_0000005068.
CHAIN 48 101 Platelet factor 4, short form.
{ECO:0000269|PubMed:7644496}.
/FTId=PRO_0000351217.
REGION 92 98 Heparin-binding.
MOD_RES 57 57 Phosphoserine.
{ECO:0000250|UniProtKB:P06765}.
DISULFID 41 67 {ECO:0000269|PubMed:6445090}.
DISULFID 43 83 {ECO:0000269|PubMed:6445090}.
CONFLICT 78 78 N -> D (in Ref. 8; AA sequence and 9; AA
sequence). {ECO:0000305}.
STRAND 42 44 {ECO:0000244|PDB:1F9Q}.
HELIX 52 54 {ECO:0000244|PDB:1F9Q}.
STRAND 55 61 {ECO:0000244|PDB:1F9Q}.
STRAND 64 66 {ECO:0000244|PDB:1F9S}.
STRAND 67 69 {ECO:0000244|PDB:1F9Q}.
STRAND 71 76 {ECO:0000244|PDB:1F9Q}.
STRAND 77 79 {ECO:0000244|PDB:1PFM}.
STRAND 81 83 {ECO:0000244|PDB:1F9Q}.
STRAND 86 88 {ECO:0000244|PDB:1F9Q}.
HELIX 90 99 {ECO:0000244|PDB:1F9Q}.
SEQUENCE 101 AA; 10845 MW; E96C2EFE9B944D85 CRC64;
MSSAAGFCAS RPGLLFLGLL LLPLVVAFAS AEAEEDGDLQ CLCVKTTSQV RPRHITSLEV
IKAGPHCPTA QLIATLKNGR KICLDLQAPL YKKIIKKLLE S


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