PF4V_HUMAN
ID PF4V_HUMAN Reviewed; 104 AA.
AC P10720; A1L4S0;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Platelet factor 4 variant;
DE AltName: Full=C-X-C motif chemokine 4 variant;
DE AltName: Full=CXCL4L1;
DE AltName: Full=PF4alt;
DE AltName: Full=PF4var1;
DE Contains:
DE RecName: Full=Platelet factor 4 variant(4-74);
DE Contains:
DE RecName: Full=Platelet factor 4 variant(5-74);
DE Contains:
DE RecName: Full=Platelet factor 4 variant(6-74);
DE Flags: Precursor;
GN Name=PF4V1; Synonyms=CXCL4V1, SCYB4V1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2725510; DOI=10.1128/mcb.9.4.1445-1451.1989;
RA Green C.J., St Charles R., Edwards B.F.P., Johnson P.H.;
RT "Identification and characterization of PF4var1, a human gene variant of
RT platelet factor 4.";
RL Mol. Cell. Biol. 9:1445-1451(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-104.
RX PubMed=1695112;
RA Eisman R., Surrey S., Ramachandran B., Schwartz E., Poncz M.;
RT "Structural and functional comparison of the genes for human platelet
RT factor 4 and PF4alt.";
RL Blood 76:336-344(1990).
RN [5]
RP PROTEIN SEQUENCE OF 31-54, FUNCTION, AND MASS SPECTROMETRY.
RX PubMed=15459074; DOI=10.1161/01.res.0000146674.38319.07;
RA Struyf S., Burdick M.D., Proost P., Van Damme J., Strieter R.M.;
RT "Platelets release CXCL4L1, a nonallelic variant of the chemokine platelet
RT factor-4/CXCL4 and potent inhibitor of angiogenesis.";
RL Circ. Res. 95:855-857(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 35-104, DISULFIDE BONDS,
RP HEPARIN-BINDING REGION, AND SUBUNIT.
RX PubMed=23536183; DOI=10.1074/jbc.m113.455329;
RA Kuo J.H., Chen Y.P., Liu J.S., Dubrac A., Quemener C., Prats H.,
RA Bikfalvi A., Wu W.G., Sue S.C.;
RT "Alternative C-terminal helix orientation alters chemokine function:
RT Structure of the Anti-angiogenic Chemokine, CXCL4L1.";
RL J. Biol. Chem. 288:13522-13533(2013).
CC -!- FUNCTION: Inhibitor of angiogenesis. Inhibitor of endothelial cell
CC chemotaxis (in vitro). {ECO:0000269|PubMed:15459074}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:23536183}.
CC -!- INTERACTION:
CC P10720; O00585: CCL21; NbExp=2; IntAct=EBI-1223944, EBI-953695;
CC P10720; O15444: CCL25; NbExp=2; IntAct=EBI-1223944, EBI-7783341;
CC P10720; O14625: CXCL11; NbExp=2; IntAct=EBI-1223944, EBI-2871971;
CC P10720; P48061: CXCL12; NbExp=4; IntAct=EBI-1223944, EBI-3913254;
CC P10720; P47992: XCL1; NbExp=2; IntAct=EBI-1223944, EBI-10209901;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: The N-terminal processed forms of platelet factor 4 variant seems
CC to be produced by proteolytic cleavage. The most abundant form is
CC Platelet factor 4 variant(5-74).
CC -!- MASS SPECTROMETRY: [Platelet factor 4 variant]: Mass=8250.9;
CC Method=Electrospray; Note=Platelet factor 4 variant.;
CC Evidence={ECO:0000269|PubMed:15459074};
CC -!- MASS SPECTROMETRY: [Platelet factor 4 variant(4-74)]: Mass=7877.7;
CC Method=Electrospray; Note=Platelet factor 4 variant(4-74).;
CC Evidence={ECO:0000269|PubMed:15459074};
CC -!- MASS SPECTROMETRY: [Platelet factor 4 variant(5-74)]: Mass=7805.8;
CC Method=Electrospray; Note=Platelet factor 4 variant(5-74).;
CC Evidence={ECO:0000269|PubMed:15459074};
CC -!- MASS SPECTROMETRY: [Platelet factor 4 variant(6-74)]: Mass=7678.6;
CC Method=Electrospray; Note=Platelet factor 4 variant(6-74).;
CC Evidence={ECO:0000269|PubMed:15459074};
CC -!- MISCELLANEOUS: Binding to heparin is much weaker than in the close
CC homolog PF4/CXCL4.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
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DR EMBL; M26167; AAA60067.1; -; Genomic_DNA.
DR EMBL; CH471057; EAX05692.1; -; Genomic_DNA.
DR EMBL; BC130653; AAI30654.1; -; mRNA.
DR EMBL; BC130657; AAI30658.1; -; mRNA.
DR CCDS; CCDS3561.1; -.
DR PIR; A31941; PFHU4A.
DR RefSeq; NP_002611.1; NM_002620.3.
DR PDB; 4HSV; X-ray; 2.08 A; A/B/C/D=35-104.
DR PDBsum; 4HSV; -.
DR AlphaFoldDB; P10720; -.
DR SMR; P10720; -.
DR BioGRID; 111220; 27.
DR IntAct; P10720; 18.
DR STRING; 9606.ENSP00000226524; -.
DR iPTMnet; P10720; -.
DR PhosphoSitePlus; P10720; -.
DR BioMuta; PF4V1; -.
DR DMDM; 130306; -.
DR jPOST; P10720; -.
DR MassIVE; P10720; -.
DR PaxDb; P10720; -.
DR PeptideAtlas; P10720; -.
DR PRIDE; P10720; -.
DR ProteomicsDB; 52639; -.
DR TopDownProteomics; P10720; -.
DR Antibodypedia; 44434; 96 antibodies from 19 providers.
DR DNASU; 5197; -.
DR Ensembl; ENST00000226524.4; ENSP00000226524.3; ENSG00000109272.4.
DR GeneID; 5197; -.
DR KEGG; hsa:5197; -.
DR MANE-Select; ENST00000226524.4; ENSP00000226524.3; NM_002620.4; NP_002611.1.
DR UCSC; uc003hhg.2; human.
DR CTD; 5197; -.
DR DisGeNET; 5197; -.
DR GeneCards; PF4V1; -.
DR HGNC; HGNC:8862; PF4V1.
DR HPA; ENSG00000109272; Tissue enhanced (intestine, lymphoid tissue).
DR MIM; 173461; gene.
DR neXtProt; NX_P10720; -.
DR OpenTargets; ENSG00000109272; -.
DR PharmGKB; PA33204; -.
DR VEuPathDB; HostDB:ENSG00000109272; -.
DR eggNOG; ENOG502TF57; Eukaryota.
DR GeneTree; ENSGT00940000163666; -.
DR HOGENOM; CLU_143902_1_2_1; -.
DR InParanoid; P10720; -.
DR OMA; RATHPEM; -.
DR OrthoDB; 1617719at2759; -.
DR PhylomeDB; P10720; -.
DR TreeFam; TF333433; -.
DR PathwayCommons; P10720; -.
DR Reactome; R-HSA-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR SignaLink; P10720; -.
DR BioGRID-ORCS; 5197; 9 hits in 1051 CRISPR screens.
DR GenomeRNAi; 5197; -.
DR Pharos; P10720; Tbio.
DR PRO; PR:P10720; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P10720; protein.
DR Bgee; ENSG00000109272; Expressed in monocyte and 85 other tissues.
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:0008201; F:heparin binding; IEA:UniProtKB-KW.
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:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0030168; P:platelet activation; IEA:InterPro.
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:SF38; PTHR10179:SF38; 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; Cytokine; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Heparin-binding; Proteoglycan; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:15459074"
FT CHAIN 31..104
FT /note="Platelet factor 4 variant"
FT /id="PRO_0000005071"
FT CHAIN 34..104
FT /note="Platelet factor 4 variant(4-74)"
FT /id="PRO_0000005072"
FT CHAIN 35..104
FT /note="Platelet factor 4 variant(5-74)"
FT /id="PRO_0000005073"
FT CHAIN 36..104
FT /note="Platelet factor 4 variant(6-74)"
FT /id="PRO_0000005074"
FT BINDING 95..101
FT /ligand="heparin"
FT /ligand_id="ChEBI:CHEBI:28304"
FT DISULFID 44..70
FT /evidence="ECO:0000269|PubMed:23536183"
FT DISULFID 46..86
FT /evidence="ECO:0000269|PubMed:23536183"
FT CONFLICT 77
FT /note="A -> S (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:4HSV"
FT TURN 55..57
FT /evidence="ECO:0007829|PDB:4HSV"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:4HSV"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:4HSV"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:4HSV"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4HSV"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:4HSV"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:4HSV"
SQ SEQUENCE 104 AA; 11553 MW; 786FE2B288532E28 CRC64;
MSSAARSRLT RATRQEMLFL ALLLLPVVVA FARAEAEEDG DLQCLCVKTT SQVRPRHITS
LEVIKAGPHC PTAQLIATLK NGRKICLDLQ ALLYKKIIKE HLES
