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Platelet basic protein (PBP) (C-X-C motif chemokine 7) (Leukocyte-derived growth factor) (LDGF) (Macrophage-derived growth factor) (MDGF) (Small-inducible cytokine B7) [Cleaved into: Connective tissue-activating peptide III (CTAP-III) (LA-PF4) (Low-affinity platelet factor IV); TC-2; Connective tissue-activating peptide III(1-81) (CTAP-III(1-81)); Beta-thromboglobulin (Beta-TG); Neutrophil-activating peptide 2(74) (NAP-2(74)); Neutrophil-activating peptide 2(73) (NAP-2(73)); Neutrophil-activating peptide 2 (NAP-2); TC-1; Neutrophil-activating peptide 2(1-66) (NAP-2(1-66)); Neutrophil-activating peptide 2(1-63) (NAP-2(1-63))]

 CXCL7_HUMAN             Reviewed;         128 AA.
P02775; B2R5F3; Q6IBJ8;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 3.
12-SEP-2018, entry version 193.
RecName: Full=Platelet basic protein;
Short=PBP;
AltName: Full=C-X-C motif chemokine 7;
AltName: Full=Leukocyte-derived growth factor;
Short=LDGF;
AltName: Full=Macrophage-derived growth factor;
Short=MDGF;
AltName: Full=Small-inducible cytokine B7;
Contains:
RecName: Full=Connective tissue-activating peptide III;
Short=CTAP-III;
AltName: Full=LA-PF4;
AltName: Full=Low-affinity platelet factor IV;
Contains:
RecName: Full=TC-2;
Contains:
RecName: Full=Connective tissue-activating peptide III(1-81);
Short=CTAP-III(1-81);
Contains:
RecName: Full=Beta-thromboglobulin;
Short=Beta-TG;
Contains:
RecName: Full=Neutrophil-activating peptide 2(74);
Short=NAP-2(74);
Contains:
RecName: Full=Neutrophil-activating peptide 2(73);
Short=NAP-2(73);
Contains:
RecName: Full=Neutrophil-activating peptide 2;
Short=NAP-2;
Contains:
RecName: Full=TC-1;
Contains:
RecName: Full=Neutrophil-activating peptide 2(1-66);
Short=NAP-2(1-66);
Contains:
RecName: Full=Neutrophil-activating peptide 2(1-63);
Short=NAP-2(1-63);
Flags: Precursor;
Name=PPBP; Synonyms=CTAP3, CXCL7, SCYB7, TGB1, THBGB1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Platelet;
PubMed=2713489;
Wenger R.H., Wicki A.N., Walz A., Kieffer N., Clemetson K.J.;
"Cloning of cDNA coding for connective tissue activating peptide III
from a human platelet-derived lambda gt11 expression library.";
Blood 73:1498-1503(1989).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1826003;
Majumdar S., Gonder D., Koutsis B., Poncz M.;
"Characterization of the human beta-thromboglobulin gene. Comparison
with the gene for platelet factor 4.";
J. Biol. Chem. 266:5785-5789(1991).
[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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Leukocyte;
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).
[9]
PROTEIN SEQUENCE OF 35-53.
PubMed=2423119; DOI=10.1021/bi00356a023;
Holt J.C., Harris M.E., Holt A.M., Lange E., Henschen A.,
Niewiarowski S.;
"Characterization of human platelet basic protein, a precursor form of
low-affinity platelet factor 4 and beta-thromboglobulin.";
Biochemistry 25:1988-1996(1986).
[10]
PROTEIN SEQUENCE OF 35-49.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[11]
PROTEIN SEQUENCE OF 44-126, IDENTIFICATION OF TC-1 AND TC-2, AND
FUNCTION.
PubMed=10877842; DOI=10.1074/jbc.275.27.20374;
Krijgsveld J., Zaat S.A., Meeldijk J., van Veelen P.A., Fang G.,
Poolman B., Brandt E., Ehlert J.E., Kuijpers A.J., Engbers G.H.,
Feijen J., Dankert J.;
"Thrombocidins, microbicidal proteins from human blood platelets, are
C-terminal deletion products of CXC chemokines.";
J. Biol. Chem. 275:20374-20381(2000).
[12]
PROTEIN SEQUENCE OF 44-66 AND 125-128.
PubMed=6572368; DOI=10.1073/pnas.80.3.765;
Castor C.W., Miller J.W., Walz D.A.;
"Structural and biological characteristics of connective tissue
activating peptide (CTAP-III), a major human platelet-derived growth
factor.";
Proc. Natl. Acad. Sci. U.S.A. 80:765-769(1983).
[13]
PROTEIN SEQUENCE OF 44-62.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[14]
PROTEIN SEQUENCE OF 48-126.
PubMed=77677; DOI=10.1021/bi00602a024;
Begg G.S., Pepper D.S., Chesterman C.N., Morgan F.J.;
"Complete covalent structure of human beta-thromboglobulin.";
Biochemistry 17:1739-1744(1978).
[15]
PROTEIN SEQUENCE OF 55-128, IDENTIFICATION OF NAP-2(73) AND NAP-2(74),
AND FUNCTION.
TISSUE=Platelet;
PubMed=8950790;
Piccardoni P., Evangelista V., Piccoli A., de Gaetano G., Walz A.,
Cerletti C.;
"Thrombin-activated human platelets release two NAP-2 variants that
stimulate polymorphonuclear leukocytes.";
Thromb. Haemost. 76:780-785(1996).
[16]
PROTEIN SEQUENCE OF 57-68.
PubMed=2783111; DOI=10.1016/0006-291X(89)92330-9;
Castor C.W., Walz D.A., Ragsdale C.G., Hossler P.A., Smith E.M.,
Bignall M.C., Aaron B.P., Mountjoy K.;
"Connective tissue activation. XXXIII. Biologically active cleavage
products of CTAP-III from human platelets.";
Biochem. Biophys. Res. Commun. 163:1071-1078(1989).
[17]
PROTEIN SEQUENCE OF 59-126.
PubMed=2522778; DOI=10.1016/0006-291X(89)92203-1;
Walz A., Baggiolini M.;
"A novel cleavage product of beta-thromboglobulin formed in cultures
of stimulated mononuclear cells activates human neutrophils.";
Biochem. Biophys. Res. Commun. 159:969-975(1989).
[18]
PROTEIN SEQUENCE OF 59-124, IDENTIFICATION OF NAP-2(1-66), AND
FUNCTION.
TISSUE=Peripheral blood monocyte;
PubMed=7890771; DOI=10.1074/jbc.270.11.6338;
Ehlert J.E., Petersen F., Kubbutat M.H., Gerdes J., Flad H.D.,
Brandt E.;
"Limited and defined truncation at the C-terminus enhances receptor
binding and degranulation activity of the neutrophil-activating
peptide 2 (NAP-2). Comparison of native and recombinant NAP-2
variants.";
J. Biol. Chem. 270:6338-6344(1995).
[19]
PROTEIN SEQUENCE OF 59-67.
PubMed=2406364; DOI=10.1084/jem.171.2.449;
Walz A., Baggiolini M.;
"Generation of the neutrophil-activating peptide NAP-2 from platelet
basic protein or connective tissue-activating peptide III through
monocyte proteases.";
J. Exp. Med. 171:449-454(1990).
[20]
SYNTHESIS OF 59-126.
PubMed=2007144; DOI=10.1021/bi00226a021;
Clark-Lewis I., Mose B., Walz A., Baggiolini M., Scott G.J.,
Aebersold R.;
"Chemical synthesis, purification, and characterization of two
inflammatory proteins, neutrophil activating peptide 1 (interleukin-8)
and neutrophil activating peptide.";
Biochemistry 30:3128-3135(1991).
[21]
IDENTIFICATION OF CTAP-III(1-81) AND NAP-2(1-63), FUNCTION, AND
PROTEOLYTIC PROCESSING OF C-TERMINAL.
PubMed=9794434;
Ehlert J.E., Gerdes J., Flad H.-D., Brandt E.;
"Novel C-terminally truncated isoforms of the CXC chemokine beta-
thromboglobulin and their impact on neutrophil functions.";
J. Immunol. 161:4975-4982(1998).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[23]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 59-128.
PubMed=8034022; DOI=10.1016/0014-5793(94)00573-7;
Kungl A.J., Machius M., Huber R., Schwer C., Lam C., Aschauer H.,
Ehn G., Lindley I.J.D., Auer M.;
"Purification, crystallization and preliminary X-ray diffraction
analysis of recombinant human neutrophil-activating peptide 2 (rhNAP-
2).";
FEBS Lett. 347:300-303(1994).
[24]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 59-128.
PubMed=7706245; DOI=10.1074/jbc.270.13.7077;
Malkowski M.G., Wu J.Y., Lazar J.B., Johnson P.H., Edwards B.F.P.;
"The crystal structure of recombinant human neutrophil-activating
peptide-2 (M6L) at 1.9-A resolution.";
J. Biol. Chem. 270:7077-7087(1995).
-!- FUNCTION: LA-PF4 stimulates DNA synthesis, mitosis, glycolysis,
intracellular cAMP accumulation, prostaglandin E2 secretion, and
synthesis of hyaluronic acid and sulfated glycosaminoglycan. It
also stimulates the formation and secretion of plasminogen
activator by human synovial cells. NAP-2 is a ligand for CXCR1 and
CXCR2, and NAP-2, NAP-2(73), NAP-2(74), NAP-2(1-66), and most
potent NAP-2(1-63) are chemoattractants and activators for
neutrophils. TC-1 and TC-2 are antibacterial proteins, in vitro
released from activated platelet alpha-granules. CTAP-III(1-81) is
more potent than CTAP-III desensitize chemokine-induced neutrophil
activation. {ECO:0000269|PubMed:10877842,
ECO:0000269|PubMed:7890771, ECO:0000269|PubMed:8950790,
ECO:0000269|PubMed:9794434}.
-!- SUBUNIT: Beta-thromboglobulin is a homotetramer.
-!- INTERACTION:
P13501:CCL5; NbExp=2; IntAct=EBI-718973, EBI-2848366;
Q07325:CXCL9; NbExp=2; IntAct=EBI-718973, EBI-3911467;
-!- SUBCELLULAR LOCATION: Secreted.
-!- PTM: Proteolytic removal of residues 1-9 produces the active
peptide connective tissue-activating peptide III (CTAP-III) (low-
affinity platelet factor IV (LA-PF4)).
-!- PTM: Proteolytic removal of residues 1-13 produces the active
peptide beta-thromboglobulin, which is released from platelets
along with platelet factor 4 and platelet-derived growth factor.
-!- PTM: NAP-2(1-66) is produced by proteolytical processing, probably
after secretion by leukocytes other than neutrophils.
{ECO:0000269|PubMed:9794434}.
-!- PTM: NAP-2(73) and NAP-2(74) seem not be produced by proteolytical
processing of secreted precursors but are released in an active
form from platelets. {ECO:0000269|PubMed:9794434}.
-!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC)
family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=CXCL7 entry;
URL="https://en.wikipedia.org/wiki/CXCL7";
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EMBL; M54995; AAA62836.1; -; mRNA.
EMBL; AF349466; AAK29642.1; -; Genomic_DNA.
EMBL; CR456805; CAG33086.1; -; mRNA.
EMBL; AC097709; AAY41004.1; -; Genomic_DNA.
EMBL; AK312166; BAG35100.1; -; mRNA.
EMBL; CH471057; EAX05695.1; -; Genomic_DNA.
EMBL; BC028217; AAH28217.1; -; mRNA.
CCDS; CCDS3563.1; -.
PIR; A39546; TGHU.
RefSeq; NP_002695.1; NM_002704.3.
UniGene; Hs.2164; -.
PDB; 1F9P; X-ray; 1.93 A; A=44-128.
PDB; 1NAP; X-ray; 1.90 A; A/B/C/D=59-128.
PDB; 1TVX; X-ray; 1.75 A; A/B/C/D=54-128.
PDBsum; 1F9P; -.
PDBsum; 1NAP; -.
PDBsum; 1TVX; -.
ProteinModelPortal; P02775; -.
SMR; P02775; -.
BioGrid; 111469; 15.
DIP; DIP-5913N; -.
IntAct; P02775; 32.
MINT; P02775; -.
STRING; 9606.ENSP00000296028; -.
DrugBank; DB03635; Ethanesulfonic Acid.
iPTMnet; P02775; -.
PhosphoSitePlus; P02775; -.
BioMuta; PPBP; -.
DMDM; 129874; -.
SWISS-2DPAGE; P02775; -.
PaxDb; P02775; -.
PeptideAtlas; P02775; -.
PRIDE; P02775; -.
ProteomicsDB; 51592; -.
TopDownProteomics; P02775; -.
DNASU; 5473; -.
Ensembl; ENST00000296028; ENSP00000296028; ENSG00000163736.
GeneID; 5473; -.
KEGG; hsa:5473; -.
UCSC; uc003hhj.4; human.
CTD; 5473; -.
DisGeNET; 5473; -.
EuPathDB; HostDB:ENSG00000163736.3; -.
GeneCards; PPBP; -.
H-InvDB; HIX0031528; -.
HGNC; HGNC:9240; PPBP.
HPA; CAB017624; -.
HPA; HPA008354; -.
MIM; 121010; gene.
neXtProt; NX_P02775; -.
OpenTargets; ENSG00000163736; -.
PharmGKB; PA33561; -.
eggNOG; ENOG410JG75; Eukaryota.
eggNOG; ENOG4111BTH; LUCA.
GeneTree; ENSGT00530000062901; -.
HOGENOM; HOG000220915; -.
HOVERGEN; HBG107789; -.
InParanoid; P02775; -.
KO; K10029; -.
OMA; LYAELRC; -.
OrthoDB; EOG091G10E9; -.
PhylomeDB; P02775; -.
TreeFam; TF333433; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; P02775; -.
GeneWiki; CXCL7; -.
GenomeRNAi; 5473; -.
PMAP-CutDB; P02775; -.
PRO; PR:P02775; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163736; Expressed in 125 organ(s), highest expression level in mononuclear cell.
CleanEx; HS_PPBP; -.
Genevisible; P02775; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central.
GO; GO:0005355; F:glucose transmembrane transporter activity; TAS:ProtInc.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IBA:GO_Central.
GO; GO:1904659; P:glucose transmembrane transport; TAS:ProtInc.
GO; GO:0006955; P:immune response; IBA:GO_Central.
GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
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; IPR036048; Interleukin_8-like_sf.
PANTHER; PTHR10179; PTHR10179; 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; Antibiotic; Antimicrobial; Chemotaxis;
Cleavage on pair of basic residues; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Growth factor; Mitogen;
Reference proteome; Secreted; Signal.
SIGNAL 1 34 {ECO:0000269|PubMed:15340161,
ECO:0000269|PubMed:2423119}.
CHAIN 35 128 Platelet basic protein.
/FTId=PRO_0000005088.
CHAIN 44 128 Connective tissue-activating peptide III.
/FTId=PRO_0000005089.
CHAIN 44 126 TC-2.
/FTId=PRO_0000005090.
CHAIN 44 124 Connective tissue-activating peptide
III(1-81).
/FTId=PRO_0000041949.
CHAIN 48 128 Beta-thromboglobulin.
/FTId=PRO_0000005091.
CHAIN 55 128 Neutrophil-activating peptide 2(74).
/FTId=PRO_0000005092.
CHAIN 56 128 Neutrophil-activating peptide 2(73).
/FTId=PRO_0000005093.
CHAIN 59 128 Neutrophil-activating peptide 2.
/FTId=PRO_0000005094.
CHAIN 59 126 TC-1.
/FTId=PRO_0000005095.
CHAIN 59 124 Neutrophil-activating peptide 2(1-66).
/FTId=PRO_0000005096.
CHAIN 59 121 Neutrophil-activating peptide 2(1-63).
/FTId=PRO_0000041950.
DISULFID 63 89
DISULFID 65 105
STRAND 50 54 {ECO:0000244|PDB:1F9P}.
HELIX 58 60 {ECO:0000244|PDB:1F9P}.
HELIX 74 76 {ECO:0000244|PDB:1TVX}.
STRAND 77 83 {ECO:0000244|PDB:1TVX}.
STRAND 89 91 {ECO:0000244|PDB:1NAP}.
STRAND 93 98 {ECO:0000244|PDB:1TVX}.
STRAND 103 106 {ECO:0000244|PDB:1TVX}.
HELIX 111 122 {ECO:0000244|PDB:1TVX}.
SEQUENCE 128 AA; 13894 MW; BEAB7B75916723D9 CRC64;
MSLRLDTTPS CNSARPLHAL QVLLLLSLLL TALASSTKGQ TKRNLAKGKE ESLDSDLYAE
LRCMCIKTTS GIHPKNIQSL EVIGKGTHCN QVEVIATLKD GRKICLDPDA PRIKKIVQKK
LAGDESAD


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