CXCL7_HUMAN
ID CXCL7_HUMAN Reviewed; 128 AA.
AC P02775; B2R5F3; Q6IBJ8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 3.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Platelet basic protein;
DE Short=PBP;
DE AltName: Full=C-X-C motif chemokine 7;
DE AltName: Full=Leukocyte-derived growth factor;
DE Short=LDGF;
DE AltName: Full=Macrophage-derived growth factor;
DE Short=MDGF;
DE AltName: Full=Small-inducible cytokine B7;
DE Contains:
DE RecName: Full=Connective tissue-activating peptide III;
DE Short=CTAP-III;
DE AltName: Full=LA-PF4;
DE AltName: Full=Low-affinity platelet factor IV;
DE Contains:
DE RecName: Full=TC-2;
DE Contains:
DE RecName: Full=Connective tissue-activating peptide III(1-81);
DE Short=CTAP-III(1-81);
DE Contains:
DE RecName: Full=Beta-thromboglobulin;
DE Short=Beta-TG;
DE Contains:
DE RecName: Full=Neutrophil-activating peptide 2(74);
DE Short=NAP-2(74);
DE Contains:
DE RecName: Full=Neutrophil-activating peptide 2(73);
DE Short=NAP-2(73);
DE Contains:
DE RecName: Full=Neutrophil-activating peptide 2;
DE Short=NAP-2;
DE Contains:
DE RecName: Full=TC-1;
DE Contains:
DE RecName: Full=Neutrophil-activating peptide 2(1-66);
DE Short=NAP-2(1-66);
DE Contains:
DE RecName: Full=Neutrophil-activating peptide 2(1-63);
DE Short=NAP-2(1-63);
DE Flags: Precursor;
GN Name=PPBP; Synonyms=CTAP3, CXCL7, SCYB7, TGB1, THBGB1;
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 [MRNA].
RC TISSUE=Platelet;
RX PubMed=2713489;
RA Wenger R.H., Wicki A.N., Walz A., Kieffer N., Clemetson K.J.;
RT "Cloning of cDNA coding for connective tissue activating peptide III from a
RT human platelet-derived lambda gt11 expression library.";
RL Blood 73:1498-1503(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1826003; DOI=10.1016/s0021-9258(19)67665-9;
RA Majumdar S., Gonder D., Koutsis B., Poncz M.;
RT "Characterization of the human beta-thromboglobulin gene. Comparison with
RT the gene for platelet factor 4.";
RL J. Biol. Chem. 266:5785-5789(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11468158; DOI=10.1182/blood.v98.3.610;
RA Zhang C., Thornton M.A., Kowalska M.A., Sachis B.S., Feldman M., Poncz M.,
RA McKenzie S.E., Reilly M.P.;
RT "Localization of distal regulatory domains in the megakaryocyte-specific
RT platelet basic protein/platelet factor 4 gene locus.";
RL Blood 98:610-617(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Leukocyte;
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 [9]
RP PROTEIN SEQUENCE OF 35-53.
RX PubMed=2423119; DOI=10.1021/bi00356a023;
RA Holt J.C., Harris M.E., Holt A.M., Lange E., Henschen A., Niewiarowski S.;
RT "Characterization of human platelet basic protein, a precursor form of low-
RT affinity platelet factor 4 and beta-thromboglobulin.";
RL Biochemistry 25:1988-1996(1986).
RN [10]
RP PROTEIN SEQUENCE OF 35-49.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [11]
RP PROTEIN SEQUENCE OF 44-126, IDENTIFICATION OF TC-1 AND TC-2, AND FUNCTION.
RX PubMed=10877842; DOI=10.1074/jbc.275.27.20374;
RA Krijgsveld J., Zaat S.A., Meeldijk J., van Veelen P.A., Fang G.,
RA Poolman B., Brandt E., Ehlert J.E., Kuijpers A.J., Engbers G.H., Feijen J.,
RA Dankert J.;
RT "Thrombocidins, microbicidal proteins from human blood platelets, are C-
RT terminal deletion products of CXC chemokines.";
RL J. Biol. Chem. 275:20374-20381(2000).
RN [12]
RP PROTEIN SEQUENCE OF 44-66 AND 125-128.
RX PubMed=6572368; DOI=10.1073/pnas.80.3.765;
RA Castor C.W., Miller J.W., Walz D.A.;
RT "Structural and biological characteristics of connective tissue activating
RT peptide (CTAP-III), a major human platelet-derived growth factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:765-769(1983).
RN [13]
RP PROTEIN SEQUENCE OF 44-62.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [14]
RP PROTEIN SEQUENCE OF 48-126.
RX PubMed=77677; DOI=10.1021/bi00602a024;
RA Begg G.S., Pepper D.S., Chesterman C.N., Morgan F.J.;
RT "Complete covalent structure of human beta-thromboglobulin.";
RL Biochemistry 17:1739-1744(1978).
RN [15]
RP PROTEIN SEQUENCE OF 55-128, IDENTIFICATION OF NAP-2(73) AND NAP-2(74), AND
RP FUNCTION.
RC TISSUE=Platelet;
RX PubMed=8950790;
RA Piccardoni P., Evangelista V., Piccoli A., de Gaetano G., Walz A.,
RA Cerletti C.;
RT "Thrombin-activated human platelets release two NAP-2 variants that
RT stimulate polymorphonuclear leukocytes.";
RL Thromb. Haemost. 76:780-785(1996).
RN [16]
RP PROTEIN SEQUENCE OF 57-68.
RX PubMed=2783111; DOI=10.1016/0006-291x(89)92330-9;
RA Castor C.W., Walz D.A., Ragsdale C.G., Hossler P.A., Smith E.M.,
RA Bignall M.C., Aaron B.P., Mountjoy K.;
RT "Connective tissue activation. XXXIII. Biologically active cleavage
RT products of CTAP-III from human platelets.";
RL Biochem. Biophys. Res. Commun. 163:1071-1078(1989).
RN [17]
RP PROTEIN SEQUENCE OF 59-126.
RX PubMed=2522778; DOI=10.1016/0006-291x(89)92203-1;
RA Walz A., Baggiolini M.;
RT "A novel cleavage product of beta-thromboglobulin formed in cultures of
RT stimulated mononuclear cells activates human neutrophils.";
RL Biochem. Biophys. Res. Commun. 159:969-975(1989).
RN [18]
RP PROTEIN SEQUENCE OF 59-124, IDENTIFICATION OF NAP-2(1-66), AND FUNCTION.
RC TISSUE=Peripheral blood monocyte;
RX PubMed=7890771; DOI=10.1074/jbc.270.11.6338;
RA Ehlert J.E., Petersen F., Kubbutat M.H., Gerdes J., Flad H.D., Brandt E.;
RT "Limited and defined truncation at the C-terminus enhances receptor binding
RT and degranulation activity of the neutrophil-activating peptide 2 (NAP-2).
RT Comparison of native and recombinant NAP-2 variants.";
RL J. Biol. Chem. 270:6338-6344(1995).
RN [19]
RP PROTEIN SEQUENCE OF 59-67.
RX PubMed=2406364; DOI=10.1084/jem.171.2.449;
RA Walz A., Baggiolini M.;
RT "Generation of the neutrophil-activating peptide NAP-2 from platelet basic
RT protein or connective tissue-activating peptide III through monocyte
RT proteases.";
RL J. Exp. Med. 171:449-454(1990).
RN [20]
RP SYNTHESIS OF 59-126.
RX PubMed=2007144; DOI=10.1021/bi00226a021;
RA Clark-Lewis I., Mose B., Walz A., Baggiolini M., Scott G.J., Aebersold R.;
RT "Chemical synthesis, purification, and characterization of two inflammatory
RT proteins, neutrophil activating peptide 1 (interleukin-8) and neutrophil
RT activating peptide.";
RL Biochemistry 30:3128-3135(1991).
RN [21]
RP IDENTIFICATION OF CTAP-III(1-81) AND NAP-2(1-63), FUNCTION, AND PROTEOLYTIC
RP PROCESSING OF C-TERMINAL.
RX PubMed=9794434;
RA Ehlert J.E., Gerdes J., Flad H.-D., Brandt E.;
RT "Novel C-terminally truncated isoforms of the CXC chemokine beta-
RT thromboglobulin and their impact on neutrophil functions.";
RL J. Immunol. 161:4975-4982(1998).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 59-128.
RX PubMed=8034022; DOI=10.1016/0014-5793(94)00573-7;
RA Kungl A.J., Machius M., Huber R., Schwer C., Lam C., Aschauer H., Ehn G.,
RA Lindley I.J.D., Auer M.;
RT "Purification, crystallization and preliminary X-ray diffraction analysis
RT of recombinant human neutrophil-activating peptide 2 (rhNAP-2).";
RL FEBS Lett. 347:300-303(1994).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 59-128.
RX PubMed=7706245; DOI=10.1074/jbc.270.13.7077;
RA Malkowski M.G., Wu J.Y., Lazar J.B., Johnson P.H., Edwards B.F.P.;
RT "The crystal structure of recombinant human neutrophil-activating peptide-2
RT (M6L) at 1.9-A resolution.";
RL J. Biol. Chem. 270:7077-7087(1995).
CC -!- FUNCTION: LA-PF4 stimulates DNA synthesis, mitosis, glycolysis,
CC intracellular cAMP accumulation, prostaglandin E2 secretion, and
CC synthesis of hyaluronic acid and sulfated glycosaminoglycan. It also
CC stimulates the formation and secretion of plasminogen activator by
CC human synovial cells. NAP-2 is a ligand for CXCR1 and CXCR2, and NAP-2,
CC NAP-2(73), NAP-2(74), NAP-2(1-66), and most potent NAP-2(1-63) are
CC chemoattractants and activators for neutrophils. TC-1 and TC-2 are
CC antibacterial proteins, in vitro released from activated platelet
CC alpha-granules. CTAP-III(1-81) is more potent than CTAP-III desensitize
CC chemokine-induced neutrophil activation. {ECO:0000269|PubMed:10877842,
CC ECO:0000269|PubMed:7890771, ECO:0000269|PubMed:8950790,
CC ECO:0000269|PubMed:9794434}.
CC -!- SUBUNIT: Beta-thromboglobulin is a homotetramer.
CC -!- INTERACTION:
CC P02775; P06307: CCK; NbExp=3; IntAct=EBI-718973, EBI-6624398;
CC P02775; P13501: CCL5; NbExp=2; IntAct=EBI-718973, EBI-2848366;
CC P02775; Q07325: CXCL9; NbExp=2; IntAct=EBI-718973, EBI-3911467;
CC P02775; O75400-2: PRPF40A; NbExp=3; IntAct=EBI-718973, EBI-5280197;
CC P02775; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-718973, EBI-2623095;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: Proteolytic removal of residues 1-9 produces the active peptide
CC connective tissue-activating peptide III (CTAP-III) (low-affinity
CC platelet factor IV (LA-PF4)).
CC -!- PTM: Proteolytic removal of residues 1-13 produces the active peptide
CC beta-thromboglobulin, which is released from platelets along with
CC platelet factor 4 and platelet-derived growth factor.
CC -!- PTM: NAP-2(1-66) is produced by proteolytical processing, probably
CC after secretion by leukocytes other than neutrophils.
CC {ECO:0000269|PubMed:9794434}.
CC -!- PTM: NAP-2(73) and NAP-2(74) seem not be produced by proteolytical
CC processing of secreted precursors but are released in an active form
CC from platelets. {ECO:0000269|PubMed:9794434}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXCL7 entry;
CC URL="https://en.wikipedia.org/wiki/CXCL7";
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DR EMBL; M54995; AAA62836.1; -; mRNA.
DR EMBL; AF349466; AAK29642.1; -; Genomic_DNA.
DR EMBL; CR456805; CAG33086.1; -; mRNA.
DR EMBL; AC097709; AAY41004.1; -; Genomic_DNA.
DR EMBL; AK312166; BAG35100.1; -; mRNA.
DR EMBL; CH471057; EAX05695.1; -; Genomic_DNA.
DR EMBL; BC028217; AAH28217.1; -; mRNA.
DR CCDS; CCDS3563.1; -.
DR PIR; A39546; TGHU.
DR RefSeq; NP_002695.1; NM_002704.3.
DR PDB; 1F9P; X-ray; 1.93 A; A=44-128.
DR PDB; 1NAP; X-ray; 1.90 A; A/B/C/D=59-128.
DR PDB; 1TVX; X-ray; 1.75 A; A/B/C/D=54-128.
DR PDBsum; 1F9P; -.
DR PDBsum; 1NAP; -.
DR PDBsum; 1TVX; -.
DR AlphaFoldDB; P02775; -.
DR SMR; P02775; -.
DR BioGRID; 111469; 27.
DR DIP; DIP-5913N; -.
DR IntAct; P02775; 35.
DR MINT; P02775; -.
DR STRING; 9606.ENSP00000296028; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB03635; Ethanesulfonic acid.
DR iPTMnet; P02775; -.
DR PhosphoSitePlus; P02775; -.
DR BioMuta; PPBP; -.
DR DMDM; 129874; -.
DR SWISS-2DPAGE; P02775; -.
DR jPOST; P02775; -.
DR MassIVE; P02775; -.
DR PaxDb; P02775; -.
DR PeptideAtlas; P02775; -.
DR PRIDE; P02775; -.
DR ProteomicsDB; 51592; -.
DR TopDownProteomics; P02775; -.
DR Antibodypedia; 1902; 642 antibodies from 36 providers.
DR DNASU; 5473; -.
DR Ensembl; ENST00000296028.4; ENSP00000296028.3; ENSG00000163736.4.
DR GeneID; 5473; -.
DR KEGG; hsa:5473; -.
DR MANE-Select; ENST00000296028.4; ENSP00000296028.3; NM_002704.3; NP_002695.1.
DR UCSC; uc003hhj.4; human.
DR CTD; 5473; -.
DR DisGeNET; 5473; -.
DR GeneCards; PPBP; -.
DR HGNC; HGNC:9240; PPBP.
DR HPA; ENSG00000163736; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 121010; gene.
DR neXtProt; NX_P02775; -.
DR OpenTargets; ENSG00000163736; -.
DR PharmGKB; PA33561; -.
DR VEuPathDB; HostDB:ENSG00000163736; -.
DR eggNOG; ENOG502S7MM; Eukaryota.
DR GeneTree; ENSGT00940000162559; -.
DR HOGENOM; CLU_143902_1_1_1; -.
DR InParanoid; P02775; -.
DR OMA; CKSARPF; -.
DR OrthoDB; 1617719at2759; -.
DR PhylomeDB; P02775; -.
DR TreeFam; TF333433; -.
DR PathwayCommons; P02775; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P02775; -.
DR SIGNOR; P02775; -.
DR BioGRID-ORCS; 5473; 12 hits in 1066 CRISPR screens.
DR EvolutionaryTrace; P02775; -.
DR GeneWiki; CXCL7; -.
DR GenomeRNAi; 5473; -.
DR Pharos; P02775; Tbio.
DR PRO; PR:P02775; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P02775; protein.
DR Bgee; ENSG00000163736; Expressed in monocyte and 128 other tissues.
DR Genevisible; P02775; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
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:0005355; F:glucose transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:1904659; P:glucose transmembrane transport; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
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 PANTHER; PTHR10179; PTHR10179; 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; Antibiotic; Antimicrobial; Chemotaxis;
KW Cleavage on pair of basic residues; Cytokine; Direct protein sequencing;
KW Disulfide bond; Growth factor; Mitogen; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:2423119"
FT CHAIN 35..128
FT /note="Platelet basic protein"
FT /id="PRO_0000005088"
FT CHAIN 44..128
FT /note="Connective tissue-activating peptide III"
FT /id="PRO_0000005089"
FT CHAIN 44..126
FT /note="TC-2"
FT /id="PRO_0000005090"
FT CHAIN 44..124
FT /note="Connective tissue-activating peptide III(1-81)"
FT /id="PRO_0000041949"
FT CHAIN 48..128
FT /note="Beta-thromboglobulin"
FT /id="PRO_0000005091"
FT CHAIN 55..128
FT /note="Neutrophil-activating peptide 2(74)"
FT /id="PRO_0000005092"
FT CHAIN 56..128
FT /note="Neutrophil-activating peptide 2(73)"
FT /id="PRO_0000005093"
FT CHAIN 59..128
FT /note="Neutrophil-activating peptide 2"
FT /id="PRO_0000005094"
FT CHAIN 59..126
FT /note="TC-1"
FT /id="PRO_0000005095"
FT CHAIN 59..124
FT /note="Neutrophil-activating peptide 2(1-66)"
FT /id="PRO_0000005096"
FT CHAIN 59..121
FT /note="Neutrophil-activating peptide 2(1-63)"
FT /id="PRO_0000041950"
FT DISULFID 63..89
FT DISULFID 65..105
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1F9P"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:1F9P"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1TVX"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:1TVX"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:1NAP"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1TVX"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:1TVX"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:1TVX"
SQ SEQUENCE 128 AA; 13894 MW; BEAB7B75916723D9 CRC64;
MSLRLDTTPS CNSARPLHAL QVLLLLSLLL TALASSTKGQ TKRNLAKGKE ESLDSDLYAE
LRCMCIKTTS GIHPKNIQSL EVIGKGTHCN QVEVIATLKD GRKICLDPDA PRIKKIVQKK
LAGDESAD
