GROA_HUMAN
ID GROA_HUMAN Reviewed; 107 AA.
AC P09341; Q9UCR7;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Growth-regulated alpha protein;
DE AltName: Full=C-X-C motif chemokine 1;
DE AltName: Full=GRO-alpha(1-73);
DE AltName: Full=Melanoma growth stimulatory activity;
DE Short=MGSA;
DE AltName: Full=Neutrophil-activating protein 3;
DE Short=NAP-3;
DE Contains:
DE RecName: Full=GRO-alpha(4-73);
DE Contains:
DE RecName: Full=GRO-alpha(5-73);
DE Contains:
DE RecName: Full=GRO-alpha(6-73);
DE Flags: Precursor;
GN Name=CXCL1; Synonyms=GRO, GRO1, GROA, MGSA, SCYB1;
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].
RX PubMed=2890161; DOI=10.1073/pnas.84.20.7188;
RA Anisowicz A., Bardwell L., Sager R.;
RT "Constitutive overexpression of a growth-regulated gene in transformed
RT Chinese hamster and human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:7188-7192(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2970963; DOI=10.1002/j.1460-2075.1988.tb03042.x;
RA Richmond A., Balentien E., Thomas H.G., Flaggs G., Barton D.E., Spiess J.,
RA Bordoni R., Francke U., Derynck R.;
RT "Molecular characterization and chromosomal mapping of melanoma growth
RT stimulatory activity, a growth factor structurally related to beta-
RT thromboglobulin.";
RL EMBO J. 7:2025-2033(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=2129556; DOI=10.1093/nar/18.21.6453;
RA Baker N.E., Kucera G., Richmond A.;
RT "Nucleotide sequence of the human melanoma growth stimulatory activity
RT (MGSA) gene.";
RL Nucleic Acids Res. 18:6453-6453(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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 [6]
RP PROTEIN SEQUENCE OF 35-107, IDENTIFICATION OF GRO-ALPHA(4-73);
RP GRO-ALPHA(5-73) AND GRO-ALPHA(6-73), PROTEOLYTIC PROCESSING OF N-TERMINAL,
RP AND FUNCTION.
RC TISSUE=Peripheral blood monocyte;
RX PubMed=10095777; DOI=10.1046/j.1432-1327.1999.00166.x;
RA Wuyts A., Govaerts C., Struyf S., Lenaerts J.-P., Put W., Conings R.,
RA Proost P., Van Damme J.;
RT "Isolation of the CXC chemokines ENA-78, GRO alpha and GRO gamma from tumor
RT cells and leukocytes reveals NH2-terminal heterogeneity. Functional
RT comparison of different natural isoforms.";
RL Eur. J. Biochem. 260:421-429(1999).
RN [7]
RP PROTEIN SEQUENCE OF 35-65.
RX PubMed=2182761; DOI=10.1084/jem.171.4.1091;
RA Schroeder J.-M., Persoon N.L.M., Christophers E.;
RT "Lipopolysaccharide-stimulated human monocytes secrete, apart from
RT neutrophil-activating peptide 1/interleukin 8, a second neutrophil-
RT activating protein. NH2-terminal amino acid sequence identity with melanoma
RT growth stimulatory activity.";
RL J. Exp. Med. 171:1091-1100(1990).
RN [8]
RP PROTEIN SEQUENCE OF 35-57.
RX PubMed=2655583; DOI=10.1042/bj2590585;
RA Golds E.E., Mason P., Nyirkos P.;
RT "Inflammatory cytokines induce synthesis and secretion of gro protein and a
RT neutrophil chemotactic factor but not beta 2-microglobulin in human
RT synovial cells and fibroblasts.";
RL Biochem. J. 259:585-588(1989).
RN [9]
RP PROTEIN SEQUENCE OF 35-51.
RC TISSUE=Skin;
RX PubMed=1755384; DOI=10.1007/978-1-4684-6009-4_12;
RA Schroeder J.-M.;
RT "Biochemical and biological characterization of NAP-1/IL-8-related
RT cytokines in lesional psoriatic scale.";
RL Adv. Exp. Med. Biol. 305:97-107(1991).
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 POSSIBLE FUNCTION.
RX PubMed=2670560; DOI=10.1002/j.1460-2075.1989.tb03569.x;
RA Wen D., Rowland A., Derynck R.;
RT "Expression and secretion of gro/MGSA by stimulated human endothelial
RT cells.";
RL EMBO J. 8:1761-1766(1989).
RN [12]
RP STRUCTURE BY NMR.
RX PubMed=8397104; DOI=10.1016/0014-5793(93)80893-y;
RA Fairbrother W.J., Reilly D., Colby T., Horuk R.;
RT "1H assignment and secondary structure determination of human melanoma
RT growth stimulating activity (MGSA) by NMR spectroscopy.";
RL FEBS Lett. 330:302-306(1993).
RN [13]
RP STRUCTURE BY NMR.
RX PubMed=8089846; DOI=10.1006/jmbi.1994.1577;
RA Fairbrother W.J., Reilly D., Colby T., Hesselgesser J., Horuk R.;
RT "The solution structure of melanoma growth stimulating activity.";
RL J. Mol. Biol. 242:252-270(1994).
RN [14]
RP STRUCTURE BY NMR.
RX PubMed=7806518; DOI=10.1016/s0021-9258(20)30077-6;
RA Kim K.S., Clark-Lewis I., Sykes B.D.;
RT "Solution structure of GRO/melanoma growth stimulatory activity determined
RT by 1H NMR spectroscopy.";
RL J. Biol. Chem. 269:32909-32915(1994).
CC -!- FUNCTION: Has chemotactic activity for neutrophils. May play a role in
CC inflammation and exerts its effects on endothelial cells in an
CC autocrine fashion. In vitro, the processed forms GRO-alpha(4-73), GRO-
CC alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic
CC activity. {ECO:0000269|PubMed:10095777}.
CC -!- INTERACTION:
CC P09341; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2806484, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: N-terminal processed forms GRO-alpha(4-73), GRO-alpha(5-73) and
CC GRO-alpha(6-73) are produced by proteolytic cleavage after secretion
CC from peripheral blood monocytes. {ECO:0000269|PubMed:10095777}.
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXCL1 entry;
CC URL="https://en.wikipedia.org/wiki/CXCL1";
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DR EMBL; J03561; AAA35933.1; -; mRNA.
DR EMBL; X12510; CAA31027.1; -; mRNA.
DR EMBL; X54489; CAA38361.1; -; Genomic_DNA.
DR EMBL; BT006880; AAP35526.1; -; mRNA.
DR EMBL; BC011976; AAH11976.1; -; mRNA.
DR CCDS; CCDS47074.1; -.
DR PIR; S13669; A28414.
DR RefSeq; NP_001502.1; NM_001511.3.
DR PDB; 1MGS; NMR; -; A/B=35-107.
DR PDB; 1MSG; NMR; -; A/B=35-106.
DR PDB; 1MSH; NMR; -; A/B=35-106.
DR PDB; 1ROD; NMR; -; A/B=40-62, A/B=89-107.
DR PDBsum; 1MGS; -.
DR PDBsum; 1MSG; -.
DR PDBsum; 1MSH; -.
DR PDBsum; 1ROD; -.
DR AlphaFoldDB; P09341; -.
DR SMR; P09341; -.
DR BioGRID; 109176; 24.
DR DIP; DIP-5896N; -.
DR IntAct; P09341; 10.
DR MINT; P09341; -.
DR STRING; 9606.ENSP00000379110; -.
DR PhosphoSitePlus; P09341; -.
DR SwissPalm; P09341; -.
DR BioMuta; CXCL1; -.
DR DMDM; 121622; -.
DR EPD; P09341; -.
DR MassIVE; P09341; -.
DR MaxQB; P09341; -.
DR PaxDb; P09341; -.
DR PeptideAtlas; P09341; -.
DR PRIDE; P09341; -.
DR ProteomicsDB; 52214; -.
DR ABCD; P09341; 3 sequenced antibodies.
DR Antibodypedia; 6268; 755 antibodies from 39 providers.
DR DNASU; 2919; -.
DR Ensembl; ENST00000395761.4; ENSP00000379110.3; ENSG00000163739.5.
DR GeneID; 2919; -.
DR KEGG; hsa:2919; -.
DR MANE-Select; ENST00000395761.4; ENSP00000379110.3; NM_001511.4; NP_001502.1.
DR UCSC; uc003hhh.4; human.
DR CTD; 2919; -.
DR DisGeNET; 2919; -.
DR GeneCards; CXCL1; -.
DR HGNC; HGNC:4602; CXCL1.
DR HPA; ENSG00000163739; Tissue enhanced (cervix, lymphoid tissue).
DR MIM; 155730; gene.
DR neXtProt; NX_P09341; -.
DR OpenTargets; ENSG00000163739; -.
DR PharmGKB; PA35050; -.
DR VEuPathDB; HostDB:ENSG00000163739; -.
DR eggNOG; ENOG502S7MM; Eukaryota.
DR GeneTree; ENSGT00940000164504; -.
DR HOGENOM; CLU_143902_1_1_1; -.
DR InParanoid; P09341; -.
DR OMA; EKMLNCD; -.
DR OrthoDB; 1618797at2759; -.
DR PhylomeDB; P09341; -.
DR TreeFam; TF333433; -.
DR PathwayCommons; P09341; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P09341; -.
DR SIGNOR; P09341; -.
DR BioGRID-ORCS; 2919; 12 hits in 1006 CRISPR screens.
DR ChiTaRS; CXCL1; human.
DR EvolutionaryTrace; P09341; -.
DR GeneWiki; CXCL1; -.
DR GenomeRNAi; 2919; -.
DR Pharos; P09341; Tbio.
DR PRO; PR:P09341; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; P09341; protein.
DR Bgee; ENSG00000163739; Expressed in olfactory segment of nasal mucosa and 156 other tissues.
DR Genevisible; P09341; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0035580; C:specific 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:0008047; F:enzyme activator activity; TAS:ProtInc.
DR GO; GO:0008083; F:growth factor activity; TAS:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
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:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
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; Cytokine; Direct protein sequencing; Disulfide bond;
KW Growth factor; Inflammatory response; Reference proteome; Secreted; Signal.
FT SIGNAL 1..34
FT /evidence="ECO:0000269|PubMed:10095777,
FT ECO:0000269|PubMed:15340161, ECO:0000269|PubMed:1755384,
FT ECO:0000269|PubMed:2182761, ECO:0000269|PubMed:2655583"
FT CHAIN 35..107
FT /note="Growth-regulated alpha protein"
FT /id="PRO_0000005049"
FT CHAIN 38..107
FT /note="GRO-alpha(4-73)"
FT /id="PRO_0000005050"
FT CHAIN 39..107
FT /note="GRO-alpha(5-73)"
FT /id="PRO_0000005051"
FT CHAIN 40..107
FT /note="GRO-alpha(6-73)"
FT /id="PRO_0000005052"
FT DISULFID 43..69
FT DISULFID 45..85
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1MSG"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:1MSG"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1MGS"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1MGS"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1MGS"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1MGS"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:1MGS"
SQ SEQUENCE 107 AA; 11301 MW; 17048A6B4D765CA2 CRC64;
MARAALSAAP SNPRLLRVAL LLLLLVAAGR RAAGASVATE LRCQCLQTLQ GIHPKNIQSV
NVKSPGPHCA QTEVIATLKN GRKACLNPAS PIVKKIIEKM LNSDKSN
