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   02-SEP-2026, entry version 229.
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_001511.4.
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   PDB; 8K4O; EM; 3.01 A; F=35-97.
DR   PDB; 8XWA; EM; 3.48 A; D/E=35-107.
DR   PDB; 8XWV; EM; 3.07 A; D/E=35-102.
DR   PDB; 9EJC; EM; 2.98 A; F=35-107.
DR   AlphaFoldDB; P09341; -.
DR   EMDB; EMD-36888; -.
DR   EMDB; EMD-38732; -.
DR   EMDB; EMD-38743; -.
DR   EMDB; EMD-43718; -.
DR   EMDB; EMD-48100; -.
DR   SMR; P09341; -.
DR   BioGRID; 109176; 24.
DR   DIP; DIP-5896N; -.
DR   FunCoup; P09341; 1029.
DR   IntAct; P09341; 21.
DR   MINT; P09341; -.
DR   NDEx; IQUERY-CP-CXCL1; 16 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000379110; -.
DR   PhosphoSitePlus; P09341; -.
DR   SwissPalm; P09341; -.
DR   BioMuta; CXCL1; -.
DR   DMDM; 121622; -.
DR   jPOST; P09341; -.
DR   MassIVE; P09341; -.
DR   PaxDb; 9606-ENSP00000379110; -.
DR   PeptideAtlas; P09341; -.
DR   ProteomicsDB; 52214; -.
DR   ABCD; P09341; 3 sequenced antibodies.
DR   Antibodypedia; 6268; 785 antibodies from 42 providers.
DR   DNASU; 2919; -.
DR   Ensembl; ENST00000395761.4; ENSP00000379110.3; ENSG00000163739.6.
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   AGR; HGNC:4602; -.
DR   ClinPGx; PA35050; -.
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   OpenTargets; ENSG00000163739; -.
DR   VEuPathDB; HostDB:ENSG00000163739; -.
DR   eggNOG; ENOG502S7MM; Eukaryota.
DR   GeneTree; ENSGT00940000164504; -.
DR   HOGENOM; CLU_143902_1_1_1; -.
DR   InParanoid; P09341; -.
DR   OMA; NTELRCR; -.
DR   OrthoDB; 8872899at2759; -.
DR   PAN-GO; P09341; 0 GO annotations based on evolutionary models.
DR   PhylomeDB; P09341; -.
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   Agora; ENSG00000163739; -.
DR   BioGRID-ORCS; 2919; 15 hits in 1093 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 157 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
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; TAS:ProtInc.
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:0006935; P:chemotaxis; TAS:ProtInc.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR   GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
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:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd00273; Chemokine_CXC; 1.
DR   FunFam; 2.40.50.40:FF:000004; C-X-C motif chemokine; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   InterPro; IPR039809; Chemokine_b/g/d.
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; PTHR12015:SF192; GROWTH-REGULATED ALPHA PROTEIN; 1.
DR   PANTHER; PTHR12015; SMALL INDUCIBLE CYTOKINE A; 1.
DR   Pfam; PF00048; IL8; 1.
DR   PRINTS; PR00436; INTERLEUKIN8.
DR   PRINTS; PR00437; SMALLCYTKCXC.
DR   SMART; SM00199; SCY; 1.
DR   SUPFAM; SSF54117; Interleukin 8-like chemokines; 1.
DR   PROSITE; PS00471; SMALL_CYTOKINES_CXC; 1.
DR   PDBsum; 1MGS; -.
DR   PDBsum; 1MSG; -.
DR   PDBsum; 1MSH; -.
DR   PDBsum; 1ROD; -.
DR   PDBsum; 8K4O; -.
DR   PDBsum; 8XWA; -.
DR   PDBsum; 8XWV; -.
DR   PDBsum; 9EJC; -.
PE   1: Evidence at protein level;
KW   3D-structure; Cytokine; Direct protein sequencing; Disulfide bond;
KW   Growth factor; Inflammatory response; Proteomics identification;
KW   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   HELIX           36..38
FT                   /evidence="ECO:0007829|PDB:9EJC"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:1MSG"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:8K4O"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:1MSG"
FT   TURN            54..56
FT                   /evidence="ECO:0007829|PDB:9EJC"
FT   STRAND          58..62
FT                   /evidence="ECO:0007829|PDB:8K4O"
FT   STRAND          66..68
FT                   /evidence="ECO:0007829|PDB:8K4O"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:8XWV"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:9EJC"
FT   TURN            79..81
FT                   /evidence="ECO:0007829|PDB:1ROD"
FT   STRAND          83..86
FT                   /evidence="ECO:0007829|PDB:9EJC"
FT   STRAND          88..90
FT                   /evidence="ECO:0007829|PDB:9EJC"
FT   HELIX           93..105
FT                   /evidence="ECO:0007829|PDB:9EJC"
SQ   SEQUENCE   107 AA;  11301 MW;  17048A6B4D765CA2 CRC64;
     MARAALSAAP SNPRLLRVAL LLLLLVAAGR RAAGASVATE LRCQCLQTLQ GIHPKNIQSV
     NVKSPGPHCA QTEVIATLKN GRKACLNPAS PIVKKIIEKM LNSDKSN
//