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P09341 (GROA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Growth-regulated alpha protein
Alternative name(s):
C-X-C motif chemokine 1
GRO-alpha(1-73)
Melanoma growth stimulatory activity
Short name=MGSA
Neutrophil-activating protein 3
Short name=NAP-3

Cleaved into the following 3 chains:

  1. GRO-alpha(4-73)
  2. GRO-alpha(5-73)
  3. GRO-alpha(6-73)
Gene names
Name:CXCL1
Synonyms:GRO, GRO1, GROA, MGSA, SCYB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length107 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has chemotactic activity for neutrophils. May play a role in inflammation and exerts its effects on endothelial cells in an autocrine fashion. In vitro, the processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) show a 30-fold higher chemotactic activity. Ref.6 Ref.11

Subcellular location

Secreted.

Post-translational modification

N-terminal processed forms GRO-alpha(4-73), GRO-alpha(5-73) and GRO-alpha(6-73) are produced by proteolytic cleavage after secretion from peripheral blood monocytes.

Sequence similarities

Belongs to the intercrine alpha (chemokine CxC) family.

Ontologies

Keywords
   Biological processInflammatory response
   Cellular componentSecreted
   DomainSignal
   Molecular functionCytokine
Growth factor
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 10820279. Source: ProtInc

actin cytoskeleton organization

Traceable author statement PubMed 9725262. Source: ProtInc

cell chemotaxis

Traceable author statement PubMed 10820279. Source: GOC

cell proliferation

Traceable author statement PubMed 8380167. Source: ProtInc

chemotaxis

Traceable author statement PubMed 10820279. Source: ProtInc

immune response

Inferred from electronic annotation. Source: InterPro

inflammatory response

Traceable author statement PubMed 9725262. Source: ProtInc

intracellular signal transduction

Traceable author statement PubMed 9551928. Source: ProtInc

negative regulation of cell proliferation

Traceable author statement PubMed 9551928. Source: ProtInc

nervous system development

Traceable author statement PubMed 9058825. Source: ProtInc

positive regulation of catalytic activity

Traceable author statement PubMed 9079638. Source: GOC

signal transduction

Traceable author statement PubMed 10820279PubMed 9725262. Source: ProtInc

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement PubMed 10881932. Source: ProtInc

   Molecular_functionchemokine activity

Traceable author statement PubMed 10820279. Source: ProtInc

enzyme activator activity

Traceable author statement PubMed 9079638. Source: ProtInc

receptor binding

Traceable author statement PubMed 10820279PubMed 9079638. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3434 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Chain35 – 10773Growth-regulated alpha protein
PRO_0000005049
Chain38 – 10770GRO-alpha(4-73)
PRO_0000005050
Chain39 – 10769GRO-alpha(5-73)
PRO_0000005051
Chain40 – 10768GRO-alpha(6-73)
PRO_0000005052

Amino acid modifications

Disulfide bond43 ↔ 69
Disulfide bond45 ↔ 85

Secondary structure

.............. 107
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09341 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 17048A6B4D765CA2

FASTA10711,301
        10         20         30         40         50         60 
MARAALSAAP SNPRLLRVAL LLLLLVAAGR RAAGASVATE LRCQCLQTLQ GIHPKNIQSV 

        70         80         90        100 
NVKSPGPHCA QTEVIATLKN GRKACLNPAS PIVKKIIEKM LNSDKSN 

« Hide

References

« Hide 'large scale' references
[1]"Constitutive overexpression of a growth-regulated gene in transformed Chinese hamster and human cells."
Anisowicz A., Bardwell L., Sager R.
Proc. Natl. Acad. Sci. U.S.A. 84:7188-7192(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular characterization and chromosomal mapping of melanoma growth stimulatory activity, a growth factor structurally related to beta-thromboglobulin."
Richmond A., Balentien E., Thomas H.G., Flaggs G., Barton D.E., Spiess J., Bordoni R., Francke U., Derynck R.
EMBO J. 7:2025-2033(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Nucleotide sequence of the human melanoma growth stimulatory activity (MGSA) gene."
Baker N.E., Kucera G., Richmond A.
Nucleic Acids Res. 18:6453-6453(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Ovary.
[6]"Isolation of the CXC chemokines ENA-78, GRO alpha and GRO gamma from tumor cells and leukocytes reveals NH2-terminal heterogeneity. Functional comparison of different natural isoforms."
Wuyts A., Govaerts C., Struyf S., Lenaerts J.-P., Put W., Conings R., Proost P., Van Damme J.
Eur. J. Biochem. 260:421-429(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-107, IDENTIFICATION OF GRO-ALPHA(4-73); GRO-ALPHA(5-73) AND GRO-ALPHA(6-73), PROTEOLYTIC PROCESSING OF N-TERMINAL, FUNCTION.
Tissue: Peripheral blood monocyte.
[7]"Lipopolysaccharide-stimulated human monocytes secrete, apart from neutrophil-activating peptide 1/interleukin 8, a second neutrophil-activating protein. NH2-terminal amino acid sequence identity with melanoma growth stimulatory activity."
Schroeder J.-M., Persoon N.L.M., Christophers E.
J. Exp. Med. 171:1091-1100(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-65.
[8]"Inflammatory cytokines induce synthesis and secretion of gro protein and a neutrophil chemotactic factor but not beta 2-microglobulin in human synovial cells and fibroblasts."
Golds E.E., Mason P., Nyirkos P.
Biochem. J. 259:585-588(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-57.
[9]"Biochemical and biological characterization of NAP-1/IL-8-related cytokines in lesional psoriatic scale."
Schroeder J.-M.
Adv. Exp. Med. Biol. 305:97-107(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-51.
Tissue: Skin.
[10]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-49.
[11]"Expression and secretion of gro/MGSA by stimulated human endothelial cells."
Wen D., Rowland A., Derynck R.
EMBO J. 8:1761-1766(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE FUNCTION.
[12]"1H assignment and secondary structure determination of human melanoma growth stimulating activity (MGSA) by NMR spectroscopy."
Fairbrother W.J., Reilly D., Colby T., Horuk R.
FEBS Lett. 330:302-306(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[13]"The solution structure of melanoma growth stimulating activity."
Fairbrother W.J., Reilly D., Colby T., Hesselgesser J., Horuk R.
J. Mol. Biol. 242:252-270(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[14]"Solution structure of GRO/melanoma growth stimulatory activity determined by 1H NMR spectroscopy."
Kim K.S., Clark-Lewis I., Sykes B.D.
J. Biol. Chem. 269:32909-32915(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Web resources

Wikipedia

CXCL1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03561 mRNA. Translation: AAA35933.1.
X12510 mRNA. Translation: CAA31027.1.
X54489 Genomic DNA. Translation: CAA38361.1.
BT006880 mRNA. Translation: AAP35526.1.
BC011976 mRNA. Translation: AAH11976.1.
CCDSCCDS47074.1.
PIRA28414. S13669.
RefSeqNP_001502.1. NM_001511.3.
UniGeneHs.708652.
Hs.789.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MGSNMR-A/B35-107[»]
1MSGNMR-A/B35-106[»]
1MSHNMR-A/B35-106[»]
1RODNMR-A/B40-62[»]
A/B89-107[»]
ProteinModelPortalP09341.
SMRP09341. Positions 35-107.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109176. 3 interactions.
DIPDIP-5896N.
IntActP09341. 1 interaction.
STRING9606.ENSP00000379110.

PTM databases

PhosphoSiteP09341.

Polymorphism databases

DMDM121622.

Proteomic databases

MaxQBP09341.
PaxDbP09341.
PRIDEP09341.

Protocols and materials databases

DNASU2919.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395761; ENSP00000379110; ENSG00000163739.
GeneID2919.
KEGGhsa:2919.
UCSCuc003hhh.3. human.

Organism-specific databases

CTD2919.
GeneCardsGC04P074724.
H-InvDBHIX0120073.
HGNCHGNC:4602. CXCL1.
MIM155730. gene.
neXtProtNX_P09341.
PharmGKBPA35050.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG266004.
HOGENOMHOG000220915.
HOVERGENHBG107789.
InParanoidP09341.
KOK05505.
OrthoDBEOG7NSB57.
PhylomeDBP09341.
TreeFamTF333433.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP09341.
BgeeP09341.
CleanExHS_CXCL1.
GenevestigatorP09341.

Family and domain databases

InterProIPR001089. Chemokine_CXC.
IPR018048. Chemokine_CXC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PANTHERPTHR10179. PTHR10179. 1 hit.
PfamPF00048. IL8. 1 hit.
[Graphical view]
PRINTSPR00437. SMALLCYTKCXC.
SMARTSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMSSF54117. SSF54117. 1 hit.
PROSITEPS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCXCL1. human.
EvolutionaryTraceP09341.
GeneWikiCXCL1.
GenomeRNAi2919.
NextBio11573.
PMAP-CutDBP09341.
PROP09341.
SOURCESearch...

Entry information

Entry nameGROA_HUMAN
AccessionPrimary (citable) accession number: P09341
Secondary accession number(s): Q9UCR7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM