Reviewed, UniProtKB/Swiss-Prot P09341 (GROA_HUMAN)

Names and origin

Protein names

Recommended name:
    Growth-regulated alpha protein
Alternative name(s):
    C-X-C motif chemokine 1
    Melanoma growth stimulatory activity
      Short name=MGSA
    Neutrophil-activating protein 3
      Short name=NAP-3
    GRO-alpha(1-73)
Cleaved into the following 3 chains:
    1- Recommended name:
            GRO-alpha(4-73)
    2- Recommended name:
            GRO-alpha(5-73)
    3- Recommended name:
            GRO-alpha(6-73)

Gene names

Name:	CXCL1
Synonyms:	GRO, GRO1, GROA, MGSA, SCYB1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	107 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Inflammatory response
Cellular component	Secreted
Domain	Signal
Molecular function	Cytokine Growth factor
PTM	Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	G-protein coupled receptor protein signaling pathway Inferred from Experiment. Source: Reactome actin cytoskeleton organization Traceable author statement. Source: ProtInc cell proliferation Traceable author statement. Source: ProtInc chemotaxis Traceable author statement. Source: ProtInc immune response Inferred from electronic annotation. Source: InterPro inflammatory response Traceable author statement. Source: ProtInc intracellular signaling cascade Traceable author statement. Source: ProtInc negative regulation of cell proliferation Traceable author statement. Source: ProtInc nervous system development Traceable author statement. Source: ProtInc
Cellular component	extracellular space Traceable author statement. Source: ProtInc
Molecular function	chemokine activity Traceable author statement. Source: ProtInc enzyme activator activity Traceable author statement. Source: ProtInc growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 34

34

Ref.6 Ref.7 Ref.8 Ref.9 Ref.10

Chain

35 – 107

73

Growth-regulated alpha protein

PRO_0000005049

Chain

38 – 107

70

GRO-alpha(4-73)

PRO_0000005050

Chain

39 – 107

69

GRO-alpha(5-73)

PRO_0000005051

Chain

40 – 107

68

GRO-alpha(6-73)

PRO_0000005052

Amino acid modifications

Disulfide bond

43 ↔ 69

Disulfide bond

45 ↔ 85

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

107

Helix Strand Turn

Details...

Turn

54 – 56

3

Beta strand

57 – 63

7

Beta strand

73 – 78

6

Beta strand

83 – 86

4

Helix

91 – 103

13

Sequences

	Sequence		Length	Mass (Da)
	P09341-1 [UniParc]. Last modified July 1, 1989. Version 1. Checksum: 17048A6B4D765CA2	FASTA	107	11,301
	10 20 30 40 50 60 MARAALSAAP SNPRLLRVAL LLLLLVAAGR RAAGASVATE LRCQCLQTLQ GIHPKNIQSV 70 80 90 100 NVKSPGPHCA QTEVIATLKN GRKACLNPAS PIVKKIIEKM LNSDKSN

References

	« Hide 'large scale' referencesShow '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: 2890161] [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: 2970963] [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: 2129556] [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: 15489334] [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: 10095777] [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: 2182761] [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: 2655583] [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: 1755384] [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: 15340161] [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: 2670560] [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: 8397104] [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: 8089846] [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: 7806518] [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.

IPI

IPI00013874.

PIR

A28414. S13669.

RefSeq

NP_001502.1.

UniGene

Hs.789

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MGS	NMR	-	A/B	35-107	[»]
1MSG	NMR	-	A/B	35-106	[»]
1MSH	NMR	-	A/B	35-106	[»]
1ROD	NMR	-	A/B	66-107	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5896N.

STRING

P09341.

Proteomic databases

PRIDE

P09341.

Genome annotation databases

Ensembl

ENST00000395761; ENSP00000379110; ENSG00000163739; Homo sapiens. [Genome view]

GeneID

2919.

KEGG

hsa:2919.

UCSC

uc003hhh.1. human.

Organism-specific databases

CTD

2919.

GeneCards

GC04P074974.

H-InvDB

HIX0004283.

HGNC

HGNC:4602. CXCL1.

MIM

155730. gene.

PharmGKB

PA35050.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG21283.

HOGENOM

HBG444970.

HOVERGEN

P09341.

InParanoid

P09341.

OMA

HFKNIQS.

OrthoDB

EOG9RBT3V.

Enzyme and pathway databases

Pathway_Interaction_DB

il23pathway. IL23-mediated signaling events.

Reactome

REACT_14797. Signaling by GPCR.

Gene expression databases

ArrayExpress

P09341.

Bgee

P09341.

CleanEx

HS_CXCL1.

Genevestigator

P09341.

Family and domain databases

InterPro

IPR002473. C-X-C/Interlkn_8.
IPR001811. Chemokine_IL8.
IPR001089. CXC_chmkine_smll.
IPR018048. Small_chemokine_CXC_CS.
[Graphical view]

Pfam

PF00048. IL8. 1 hit.
[Graphical view]

PRINTS

PR00436. INTERLEUKIN8.
PR00437. SMALLCYTKCXC.

SMART

SM00199. SCY. 1 hit.
[Graphical view]

PROSITE

PS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

11573.

PMAP-CutDB

P09341.

SOURCE

Search...

Entry information

Entry name

GROA_HUMAN

Accession

Primary (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:	February 9, 2010
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.