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P25024 (CXCR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | 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:
C-X-C chemokine receptor type 1

Short name=CXC-R1
Short name=CXCR-1
Alternative name(s):
CDw128a
High affinity interleukin-8 receptor A
Short name=IL-8R A
IL-8 receptor type 1
CD_antigen=CD181
Gene names
Name:CXCR1
Synonyms:CMKAR1, IL8RA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length350 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor to interleukin-8, which is a powerful neutrophils chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activate a phosphatidylinositol-calcium second messenger system. This receptor binds to IL-8 with a high affinity and to MGSA (GRO) with a low affinity.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 8381837. Source: ProtInc

cell surface receptor signaling pathway

Inferred from direct assay PubMed 10734056. Source: UniProtKB

chemokine-mediated signaling pathway

Traceable author statement Ref.1. Source: GOC

chemotaxis

Traceable author statement PubMed 10725748. Source: ProtInc

dendritic cell chemotaxis

Traceable author statement PubMed 16621978. Source: BHF-UCL

inflammatory response

Traceable author statement PubMed 10725748. Source: ProtInc

interleukin-8-mediated signaling pathway

Inferred from direct assay PubMed 10734056. Source: GOC

receptor internalization

Inferred from direct assay PubMed 10734056. Source: UniProtKB

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Traceable author statement PubMed 10725748. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionG-protein coupled receptor activity

Traceable author statement PubMed 8381837. Source: ProtInc

chemokine receptor activity

Traceable author statement Ref.1. Source: ProtInc

interleukin-8 binding

Inferred from physical interaction PubMed 11564821. Source: UniProtKB

interleukin-8 receptor activity

Inferred from direct assay PubMed 10734056. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 350350C-X-C chemokine receptor type 1
PRO_0000069330

Regions

Topological domain1 – 3939Extracellular Potential
Transmembrane40 – 6627Helical; Name=1; Potential
Topological domain67 – 759Cytoplasmic Potential
Transmembrane76 – 9621Helical; Name=2; Potential
Topological domain97 – 11115Extracellular Potential
Transmembrane112 – 13322Helical; Name=3; Potential
Topological domain134 – 15421Cytoplasmic Potential
Transmembrane155 – 17420Helical; Name=4; Potential
Topological domain175 – 19925Extracellular Potential
Transmembrane200 – 22021Helical; Name=5; Potential
Topological domain221 – 24222Cytoplasmic Potential
Transmembrane243 – 26422Helical; Name=6; Potential
Topological domain265 – 28521Extracellular Potential
Transmembrane286 – 30823Helical; Name=7; Potential
Topological domain309 – 35042Cytoplasmic Potential

Amino acid modifications

Glycosylation31N-linked (GlcNAc...) Potential
Glycosylation161N-linked (GlcNAc...) Potential
Disulfide bond110 ↔ 187 By similarity

Natural variations

Natural variant311M → R. Ref.5 Ref.8 Ref.11
Corresponds to variant rs16858811 [ dbSNP | Ensembl ].
VAR_021061
Natural variant711R → C.
Corresponds to variant rs1805038 [ dbSNP | Ensembl ].
VAR_016236
Natural variant2681M → L.
Corresponds to variant rs9282752 [ dbSNP | Ensembl ].
VAR_026525
Natural variant2761S → T Common polymorphism. Ref.1 Ref.5 Ref.8 Ref.12
Corresponds to variant rs2234671 [ dbSNP | Ensembl ].
VAR_003479
Natural variant3061A → T. Ref.12
VAR_016237
Natural variant3351R → C. Ref.5 Ref.8 Ref.11 Ref.12
Corresponds to variant rs16858808 [ dbSNP | Ensembl ].
VAR_016238
Natural variant3421S → L. Ref.8
Corresponds to variant rs16858806 [ dbSNP | Ensembl ].
VAR_021062

Experimental info

Sequence conflict1541K → N in AAH72397. Ref.11

Secondary structure

.................................... 350
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25024 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: 2463E868C0EB0DE2

FASTA35039,791
        10         20         30         40         50         60 
MSNITDPQMW DFDDLNFTGM PPADEDYSPC MLETETLNKY VVIIAYALVF LLSLLGNSLV 

        70         80         90        100        110        120 
MLVILYSRVG RSVTDVYLLN LALADLLFAL TLPIWAASKV NGWIFGTFLC KVVSLLKEVN 

       130        140        150        160        170        180 
FYSGILLLAC ISVDRYLAIV HATRTLTQKR HLVKFVCLGC WGLSMNLSLP FFLFRQAYHP 

       190        200        210        220        230        240 
NNSSPVCYEV LGNDTAKWRM VLRILPHTFG FIVPLFVMLF CYGFTLRTLF KAHMGQKHRA 

       250        260        270        280        290        300 
MRVIFAVVLI FLLCWLPYNL VLLADTLMRT QVIQESCERR NNIGRALDAT EILGFLHSCL 

       310        320        330        340        350 
NPIIYAFIGQ NFRHGFLKIL AMHGLVSKEF LARHRVTSYT SSSVNVSSNL 

« Hide

References

« Hide 'large scale' references
[1]"Structure and functional expression of a human interleukin-8 receptor."
Holmes W.E., Lee J., Kuang W.-J., Rice G.C., Wood W.I.
Science 253:1278-1280(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANT THR-276.
[2]"Molecular characterization of receptors for human interleukin-8, GRO/melanoma growth-stimulatory activity and neutrophil activating peptide-2."
Cerretti D.P., Kozlosky C.J., Vanden Bos T., Nelson N., Gearing D.P., Beckmann M.P.
Mol. Immunol. 30:359-367(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]"The high-affinity interleukin 8 receptor gene (IL8RA) maps to the 2q33-q36 region of the human genome: cloning of a pseudogene (IL8RBP) for the low-affinity receptor."
Mollereau C., Passage E., Mattei M.-G., Vassart G., Parmentier M.
Genomics 16:248-251(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Comparison of the genomic organization and promoter function for human interleukin-8 receptors A and B."
Ahuja S.K., Shetty A., Tiffany H.L., Murphy P.M.
J. Biol. Chem. 269:26381-26389(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[5]"Molecular evolution of CXCR1, a G protein-coupled receptor involved in signal transduction of neutrophils."
Liu Y., Yang S., Lin A.A., Cavalli-Sforza L.L., Su B.
J. Mol. Evol. 61:691-696(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-31; THR-276 AND CYS-335.
[6]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]SeattleSNPs variation discovery resource
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-31; THR-276; CYS-335 AND LEU-342.
[9]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]"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], VARIANTS ARG-31 AND CYS-335.
Tissue: Blood.
[12]"Single nucleotide polymorphisms in the coding regions of human CXC-chemokine receptors CXCR1, CXCR2 and CXCR3."
Kato H., Tsuchiya N., Tokunaga K.
Genes Immun. 1:330-337(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 223-350, VARIANTS THR-276; THR-306 AND CYS-335.
[13]"Characterization of two high affinity human interleukin-8 receptors."
Lee J., Horuk R., Rice G.C., Bennett G.L., Camerato T., Wood W.I.
J. Biol. Chem. 267:16283-16287(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[14]"Structure of a CXC chemokine-receptor fragment in complex with interleukin-8."
Skelton N.J., Quan C., Reilly D., Lowman H.
Structure 7:157-168(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 9-29 IN COMPLEX WITH IL-8.
+Additional computationally mapped references.

Web resources

Wikipedia

CXC chemokine receptors entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19591 mRNA. Translation: AAB59436.1.
L19592 Genomic DNA. Translation: AAA59160.1.
M68932 mRNA. Translation: AAA59159.1.
X65858 Genomic DNA. Translation: CAA46688.1.
U11870 Genomic DNA. Translation: AAA64378.1.
AY916762 Genomic DNA. Translation: AAY21512.1.
AY916763 Genomic DNA. Translation: AAY21513.1.
AY916764 Genomic DNA. Translation: AAY21514.1.
AY916765 Genomic DNA. Translation: AAY21515.1.
AY916766 Genomic DNA. Translation: AAY21516.1.
AY916769 Genomic DNA. Translation: AAY21519.1.
AY916772 Genomic DNA. Translation: AAY21522.1.
AY916773 Genomic DNA. Translation: AAY21523.1.
CR541994 mRNA. Translation: CAG46791.1.
CR542029 mRNA. Translation: CAG46826.1.
AK312668 mRNA. Translation: BAG35550.1.
AY651785 Genomic DNA. Translation: AAT46689.1.
AC097483 Genomic DNA. Translation: AAX93212.1.
CH471063 Genomic DNA. Translation: EAW70590.1.
BC028221 mRNA. Translation: AAH28221.1.
BC072397 mRNA. Translation: AAH72397.1.
AB032728 Genomic DNA. Translation: BAA92290.1.
AB032729 Genomic DNA. Translation: BAA92291.1.
AB032730 Genomic DNA. Translation: BAA92292.1.
AB032731 Genomic DNA. Translation: BAA92293.1.
AB032732 Genomic DNA. Translation: BAA92294.1.
PIRA39445. I37449.
RefSeqNP_000625.1. NM_000634.2.
UniGeneHs.194778.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ILPNMR-C9-29[»]
1ILQNMR-C9-29[»]
2LNLNMR-A29-324[»]
ProteinModelPortalP25024.
SMRP25024. Positions 29-324.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109791. 5 interactions.
DIPDIP-3779N.
IntActP25024. 4 interactions.
MINTMINT-1516942.

Chemistry

BindingDBP25024.
ChEMBLCHEMBL4029.
GuidetoPHARMACOLOGY68.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP25024.

Polymorphism databases

DMDM108936015.

Proteomic databases

PaxDbP25024.
PRIDEP25024.

Protocols and materials databases

DNASU3577.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295683; ENSP00000295683; ENSG00000163464.
GeneID3577.
KEGGhsa:3577.
UCSCuc002vhc.3. human.

Organism-specific databases

CTD3577.
GeneCardsGC02M219028.
H-InvDBHIX0203926.
HGNCHGNC:6026. CXCR1.
HPAHPA031991.
MIM146929. gene.
neXtProtNX_P25024.
PharmGKBPA29842.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146068.
HOVERGENHBG106917.
InParanoidP25024.
KOK04175.
OMAPVCYEVL.
OrthoDBEOG7ZPNK9.
PhylomeDBP25024.
TreeFamTF330966.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP25024.
GenevestigatorP25024.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR001355. Chemokine_CXCR1.
IPR000174. Chemokine_CXCR_1/2.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24227. PTHR24227. 1 hit.
PTHR24227:SF47. PTHR24227:SF47. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00427. INTRLEUKIN8R.
PR00572. INTRLEUKN8AR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP25024.
GeneWikiInterleukin_8_receptor,_alpha.
GenomeRNAi3577.
NextBio13982.
PROP25024.
SOURCESearch...

Entry information

Entry nameCXCR1_HUMAN
AccessionPrimary (citable) accession number: P25024
Secondary accession number(s): B2R6Q3 expand/collapse secondary AC list , Q2YEF8, Q2YEG4, Q2YEG5, Q2YEG7, Q2YEG8, Q53R18, Q6IN95, Q8N6T6, Q9P2T8, Q9P2T9, Q9P2U0, Q9P2U1, Q9P2U2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 30, 2006
Last modified: April 16, 2014
This is version 148 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries