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UniProtKB/Swiss-Prot entry P20701


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ITAL_HUMAN
Primary accession number P20701
Secondary accession numbers O43746 Q45H73 Q9UBC8
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on February 7, 2006 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 109)
Name and origin of the protein
Protein name Integrin alpha-L [Precursor]
Synonyms Leukocyte adhesion glycoprotein LFA-1 alpha chain
LFA-1A
Leukocyte function-associated molecule 1 alpha chain
CD11 antigen-like family member A
CD11a antigen
Gene name
Name: ITGAL
Synonyms: CD11A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND VARIANT TRP-214.
DOI=10.1083/jcb.108.2.703; PubMed=2537322 [NCBI, ExPASy, EBI, Israel, Japan]
Larson R.S., Corbi A.L., Berman L., Springer T.;
"Primary structure of the leukocyte function-associated molecule-1 alpha subunit: an integrin with an embedded domain defining a protein superfamily.";
J. Cell Biol. 108:703-712(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2), AND VARIANT TRP-214.
DOI=10.1006/geno.1999.5927; PubMed=10493829 [NCBI, ExPASy, EBI, Israel, Japan]
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.;
"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q.";
Genomics 60:295-308(1999).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-144; TRP-214; LYS-746 AND THR-791.
NIEHS SNPs program;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
DOI=10.1073/pnas.90.11.5364; PubMed=8099450 [NCBI, ExPASy, EBI, Israel, Japan]
Shelley C.S., Farokhzad O.C., Arnaout M.A.;
"Identification of cell-specific and developmentally regulated nuclear factors that direct myeloid and lymphoid expression of the CD11a gene.";
Proc. Natl. Acad. Sci. U.S.A. 90:5364-5368(1993).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
PubMed=8103515 [NCBI, ExPASy, EBI, Israel, Japan]
Nueda A., Lopez-Cabrera M., Vara A., Corbi A.L.;
"Characterization of the CD11a (alpha L, LFA-1 alpha) integrin gene promoter.";
J. Biol. Chem. 268:19305-19311(1993).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
DOI=10.1073/pnas.90.9.4221; PubMed=8097887 [NCBI, ExPASy, EBI, Israel, Japan]
Cornwell R.D., Gollahon K.A., Hickstein D.D.;
"Description of the leukocyte function-associated antigen 1 (LFA-1 or CD11a) promoter.";
Proc. Natl. Acad. Sci. U.S.A. 90:4221-4225(1993).
[7]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 153-335, AND SEQUENCE REVISION TO 214.
DOI=10.1073/pnas.92.22.10277; PubMed=7479767 [NCBI, ExPASy, EBI, Israel, Japan]
Qu A., Leahy D.J.;
"Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin.";
Proc. Natl. Acad. Sci. U.S.A. 92:10277-10281(1995).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-335.
DOI=10.1016/S0969-2126(96)00100-1; PubMed=8805579 [NCBI, ExPASy, EBI, Israel, Japan]
Qu A., Leahy D.J.;
"The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin.";
Structure 4:931-942(1996).
[9]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 153-334.
DOI=10.1006/jmbi.1999.3047; PubMed=10493852 [NCBI, ExPASy, EBI, Israel, Japan]
Kallen J., Welzenbach K., Ramage P., Geyl D., Kriwacki R., Legge G., Cottens S., Weitz-Schmidt G., Hommel U.;
"Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a I-domain.";
J. Mol. Biol. 292:1-9(1999).
[10]
X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 155-331 IN COMPLEX WITH ICAM1.
DOI=10.1016/S0092-8674(02)01257-6; PubMed=12526797 [NCBI, ExPASy, EBI, Israel, Japan]
Shimaoka M., Xiao T., Liu J.H., Yang Y., Dong Y., Jun C.D., McCormack A., Zhang R., Joachimiak A., Takagi J., Wang J.H., Springer T.A.;
"Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation.";
Cell 112:99-111(2003).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y00796; CAA68747.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002310; AAC31672.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ131904; AAZ38713.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M95609; AAA16474.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Z22804; CAA80461.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M87662; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
IPI IPI00025380; -.
IPI00219896; -.
PIR S03308; S03308.
RefSeq NP_002200.2; -.
UniGene Hs.174103
3D structure databases
PDB
1CQP; X-ray; 2.60 A; A/B=153-334.[ExPASy / RCSB / EBI]
1DGQ; NMR; -; A=152-336.[ExPASy / RCSB / EBI]
1IJ4; Model; -; L=153-333.[ExPASy / RCSB / EBI]
1LFA; X-ray; 1.80 A; A/B=150-336.[ExPASy / RCSB / EBI]
1MJN; X-ray; 1.30 A; A=153-331.[ExPASy / RCSB / EBI]
1MQ8; X-ray; 3.30 A; B/D=155-331.[ExPASy / RCSB / EBI]
1MQ9; X-ray; 2.00 A; A=153-331.[ExPASy / RCSB / EBI]
1MQA; X-ray; 2.50 A; A=153-331.[ExPASy / RCSB / EBI]
1RD4; X-ray; 2.40 A; A/B/C/D=150-336.[ExPASy / RCSB / EBI]
1T0P; X-ray; 1.66 A; A=153-326.[ExPASy / RCSB / EBI]
1XDD; X-ray; 2.20 A; A/B=152-336.[ExPASy / RCSB / EBI]
1XDG; X-ray; 2.10 A; A/B=152-336.[ExPASy / RCSB / EBI]
1XUO; X-ray; 1.80 A; A/B=152-336.[ExPASy / RCSB / EBI]
1ZON; X-ray; 2.00 A; A=150-336.[ExPASy / RCSB / EBI]
1ZOO; X-ray; 3.00 A; A/B=150-336.[ExPASy / RCSB / EBI]
1ZOP; X-ray; 2.00 A; A/B=150-336.[ExPASy / RCSB / EBI]
2ICA; X-ray; 1.56 A; A=154-332.[ExPASy / RCSB / EBI]
2K8O; NMR; -; A=1113-1170.[ExPASy / RCSB / EBI]
2O7N; X-ray; 1.75 A; A=154-332.[ExPASy / RCSB / EBI]
3BN3; X-ray; 2.10 A; A=154-332.[ExPASy / RCSB / EBI]
3BQM; X-ray; 1.95 A; B/C=153-334.[ExPASy / RCSB / EBI]
3BQN; X-ray; 1.80 A; B/C=153-334.[ExPASy / RCSB / EBI]
3E2M; X-ray; 2.00 A; A/B=152-334.[ExPASy / RCSB / EBI]
3EOA; X-ray; 2.80 A; I/J=153-333.[ExPASy / RCSB / EBI]
3EOB; X-ray; 3.60 A; I/J=153-333.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CQP; -.
1DGQ; -.
1IJ4; -.
1LFA; -.
1MJN; -.
1MQ8; -.
1MQ9; -.
1MQA; -.
1RD4; -.
1T0P; -.
1XDD; -.
1XDG; -.
1XUO; -.
1ZON; -.
1ZOO; -.
1ZOP; -.
2ICA; -.
2K8O; -.
2O7N; -.
3BN3; -.
3BQM; -.
3BQN; -.
3E2M; -.
3EOA; -.
3EOB; -.
ModBase P20701.
Protein-protein interaction databases
IntAct P20701; 4.
PTM databases
PhosphoSite P20701; -.
Enzyme and pathway databases
Pathway_Interaction_DB a4b1_paxdep_pathway; Paxillin-dependent events mediated by a4b1.
Reactome REACT_13552; Integrin cell surface interactions.
REACT_604; Hemostasis.
REACT_6900; Signaling in Immune system.
Organism-specific databases
GeneCards GC16P030391; -.
HGNC HGNC:6148; ITGAL.
GenAtlas ITGAL.
MIM 153370; gene. [NCBI / EBI]
PharmGKB PA29948; -.
Gene expression databases
ArrayExpress P20701; -.
Bgee P20701; -.
CleanEx HS_ITGAL; -.
GermOnline ENSG00000005844; Homo sapiens.
Ontologies
GO
GO:0008305; Cellular component: integrin complex (non-traceable author statement from UniProtKB).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0050839; Molecular function: cell adhesion molecule binding (inferred from physical interaction from UniProtKB).
GO:0000287; Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004872; Molecular function: receptor activity (inferred from electronic annotation from UniProtKB-KW).
GO:0006928; Biological process: cell motion (traceable author statement from ProtInc).
GO:0007157; Biological process: heterophilic cell adhesion (inferred from mutant phenotype from UniProtKB).
GO:0006954; Biological process: inflammatory response (non-traceable author statement from UniProtKB).
GO:0007229; Biological process: integrin-mediated signaling pathway (inferred from electronic annotation from UniProtKB-KW).
GO:0007159; Biological process: leukocyte adhesion (inferred from mutant phenotype from UniProtKB).
GO:0002291; Biological process: T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR013517; FG-GAP.
IPR013519; Int_alpha_beta-p.
IPR000413; Integrin_alpha.
IPR013649; Integrin_alpha-2.
IPR013513; Integrin_alpha_C.
IPR018184; Integrin_alpha_C_CS.
IPR002035; VWF_A.
Graphical view of domain structure.
Pfam PF01839; FG-GAP; 2.
PF00357; Integrin_alpha; 1.
PF08441; Integrin_alpha2; 1.
PF00092; VWA; 1.
Pfam graphical view of domain structure.
PRINTS PR01185; INTEGRINA.
SMART SM00191; Int_alpha; 5.
SM00327; VWA; 1.
SMART graphical view of domain structure.
PROSITE PS00242; INTEGRIN_ALPHA; 1.
PS50234; VWFA; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P20701; -.
Genome annotation databases
Ensembl ENSG00000005844; Homo sapiens. [Contig view]
GeneID 3683; -.
Phylogenomic databases
HOGENOM P20701; -.
HOVERGEN P20701; -.
OMA P20701; LSFRKVE.
Other
DrugBank DB00095; Efalizumab.
NextBio 14415; -.
SOURCE ITGAL; Homo sapiens.
ProtoNet P20701.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Calcium; Cell adhesion; Direct protein sequencing; Disulfide bond; Glycoprotein; Integrin; Magnesium; Membrane; Polymorphism; Receptor; Repeat; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
SIGNAL   1     25  25      
CHAIN   26   1170  1145     Integrin alpha-L. PRO_0000016292
TOPO_DOM   26   1090  1065     Extracellular (Potential). 
TRANSMEM   1091   1111  21     Potential. 
TOPO_DOM   1112   1170  59     Cytoplasmic (Potential). 
REPEAT   42     91  50     FG-GAP 1. 
REPEAT   92    149  58     FG-GAP 2. 
DOMAIN   156    327  172     VWFA. 
REPEAT   350    400  51     FG-GAP 3. 
REPEAT   401    455  55     FG-GAP 4. 
REPEAT   457    516  60     FG-GAP 5. 
REPEAT   518    575  58     FG-GAP 6. 
REPEAT   578    630  53     FG-GAP 7. 
CA_BIND   468    476  9     Potential. 
CA_BIND   530    538  9     Potential. 
CA_BIND   590    598  9     Potential. 
MOTIF   1115   1119  5     GFFKR motif. 
CARBOHYD   65     65        N-linked (GlcNAc...) (Potential). 
CARBOHYD   89     89        N-linked (GlcNAc...) (Potential). 
CARBOHYD   188    188        N-linked (GlcNAc...) (Potential). 
CARBOHYD   649    649        N-linked (GlcNAc...) (Potential). 
CARBOHYD   670    670        N-linked (GlcNAc...) (Potential). 
CARBOHYD   726    726        N-linked (GlcNAc...) (Potential). 
CARBOHYD   730    730        N-linked (GlcNAc...) (Potential). 
CARBOHYD   862    862        N-linked (GlcNAc...) (Potential). 
CARBOHYD   885    885        N-linked (GlcNAc...) (Potential). 
CARBOHYD   897    897        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1060   1060        N-linked (GlcNAc...) (Potential). 
CARBOHYD   1071   1071        N-linked (GlcNAc...) (Potential). 
DISULFID   73     80        By similarity. 
DISULFID   111    129        By similarity. 
DISULFID   653    707        By similarity. 
DISULFID   771    777        By similarity. 
DISULFID   845    861        By similarity. 
DISULFID   998   1013        By similarity. 
DISULFID   1021   1052        By similarity. 
VAR_SEQ   954    954        Q -> QGVHGLVEMQTSKQILCRPAGDAEHTVGAQEGELPCPWGV SEAFRDNIRAGPCR (in isoform 2). VSP_002738
VARIANT   144    144  1     R -> H (in dbSNP:rs34166708 [NCBI]). VAR_025235 
VARIANT   214    214  1     R -> W (in dbSNP:rs1064524 [NCBI]). VAR_025236 [3D]
VARIANT   746    746  1     Q -> K (in dbSNP:rs34838942 [NCBI]). VAR_025237 
VARIANT   791    791  1     R -> T (in dbSNP:rs2230433 [NCBI]). VAR_025238 
CONFLICT   660    660        I -> Y (in Ref. 1; CAA68747). 
STRAND   155    162  8      
HELIX   169    185  17      
TURN   186    188  3      
STRAND   189    206  18      
HELIX   208    213  6      
HELIX   217    221  5      
HELIX   233    243  11      
HELIX   247    249  3      
STRAND   255    265  11      
HELIX   274    276  3      
STRAND   279    287  9      
HELIX   288    290  3      
HELIX   293    297  5      
HELIX   298    302  5      
HELIX   307    310  4      
STRAND   311    317  7      
HELIX   319    328  10      
STRAND   331    333  3      
Sequence information
Length: 1170 AA [This is the length of the unprocessed precursor] Molecular weight: 128770 Da [This is the MW of the unprocessed precursor] CRC64: 22A7AF92EF286876 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKDSCITVMA MALLSGFFFF APASSYNLDV RGARSFSPPR AGRHFGYRVL QVGNGVIVGA 

        70         80         90        100        110        120 
PGEGNSTGSL YQCQSGTGHC LPVTLRGSNY TSKYLGMTLA TDPTDGSILA CDPGLSRTCD 

       130        140        150        160        170        180 
QNTYLSGLCY LFRQNLQGPM LQGRPGFQEC IKGNVDLVFL FDGSMSLQPD EFQKILDFMK 

       190        200        210        220        230        240 
DVMKKLSNTS YQFAAVQFST SYKTEFDFSD YVKRKDPDAL LKHVKHMLLL TNTFGAINYV 

       250        260        270        280        290        300 
ATEVFREELG ARPDATKVLI IITDGEATDS GNIDAAKDII RYIIGIGKHF QTKESQETLH 

       310        320        330        340        350        360 
KFASKPASEF VKILDTFEKL KDLFTELQKK IYVIEGTSKQ DLTSFNMELS SSGISADLSR 

       370        380        390        400        410        420 
GHAVVGAVGA KDWAGGFLDL KADLQDDTFI GNEPLTPEVR AGYLGYTVTW LPSRQKTSLL 

       430        440        450        460        470        480 
ASGAPRYQHM GRVLLFQEPQ GGGHWSQVQT IHGTQIGSYF GGELCGVDVD QDGETELLLI 

       490        500        510        520        530        540 
GAPLFYGEQR GGRVFIYQRR QLGFEEVSEL QGDPGYPLGR FGEAITALTD INGDGLVDVA 

       550        560        570        580        590        600 
VGAPLEEQGA VYIFNGRHGG LSPQPSQRIE GTQVLSGIQW FGRSIHGVKD LEGDGLADVA 

       610        620        630        640        650        660 
VGAESQMIVL SSRPVVDMVT LMSFSPAEIP VHEVECSYST SNKMKEGVNI TICFQIKSLI 

       670        680        690        700        710        720 
PQFQGRLVAN LTYTLQLDGH RTRRRGLFPG GRHELRRNIA VTTSMSCTDF SFHFPVCVQD 

       730        740        750        760        770        780 
LISPINVSLN FSLWEEEGTP RDQRAQGKDI PPILRPSLHS ETWEIPFEKN CGEDKKCEAN 

       790        800        810        820        830        840 
LRVSFSPARS RALRLTAFAS LSVELSLSNL EEDAYWVQLD LHFPPGLSFR KVEMLKPHSQ 

       850        860        870        880        890        900 
IPVSCEELPE ESRLLSRALS CNVSSPIFKA GHSVALQMMF NTLVNSSWGD SVELHANVTC 

       910        920        930        940        950        960 
NNEDSDLLED NSATTIIPIL YPINILIQDQ EDSTLYVSFT PKGPKIHQVK HMYQVRIQPS 

       970        980        990       1000       1010       1020 
IHDHNIPTLE AVVGVPQPPS EGPITHQWSV QMEPPVPCHY EDLERLPDAA EPCLPGALFR 

      1030       1040       1050       1060       1070       1080 
CPVVFRQEIL VQVIGTLELV GEIEASSMFS LCSSLSISFN SSKHFHLYGS NASLAQVVMK 

      1090       1100       1110       1120       1130       1140 
VDVVYEKQML YLYVLSGIGG LLLLLLIFIV LYKVGFFKRN LKEKMEAGRG VPNGIPAEDS 

      1150       1160       1170 
EQLASGQEAG DPGCLKPLHE KDSESGGGKD 

P20701 in FASTA format

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