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P20701

- ITAL_HUMAN

UniProt

P20701 - ITAL_HUMAN

Protein

Integrin alpha-L

Gene

ITGAL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (07 Feb 2006)
      Previous versions | rss
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    Functioni

    Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. It is involved in a variety of immune phenomena including leukocyte-endothelial cell interaction, cytotoxic T-cell mediated killing, and antibody dependent killing by granulocytes and monocytes.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi468 – 4769Sequence Analysis
    Calcium bindingi530 – 5389Sequence Analysis
    Calcium bindingi590 – 5989Sequence Analysis

    GO - Molecular functioni

    1. cell adhesion molecule binding Source: BHF-UCL
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. activated T cell proliferation Source: Ensembl
    2. blood coagulation Source: Reactome
    3. cell adhesion Source: UniProtKB
    4. cellular component movement Source: ProtInc
    5. extracellular matrix organization Source: Reactome
    6. heterophilic cell-cell adhesion Source: BHF-UCL
    7. inflammatory response Source: UniProtKB
    8. integrin-mediated signaling pathway Source: UniProtKB-KW
    9. leukocyte cell-cell adhesion Source: BHF-UCL
    10. leukocyte migration Source: Reactome
    11. positive regulation of calcium-mediated signaling Source: Ensembl
    12. positive regulation of cell-cell adhesion Source: Ensembl
    13. positive regulation of T cell proliferation Source: Ensembl
    14. regulation of immune response Source: Reactome
    15. signal transduction Source: UniProtKB
    16. T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Source: BHF-UCL

    Keywords - Molecular functioni

    Integrin, Receptor

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_13552. Integrin cell surface interactions.
    SignaLinkiP20701.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Integrin alpha-L
    Alternative name(s):
    CD11 antigen-like family member A
    Leukocyte adhesion glycoprotein LFA-1 alpha chain
    Short name:
    LFA-1A
    Leukocyte function-associated molecule 1 alpha chain
    CD_antigen: CD11a
    Gene namesi
    Name:ITGAL
    Synonyms:CD11A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:6148. ITGAL.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. external side of plasma membrane Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. immunological synapse Source: Ensembl
    5. integrin complex Source: UniProtKB
    6. membrane Source: UniProtKB
    7. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29948.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2525Add
    BLAST
    Chaini26 – 11701145Integrin alpha-LPRO_0000016292Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi65 – 651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi73 ↔ 80By similarity
    Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi111 ↔ 129By similarity
    Glycosylationi188 – 1881N-linked (GlcNAc...)1 Publication
    Glycosylationi649 – 6491N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi653 ↔ 707By similarity
    Glycosylationi670 – 6701N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi726 – 7261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi730 – 7301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi771 ↔ 777By similarity
    Disulfide bondi845 ↔ 861By similarity
    Glycosylationi862 – 8621N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi885 – 8851N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi897 – 8971N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi998 ↔ 1013By similarity
    Disulfide bondi1021 ↔ 1052By similarity
    Glycosylationi1060 – 10601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1071 – 10711N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP20701.
    PaxDbiP20701.
    PRIDEiP20701.

    PTM databases

    PhosphoSiteiP20701.

    Expressioni

    Tissue specificityi

    Leukocytes.

    Gene expression databases

    ArrayExpressiP20701.
    BgeeiP20701.
    CleanExiHS_ITGAL.
    GenevestigatoriP20701.

    Organism-specific databases

    HPAiCAB025011.

    Interactioni

    Subunit structurei

    Heterodimer of an alpha and a beta subunit. Alpha-L associates with beta-2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q9WMX22EBI-961214,EBI-6863748From a different organism.
    PTPRCP085752EBI-961214,EBI-1341

    Protein-protein interaction databases

    BioGridi109889. 6 interactions.
    IntActiP20701. 7 interactions.
    MINTiMINT-1130696.
    STRINGi9606.ENSP00000349252.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi155 – 1628
    Helixi169 – 18517
    Turni186 – 1883
    Beta strandi189 – 20618
    Helixi208 – 2147
    Helixi217 – 2215
    Helixi233 – 24311
    Helixi247 – 2493
    Beta strandi255 – 26511
    Helixi274 – 2763
    Beta strandi279 – 2879
    Helixi288 – 2903
    Helixi293 – 2975
    Helixi298 – 3025
    Helixi307 – 3104
    Beta strandi311 – 3166
    Helixi317 – 3193
    Helixi323 – 3308
    Beta strandi331 – 3333
    Turni1082 – 10865
    Helixi1090 – 111425
    Helixi1118 – 11236
    Turni1124 – 11274
    Helixi1137 – 114711
    Helixi1153 – 11553
    Helixi1156 – 116510
    Helixi1167 – 11704

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CQPX-ray2.60A/B153-334[»]
    1DGQNMR-A152-336[»]
    1IJ4model-L153-333[»]
    1LFAX-ray1.80A/B150-336[»]
    1MJNX-ray1.30A153-331[»]
    1MQ8X-ray3.30B/D155-331[»]
    1MQ9X-ray2.00A153-331[»]
    1MQAX-ray2.50A153-331[»]
    1RD4X-ray2.40A/B/C/D150-336[»]
    1T0PX-ray1.66A153-326[»]
    1XDDX-ray2.20A/B152-336[»]
    1XDGX-ray2.10A/B152-336[»]
    1XUOX-ray1.80A/B152-336[»]
    1ZONX-ray2.00A150-336[»]
    1ZOOX-ray3.00A/B150-336[»]
    1ZOPX-ray2.00A/B150-336[»]
    2ICAX-ray1.56A154-332[»]
    2K8ONMR-A1113-1170[»]
    2M3ENMR-A1082-1128[»]
    2O7NX-ray1.75A154-332[»]
    3BN3X-ray2.10A154-332[»]
    3BQMX-ray1.95B/C153-334[»]
    3BQNX-ray1.80B/C153-334[»]
    3E2MX-ray2.00A/B152-334[»]
    3EOAX-ray2.80I/J153-333[»]
    3EOBX-ray3.60I/J153-333[»]
    3F74X-ray1.70A/B/C153-332[»]
    3F78X-ray1.60A/B/C153-332[»]
    3HI6X-ray2.30A/B153-332[»]
    3M6FX-ray1.85A154-332[»]
    3TCXX-ray3.60B/D/F/H/J/L/N/P/R/T/V/X/Z/b154-332[»]
    4IXDX-ray1.80A152-336[»]
    ProteinModelPortaliP20701.
    SMRiP20701. Positions 26-1072, 1082-1170.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20701.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini26 – 10901065ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1112 – 117059CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1091 – 111121HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati31 – 8252FG-GAP 1Add
    BLAST
    Repeati83 – 14159FG-GAP 2Add
    BLAST
    Domaini156 – 327172VWFAPROSITE-ProRule annotationAdd
    BLAST
    Repeati338 – 38952FG-GAP 3Add
    BLAST
    Repeati390 – 44556FG-GAP 4Add
    BLAST
    Repeati446 – 50661FG-GAP 5Add
    BLAST
    Repeati507 – 56357FG-GAP 6Add
    BLAST
    Repeati567 – 62761FG-GAP 7Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1115 – 11195GFFKR motif

    Domaini

    The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage.

    Sequence similaritiesi

    Belongs to the integrin alpha chain family.Curated
    Contains 7 FG-GAP repeats.Curated
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG296688.
    HOGENOMiHOG000113114.
    HOVERGENiHBG006188.
    InParanoidiP20701.
    KOiK05718.
    OMAiGEDKKCE.
    OrthoDBiEOG74XS5V.
    PhylomeDBiP20701.
    TreeFamiTF105391.

    Family and domain databases

    InterProiIPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF01839. FG-GAP. 1 hit.
    PF00357. Integrin_alpha. 1 hit.
    PF08441. Integrin_alpha2. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view]
    PRINTSiPR01185. INTEGRINA.
    SMARTiSM00191. Int_alpha. 5 hits.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    PROSITEiPS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P20701-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKDSCITVMA MALLSGFFFF APASSYNLDV RGARSFSPPR AGRHFGYRVL     50
    QVGNGVIVGA PGEGNSTGSL YQCQSGTGHC LPVTLRGSNY TSKYLGMTLA 100
    TDPTDGSILA CDPGLSRTCD QNTYLSGLCY LFRQNLQGPM LQGRPGFQEC 150
    IKGNVDLVFL FDGSMSLQPD EFQKILDFMK DVMKKLSNTS YQFAAVQFST 200
    SYKTEFDFSD YVKRKDPDAL LKHVKHMLLL TNTFGAINYV ATEVFREELG 250
    ARPDATKVLI IITDGEATDS GNIDAAKDII RYIIGIGKHF QTKESQETLH 300
    KFASKPASEF VKILDTFEKL KDLFTELQKK IYVIEGTSKQ DLTSFNMELS 350
    SSGISADLSR GHAVVGAVGA KDWAGGFLDL KADLQDDTFI GNEPLTPEVR 400
    AGYLGYTVTW LPSRQKTSLL ASGAPRYQHM GRVLLFQEPQ GGGHWSQVQT 450
    IHGTQIGSYF GGELCGVDVD QDGETELLLI GAPLFYGEQR GGRVFIYQRR 500
    QLGFEEVSEL QGDPGYPLGR FGEAITALTD INGDGLVDVA VGAPLEEQGA 550
    VYIFNGRHGG LSPQPSQRIE GTQVLSGIQW FGRSIHGVKD LEGDGLADVA 600
    VGAESQMIVL SSRPVVDMVT LMSFSPAEIP VHEVECSYST SNKMKEGVNI 650
    TICFQIKSLI PQFQGRLVAN LTYTLQLDGH RTRRRGLFPG GRHELRRNIA 700
    VTTSMSCTDF SFHFPVCVQD LISPINVSLN FSLWEEEGTP RDQRAQGKDI 750
    PPILRPSLHS ETWEIPFEKN CGEDKKCEAN LRVSFSPARS RALRLTAFAS 800
    LSVELSLSNL EEDAYWVQLD LHFPPGLSFR KVEMLKPHSQ IPVSCEELPE 850
    ESRLLSRALS CNVSSPIFKA GHSVALQMMF NTLVNSSWGD SVELHANVTC 900
    NNEDSDLLED NSATTIIPIL YPINILIQDQ EDSTLYVSFT PKGPKIHQVK 950
    HMYQVRIQPS IHDHNIPTLE AVVGVPQPPS EGPITHQWSV QMEPPVPCHY 1000
    EDLERLPDAA EPCLPGALFR CPVVFRQEIL VQVIGTLELV GEIEASSMFS 1050
    LCSSLSISFN SSKHFHLYGS NASLAQVVMK VDVVYEKQML YLYVLSGIGG 1100
    LLLLLLIFIV LYKVGFFKRN LKEKMEAGRG VPNGIPAEDS EQLASGQEAG 1150
    DPGCLKPLHE KDSESGGGKD 1170
    Length:1,170
    Mass (Da):128,770
    Last modified:February 7, 2006 - v3
    Checksum:i22A7AF92EF286876
    GO
    Isoform 2 (identifier: P20701-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         954-954: Q → QGVHGLVEMQTSKQILCRPAGDAEHTVGAQEGELPCPWGVSEAFRDNIRAGPCR

    Note: No experimental confirmation available.

    Show »
    Length:1,223
    Mass (Da):134,427
    Checksum:iAF2302FAC076924D
    GO
    Isoform 3 (identifier: P20701-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         110-192: Missing.
         746-746: Missing.

    Show »
    Length:1,086
    Mass (Da):119,224
    Checksum:iF6FF2546E8C632F9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti660 – 6601I → Y in CAA68747. (PubMed:2537322)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti144 – 1441R → H.1 Publication
    Corresponds to variant rs34166708 [ dbSNP | Ensembl ].
    VAR_025235
    Natural varianti214 – 2141R → W.3 Publications
    Corresponds to variant rs1064524 [ dbSNP | Ensembl ].
    VAR_025236
    Natural varianti746 – 7461Q → K.1 Publication
    Corresponds to variant rs34838942 [ dbSNP | Ensembl ].
    VAR_025237
    Natural varianti791 – 7911R → T.1 Publication
    Corresponds to variant rs2230433 [ dbSNP | Ensembl ].
    VAR_025238

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei110 – 19283Missing in isoform 3. 1 PublicationVSP_042842Add
    BLAST
    Alternative sequencei746 – 7461Missing in isoform 3. 1 PublicationVSP_042843
    Alternative sequencei954 – 9541Q → QGVHGLVEMQTSKQILCRPA GDAEHTVGAQEGELPCPWGV SEAFRDNIRAGPCR in isoform 2. CuratedVSP_002738

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00796 mRNA. Translation: CAA68747.1.
    DQ131904 Genomic DNA. Translation: AAZ38713.1.
    AC002310 Genomic DNA. Translation: AAC31672.1.
    AC116348 Genomic DNA. No translation available.
    CH471192 Genomic DNA. Translation: EAW52243.1.
    BC008777 mRNA. Translation: AAH08777.1.
    M95609 Genomic DNA. Translation: AAA16474.2.
    Z22804 Genomic DNA. Translation: CAA80461.1.
    M87662 Genomic DNA. No translation available.
    CCDSiCCDS32433.1. [P20701-1]
    CCDS45461.1. [P20701-3]
    PIRiS03308.
    RefSeqiNP_001107852.1. NM_001114380.1. [P20701-3]
    NP_002200.2. NM_002209.2. [P20701-1]
    UniGeneiHs.174103.

    Genome annotation databases

    EnsembliENST00000356798; ENSP00000349252; ENSG00000005844. [P20701-1]
    ENST00000358164; ENSP00000350886; ENSG00000005844. [P20701-3]
    GeneIDi3683.
    KEGGihsa:3683.
    UCSCiuc002dyi.4. human. [P20701-1]
    uc002dyj.4. human. [P20701-3]

    Polymorphism databases

    DMDMi88911345.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00796 mRNA. Translation: CAA68747.1 .
    DQ131904 Genomic DNA. Translation: AAZ38713.1 .
    AC002310 Genomic DNA. Translation: AAC31672.1 .
    AC116348 Genomic DNA. No translation available.
    CH471192 Genomic DNA. Translation: EAW52243.1 .
    BC008777 mRNA. Translation: AAH08777.1 .
    M95609 Genomic DNA. Translation: AAA16474.2 .
    Z22804 Genomic DNA. Translation: CAA80461.1 .
    M87662 Genomic DNA. No translation available.
    CCDSi CCDS32433.1. [P20701-1 ]
    CCDS45461.1. [P20701-3 ]
    PIRi S03308.
    RefSeqi NP_001107852.1. NM_001114380.1. [P20701-3 ]
    NP_002200.2. NM_002209.2. [P20701-1 ]
    UniGenei Hs.174103.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CQP X-ray 2.60 A/B 153-334 [» ]
    1DGQ NMR - A 152-336 [» ]
    1IJ4 model - L 153-333 [» ]
    1LFA X-ray 1.80 A/B 150-336 [» ]
    1MJN X-ray 1.30 A 153-331 [» ]
    1MQ8 X-ray 3.30 B/D 155-331 [» ]
    1MQ9 X-ray 2.00 A 153-331 [» ]
    1MQA X-ray 2.50 A 153-331 [» ]
    1RD4 X-ray 2.40 A/B/C/D 150-336 [» ]
    1T0P X-ray 1.66 A 153-326 [» ]
    1XDD X-ray 2.20 A/B 152-336 [» ]
    1XDG X-ray 2.10 A/B 152-336 [» ]
    1XUO X-ray 1.80 A/B 152-336 [» ]
    1ZON X-ray 2.00 A 150-336 [» ]
    1ZOO X-ray 3.00 A/B 150-336 [» ]
    1ZOP X-ray 2.00 A/B 150-336 [» ]
    2ICA X-ray 1.56 A 154-332 [» ]
    2K8O NMR - A 1113-1170 [» ]
    2M3E NMR - A 1082-1128 [» ]
    2O7N X-ray 1.75 A 154-332 [» ]
    3BN3 X-ray 2.10 A 154-332 [» ]
    3BQM X-ray 1.95 B/C 153-334 [» ]
    3BQN X-ray 1.80 B/C 153-334 [» ]
    3E2M X-ray 2.00 A/B 152-334 [» ]
    3EOA X-ray 2.80 I/J 153-333 [» ]
    3EOB X-ray 3.60 I/J 153-333 [» ]
    3F74 X-ray 1.70 A/B/C 153-332 [» ]
    3F78 X-ray 1.60 A/B/C 153-332 [» ]
    3HI6 X-ray 2.30 A/B 153-332 [» ]
    3M6F X-ray 1.85 A 154-332 [» ]
    3TCX X-ray 3.60 B/D/F/H/J/L/N/P/R/T/V/X/Z/b 154-332 [» ]
    4IXD X-ray 1.80 A 152-336 [» ]
    ProteinModelPortali P20701.
    SMRi P20701. Positions 26-1072, 1082-1170.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109889. 6 interactions.
    IntActi P20701. 7 interactions.
    MINTi MINT-1130696.
    STRINGi 9606.ENSP00000349252.

    Chemistry

    BindingDBi P20701.
    ChEMBLi CHEMBL2096661.
    DrugBanki DB00095. Efalizumab.

    PTM databases

    PhosphoSitei P20701.

    Polymorphism databases

    DMDMi 88911345.

    Proteomic databases

    MaxQBi P20701.
    PaxDbi P20701.
    PRIDEi P20701.

    Protocols and materials databases

    DNASUi 3683.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356798 ; ENSP00000349252 ; ENSG00000005844 . [P20701-1 ]
    ENST00000358164 ; ENSP00000350886 ; ENSG00000005844 . [P20701-3 ]
    GeneIDi 3683.
    KEGGi hsa:3683.
    UCSCi uc002dyi.4. human. [P20701-1 ]
    uc002dyj.4. human. [P20701-3 ]

    Organism-specific databases

    CTDi 3683.
    GeneCardsi GC16P030483.
    H-InvDB HIX0012960.
    HIX0026987.
    HGNCi HGNC:6148. ITGAL.
    HPAi CAB025011.
    MIMi 153370. gene.
    neXtProti NX_P20701.
    PharmGKBi PA29948.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296688.
    HOGENOMi HOG000113114.
    HOVERGENi HBG006188.
    InParanoidi P20701.
    KOi K05718.
    OMAi GEDKKCE.
    OrthoDBi EOG74XS5V.
    PhylomeDBi P20701.
    TreeFami TF105391.

    Enzyme and pathway databases

    Reactomei REACT_11152. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
    REACT_12051. Cell surface interactions at the vascular wall.
    REACT_13552. Integrin cell surface interactions.
    SignaLinki P20701.

    Miscellaneous databases

    EvolutionaryTracei P20701.
    GeneWikii CD11a.
    GenomeRNAii 3683.
    NextBioi 14415.
    PROi P20701.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20701.
    Bgeei P20701.
    CleanExi HS_ITGAL.
    Genevestigatori P20701.

    Family and domain databases

    InterProi IPR013517. FG-GAP.
    IPR013519. Int_alpha_beta-p.
    IPR000413. Integrin_alpha.
    IPR013649. Integrin_alpha-2.
    IPR018184. Integrin_alpha_C_CS.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF01839. FG-GAP. 1 hit.
    PF00357. Integrin_alpha. 1 hit.
    PF08441. Integrin_alpha2. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    PRINTSi PR01185. INTEGRINA.
    SMARTi SM00191. Int_alpha. 5 hits.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    PROSITEi PS51470. FG_GAP. 7 hits.
    PS00242. INTEGRIN_ALPHA. 1 hit.
    PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of the leukocyte function-associated molecule-1 alpha subunit: an integrin with an embedded domain defining a protein superfamily."
      Larson R.S., Corbi A.L., Berman L., Springer T.
      J. Cell Biol. 108:703-712(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT TRP-214.
    2. NIEHS SNPs program
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-144; TRP-214; LYS-746 AND THR-791.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2), VARIANT TRP-214.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 3).
      Tissue: Lymph.
    7. "Identification of cell-specific and developmentally regulated nuclear factors that direct myeloid and lymphoid expression of the CD11a gene."
      Shelley C.S., Farokhzad O.C., Arnaout M.A.
      Proc. Natl. Acad. Sci. U.S.A. 90:5364-5368(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
    8. "Characterization of the CD11a (alpha L, LFA-1 alpha) integrin gene promoter."
      Nueda A., Lopez-Cabrera M., Vara A., Corbi A.L.
      J. Biol. Chem. 268:19305-19311(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
    9. "Description of the leukocyte function-associated antigen 1 (LFA-1 or CD11a) promoter."
      Cornwell R.D., Gollahon K.A., Hickstein D.D.
      Proc. Natl. Acad. Sci. U.S.A. 90:4221-4225(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20.
    10. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-188.
      Tissue: Leukemic T-cell.
    11. "Crystal structure of the I-domain from the CD11a/CD18 (LFA-1, alpha L beta 2) integrin."
      Qu A., Leahy D.J.
      Proc. Natl. Acad. Sci. U.S.A. 92:10277-10281(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 153-335, SEQUENCE REVISION TO 214.
    12. "The role of the divalent cation in the structure of the I domain from the CD11a/CD18 integrin."
      Qu A., Leahy D.J.
      Structure 4:931-942(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-335.
    13. "Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a I-domain."
      Kallen J., Welzenbach K., Ramage P., Geyl D., Kriwacki R., Legge G., Cottens S., Weitz-Schmidt G., Hommel U.
      J. Mol. Biol. 292:1-9(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 153-334.
    14. "Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation."
      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.
      Cell 112:99-111(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 155-331 IN COMPLEX WITH ICAM1.

    Entry informationi

    Entry nameiITAL_HUMAN
    AccessioniPrimary (citable) accession number: P20701
    Secondary accession number(s): O43746
    , Q45H73, Q96HB1, Q9UBC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: February 7, 2006
    Last modified: October 1, 2014
    This is version 165 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3