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Protein

Integrin alpha-L

Gene

ITGAL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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: UniProtKB
  2. ICAM-3 receptor activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. activated T cell proliferation Source: Ensembl
  2. blood coagulation Source: Reactome
  3. cell adhesion Source: UniProtKB
  4. cell-matrix adhesion Source: UniProtKB
  5. extracellular matrix organization Source: Reactome
  6. heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules 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. movement of cell or subcellular component Source: ProtInc
  12. positive regulation of calcium-mediated signaling Source: Ensembl
  13. positive regulation of T cell proliferation Source: Ensembl
  14. receptor clustering Source: UniProtKB
  15. regulation of immune response Source: Reactome
  16. signal transduction Source: UniProtKB
  17. T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Source: BHF-UCL
Complete GO annotation...

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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:6148. ITGAL.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 10901065ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1091 – 111121HelicalSequence AnalysisAdd
BLAST
Topological domaini1112 – 117059CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cell surface Source: UniProtKB
  3. external side of plasma membrane Source: Ensembl
  4. extracellular vesicular exosome Source: UniProtKB
  5. immunological synapse Source: Ensembl
  6. integrin alphaL-beta2 complex Source: UniProtKB
  7. integrin complex Source: UniProtKB
  8. membrane Source: UniProtKB
  9. plasma membrane Source: Reactome
Complete GO annotation...

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

BgeeiP20701.
CleanExiHS_ITGAL.
ExpressionAtlasiP20701. baseline and differential.
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. 7 interactions.
DIPiDIP-623N.
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 – 1628Combined sources
Helixi169 – 18517Combined sources
Turni186 – 1883Combined sources
Beta strandi189 – 20618Combined sources
Helixi208 – 2147Combined sources
Helixi217 – 2215Combined sources
Helixi233 – 24311Combined sources
Helixi247 – 2493Combined sources
Beta strandi255 – 26511Combined sources
Helixi274 – 2763Combined sources
Beta strandi279 – 2879Combined sources
Helixi288 – 2903Combined sources
Helixi293 – 2975Combined sources
Helixi298 – 3025Combined sources
Helixi307 – 3104Combined sources
Beta strandi311 – 3166Combined sources
Helixi317 – 3193Combined sources
Helixi323 – 3308Combined sources
Beta strandi331 – 3333Combined sources
Turni1082 – 10865Combined sources
Helixi1090 – 111425Combined sources
Helixi1118 – 11236Combined sources
Turni1124 – 11274Combined sources
Helixi1137 – 114711Combined sources
Helixi1153 – 11553Combined sources
Helixi1156 – 116510Combined sources
Helixi1167 – 11704Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.

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.
GeneTreeiENSGT00760000118782.
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. AlignAdd to basket

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

        10         20         30         40         50
MKDSCITVMA MALLSGFFFF APASSYNLDV RGARSFSPPR AGRHFGYRVL
60 70 80 90 100
QVGNGVIVGA PGEGNSTGSL YQCQSGTGHC LPVTLRGSNY TSKYLGMTLA
110 120 130 140 150
TDPTDGSILA CDPGLSRTCD QNTYLSGLCY LFRQNLQGPM LQGRPGFQEC
160 170 180 190 200
IKGNVDLVFL FDGSMSLQPD EFQKILDFMK DVMKKLSNTS YQFAAVQFST
210 220 230 240 250
SYKTEFDFSD YVKRKDPDAL LKHVKHMLLL TNTFGAINYV ATEVFREELG
260 270 280 290 300
ARPDATKVLI IITDGEATDS GNIDAAKDII RYIIGIGKHF QTKESQETLH
310 320 330 340 350
KFASKPASEF VKILDTFEKL KDLFTELQKK IYVIEGTSKQ DLTSFNMELS
360 370 380 390 400
SSGISADLSR GHAVVGAVGA KDWAGGFLDL KADLQDDTFI GNEPLTPEVR
410 420 430 440 450
AGYLGYTVTW LPSRQKTSLL ASGAPRYQHM GRVLLFQEPQ GGGHWSQVQT
460 470 480 490 500
IHGTQIGSYF GGELCGVDVD QDGETELLLI GAPLFYGEQR GGRVFIYQRR
510 520 530 540 550
QLGFEEVSEL QGDPGYPLGR FGEAITALTD INGDGLVDVA VGAPLEEQGA
560 570 580 590 600
VYIFNGRHGG LSPQPSQRIE GTQVLSGIQW FGRSIHGVKD LEGDGLADVA
610 620 630 640 650
VGAESQMIVL SSRPVVDMVT LMSFSPAEIP VHEVECSYST SNKMKEGVNI
660 670 680 690 700
TICFQIKSLI PQFQGRLVAN LTYTLQLDGH RTRRRGLFPG GRHELRRNIA
710 720 730 740 750
VTTSMSCTDF SFHFPVCVQD LISPINVSLN FSLWEEEGTP RDQRAQGKDI
760 770 780 790 800
PPILRPSLHS ETWEIPFEKN CGEDKKCEAN LRVSFSPARS RALRLTAFAS
810 820 830 840 850
LSVELSLSNL EEDAYWVQLD LHFPPGLSFR KVEMLKPHSQ IPVSCEELPE
860 870 880 890 900
ESRLLSRALS CNVSSPIFKA GHSVALQMMF NTLVNSSWGD SVELHANVTC
910 920 930 940 950
NNEDSDLLED NSATTIIPIL YPINILIQDQ EDSTLYVSFT PKGPKIHQVK
960 970 980 990 1000
HMYQVRIQPS IHDHNIPTLE AVVGVPQPPS EGPITHQWSV QMEPPVPCHY
1010 1020 1030 1040 1050
EDLERLPDAA EPCLPGALFR CPVVFRQEIL VQVIGTLELV GEIEASSMFS
1060 1070 1080 1090 1100
LCSSLSISFN SSKHFHLYGS NASLAQVVMK VDVVYEKQML YLYVLSGIGG
1110 1120 1130 1140 1150
LLLLLLIFIV LYKVGFFKRN LKEKMEAGRG VPNGIPAEDS EQLASGQEAG
1160 1170
DPGCLKPLHE KDSESGGGKD
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi109889. 7 interactions.
DIPiDIP-623N.
IntActiP20701. 7 interactions.
MINTiMINT-1130696.
STRINGi9606.ENSP00000349252.

Chemistry

BindingDBiP20701.
ChEMBLiCHEMBL2096661.
DrugBankiDB00098. Antithymocyte globulin.
DB00095. Efalizumab.
DB00227. Lovastatin.

PTM databases

PhosphoSiteiP20701.

Polymorphism databases

DMDMi88911345.

Proteomic databases

MaxQBiP20701.
PaxDbiP20701.
PRIDEiP20701.

Protocols and materials databases

DNASUi3683.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi3683.
GeneCardsiGC16P030483.
H-InvDBHIX0012960.
HIX0026987.
HGNCiHGNC:6148. ITGAL.
HPAiCAB025011.
MIMi153370. gene.
neXtProtiNX_P20701.
PharmGKBiPA29948.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG296688.
GeneTreeiENSGT00760000118782.
HOGENOMiHOG000113114.
HOVERGENiHBG006188.
InParanoidiP20701.
KOiK05718.
OMAiGEDKKCE.
OrthoDBiEOG74XS5V.
PhylomeDBiP20701.
TreeFamiTF105391.

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.

Miscellaneous databases

ChiTaRSiITGAL. human.
EvolutionaryTraceiP20701.
GeneWikiiCD11a.
GenomeRNAii3683.
NextBioi14415.
PROiP20701.
SOURCEiSearch...

Gene expression databases

BgeeiP20701.
CleanExiHS_ITGAL.
ExpressionAtlasiP20701. baseline and differential.
GenevestigatoriP20701.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT TRP-214.
  2. NIEHS SNPs program
    Submitted (JUN-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(2003) [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(2003) [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(1992) [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(1992) [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(1992) [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(2008) [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(1994) [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(1995) [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(1998) [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(2002) [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: March 4, 2015
This is version 169 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.