P20701 (ITAL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ITGAL
Synonyms:	CD11A

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1170 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	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.
Subunit structure	Heterodimer of an alpha and a beta subunit. Alpha-L associates with beta-2.
Subcellular location	Membrane; Single-pass type I membrane protein.
Tissue specificity	Leukocytes.
Domain	The integrin I-domain (insert) is a VWFA domain. Integrins with I-domains do not undergo protease cleavage.
Sequence similarities	Belongs to the integrin alpha chain family. Contains 7 FG-GAP repeats. Contains 1 VWFA domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal Transmembrane Transmembrane helix
Ligand	Calcium Magnesium Metal-binding
Molecular function	Integrin Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell Inferred from mutant phenotype PubMed 2477710. Source: BHF-UCL activated T cell proliferation Inferred from electronic annotation. Source: Compara blood coagulation Traceable author statement. Source: Reactome heterophilic cell-cell adhesion Inferred from mutant phenotype PubMed 2477710. Source: BHF-UCL inflammatory response Non-traceable author statement Ref.8. Source: UniProtKB integrin-mediated signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW leukocyte cell-cell adhesion Inferred from mutant phenotype PubMed 2477710. Source: BHF-UCL leukocyte migration Traceable author statement. Source: Reactome positive regulation of T cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of calcium-mediated signaling Inferred from electronic annotation. Source: Compara positive regulation of cell-cell adhesion Inferred from electronic annotation. Source: Compara regulation of immune response Traceable author statement. Source: Reactome signal transduction Non-traceable author statement Ref.8. Source: UniProtKB
Cellular_component	external side of plasma membrane Inferred from electronic annotation. Source: Compara immunological synapse Inferred from electronic annotation. Source: Compara integrin complex Non-traceable author statement Ref.8. Source: UniProtKB
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P20701-1)

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.

Isoform 2 (identifier: P20701-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: P20701-3)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Chain

26 – 1170

1145

Integrin alpha-L

PRO_0000016292

Regions

Topological domain

26 – 1090

1065

Extracellular Potential

Transmembrane

1091 – 1111

21

Helical; Potential

Topological domain

1112 – 1170

59

Cytoplasmic Potential

Repeat

31 – 82

52

FG-GAP 1

Repeat

83 – 141

59

FG-GAP 2

Domain

156 – 327

172

VWFA

Repeat

338 – 389

52

FG-GAP 3

Repeat

390 – 445

56

FG-GAP 4

Repeat

446 – 506

61

FG-GAP 5

Repeat

507 – 563

57

FG-GAP 6

Repeat

567 – 627

61

FG-GAP 7

Calcium binding

468 – 476

9

Potential

Calcium binding

530 – 538

9

Potential

Calcium binding

590 – 598

9

Potential

Motif

1115 – 1119

5

GFFKR motif

Amino acid modifications

Glycosylation

65

1

N-linked (GlcNAc...) Potential

Glycosylation

89

1

N-linked (GlcNAc...) Potential

Glycosylation

188

1

N-linked (GlcNAc...) Ref.10

Glycosylation

649

1

N-linked (GlcNAc...) Potential

Glycosylation

670

1

N-linked (GlcNAc...) Potential

Glycosylation

726

1

N-linked (GlcNAc...) Potential

Glycosylation

730

1

N-linked (GlcNAc...) Potential

Glycosylation

862

1

N-linked (GlcNAc...) Potential

Glycosylation

885

1

N-linked (GlcNAc...) Potential

Glycosylation

897

1

N-linked (GlcNAc...) Potential

Glycosylation

1060

1

N-linked (GlcNAc...) Potential

Glycosylation

1071

1

N-linked (GlcNAc...) Potential

Disulfide bond

73 ↔ 80

By similarity

Disulfide bond

111 ↔ 129

By similarity

Disulfide bond

653 ↔ 707

By similarity

Disulfide bond

771 ↔ 777

By similarity

Disulfide bond

845 ↔ 861

By similarity

Disulfide bond

998 ↔ 1013

By similarity

Disulfide bond

1021 ↔ 1052

By similarity

Natural variations

Alternative sequence

110 – 192

83

Missing in isoform 3.

VSP_042842

Alternative sequence

746

1

Missing in isoform 3.

VSP_042843

Alternative sequence

954

1

Q → QGVHGLVEMQTSKQILCRPA GDAEHTVGAQEGELPCPWGV SEAFRDNIRAGPCR in isoform 2.

VSP_002738

Natural variant

144

1

R → H. Ref.2
Corresponds to variant rs34166708 [ dbSNP | Ensembl ].

VAR_025235

Natural variant

214

1

R → W. Ref.1 Ref.2 Ref.3
Corresponds to variant rs1064524 [ dbSNP | Ensembl ].

VAR_025236

Natural variant

746

1

Q → K. Ref.2
Corresponds to variant rs34838942 [ dbSNP | Ensembl ].

VAR_025237

Natural variant

791

1

R → T. Ref.2
Corresponds to variant rs2230433 [ dbSNP | Ensembl ].

VAR_025238

Experimental info

Sequence conflict

660

1

I → Y in CAA68747. Ref.1

Secondary structure

1

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1170

Helix Strand Turn

Details...

Beta strand

155 – 162

8

Helix

169 – 185

17

Turn

186 – 188

3

Beta strand

189 – 206

18

Helix

208 – 214

7

Helix

217 – 221

5

Helix

233 – 243

11

Helix

247 – 249

3

Beta strand

255 – 265

11

Helix

274 – 276

3

Beta strand

279 – 287

9

Helix

288 – 290

3

Helix

293 – 297

5

Helix

298 – 302

5

Helix

307 – 310

4

Beta strand

311 – 316

6

Helix

317 – 319

3

Helix

323 – 330

8

Beta strand

331 – 333

3

Helix

1118 – 1123

6

Turn

1124 – 1127

4

Helix

1137 – 1147

11

Helix

1153 – 1155

3

Helix

1156 – 1165

10

Helix

1167 – 1170

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 7, 2006. Version 3. Checksum: 22A7AF92EF286876	FASTA	1,170	128,770
	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
	Isoform 2 [UniParc]. Checksum: AF2302FAC076924D	FASTA	1,223	134,427
	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 HMYQGVHGLV 970 980 990 1000 1010 1020 EMQTSKQILC RPAGDAEHTV GAQEGELPCP WGVSEAFRDN IRAGPCRVRI QPSIHDHNIP 1030 1040 1050 1060 1070 1080 TLEAVVGVPQ PPSEGPITHQ WSVQMEPPVP CHYEDLERLP DAAEPCLPGA LFRCPVVFRQ 1090 1100 1110 1120 1130 1140 EILVQVIGTL ELVGEIEASS MFSLCSSLSI SFNSSKHFHL YGSNASLAQV VMKVDVVYEK 1150 1160 1170 1180 1190 1200 QMLYLYVLSG IGGLLLLLLI FIVLYKVGFF KRNLKEKMEA GRGVPNGIPA EDSEQLASGQ 1210 1220 EAGDPGCLKP LHEKDSESGG GKD
	Isoform 3 [UniParc]. Checksum: F6FF2546E8C632F9	FASTA	1,086	119,224
	10 20 30 40 50 60 MKDSCITVMA MALLSGFFFF APASSYNLDV RGARSFSPPR AGRHFGYRVL QVGNGVIVGA 70 80 90 100 110 120 PGEGNSTGSL YQCQSGTGHC LPVTLRGSNY TSKYLGMTLA TDPTDGSILF AAVQFSTSYK 130 140 150 160 170 180 TEFDFSDYVK RKDPDALLKH VKHMLLLTNT FGAINYVATE VFREELGARP DATKVLIIIT 190 200 210 220 230 240 DGEATDSGNI DAAKDIIRYI IGIGKHFQTK ESQETLHKFA SKPASEFVKI LDTFEKLKDL 250 260 270 280 290 300 FTELQKKIYV IEGTSKQDLT SFNMELSSSG ISADLSRGHA VVGAVGAKDW AGGFLDLKAD 310 320 330 340 350 360 LQDDTFIGNE PLTPEVRAGY LGYTVTWLPS RQKTSLLASG APRYQHMGRV LLFQEPQGGG 370 380 390 400 410 420 HWSQVQTIHG TQIGSYFGGE LCGVDVDQDG ETELLLIGAP LFYGEQRGGR VFIYQRRQLG 430 440 450 460 470 480 FEEVSELQGD PGYPLGRFGE AITALTDING DGLVDVAVGA PLEEQGAVYI FNGRHGGLSP 490 500 510 520 530 540 QPSQRIEGTQ VLSGIQWFGR SIHGVKDLEG DGLADVAVGA ESQMIVLSSR PVVDMVTLMS 550 560 570 580 590 600 FSPAEIPVHE VECSYSTSNK MKEGVNITIC FQIKSLIPQF QGRLVANLTY TLQLDGHRTR 610 620 630 640 650 660 RRGLFPGGRH ELRRNIAVTT SMSCTDFSFH FPVCVQDLIS PINVSLNFSL WEEEGTPRDQ 670 680 690 700 710 720 RAGKDIPPIL RPSLHSETWE IPFEKNCGED KKCEANLRVS FSPARSRALR LTAFASLSVE 730 740 750 760 770 780 LSLSNLEEDA YWVQLDLHFP PGLSFRKVEM LKPHSQIPVS CEELPEESRL LSRALSCNVS 790 800 810 820 830 840 SPIFKAGHSV ALQMMFNTLV NSSWGDSVEL HANVTCNNED SDLLEDNSAT TIIPILYPIN 850 860 870 880 890 900 ILIQDQEDST LYVSFTPKGP KIHQVKHMYQ VRIQPSIHDH NIPTLEAVVG VPQPPSEGPI 910 920 930 940 950 960 THQWSVQMEP PVPCHYEDLE RLPDAAEPCL PGALFRCPVV FRQEILVQVI GTLELVGEIE 970 980 990 1000 1010 1020 ASSMFSLCSS LSISFNSSKH FHLYGSNASL AQVVMKVDVV YEKQMLYLYV LSGIGGLLLL 1030 1040 1050 1060 1070 1080 LLIFIVLYKV GFFKRNLKEK MEAGRGVPNG IPAEDSEQLA SGQEAGDPGC LKPLHEKDSE SGGGKD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q." 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. Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract] 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]	Mural R.J., Istrail S., Sutton 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. , 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].
[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, MASS SPECTROMETRY. 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.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00025380.
IPI00219896.

PIR

S03308.

RefSeq

NP_001107852.1. NM_001114380.1.
NP_002200.2. NM_002209.2.

UniGene

Hs.174103.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
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	[»]

ProteinModelPortal

P20701.

ModBase

Search...

Protein-protein interaction databases

IntAct

P20701. 5 interactions.

MINT

MINT-1130696.

STRING

9606.ENSP00000349252.

PTM databases

PhosphoSite

P20701.

Polymorphism databases

DMDM

88911345.

Proteomic databases

PaxDb

P20701.

PRIDE

P20701.

Protocols and materials databases

DNASU

3683.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356798; ENSP00000349252; ENSG00000005844.
ENST00000358164; ENSP00000350886; ENSG00000005844.

GeneID

3683.

KEGG

hsa:3683.

UCSC

uc002dyi.4. human.
uc002dyj.4. human.

Organism-specific databases

CTD

3683.

GeneCards

GC16P030483.

H-InvDB

HIX0012960.
HIX0026987.

HGNC

HGNC:6148. ITGAL.

HPA

CAB025011.

MIM

153370. gene.

neXtProt

NX_P20701.

PharmGKB

PA29948.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG296688.

HOGENOM

HOG000113114.

HOVERGEN

HBG006188.

InParanoid

P20701.

KO

K05718.

OMA

GEDKKCE.

Enzyme and pathway databases

Pathway_Interaction_DB

a4b1_paxdep_pathway. Paxillin-dependent events mediated by a4b1.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SignaLink

P20701.

Gene expression databases

ArrayExpress

P20701.

Bgee

P20701.

CleanEx

HS_ITGAL.

Genevestigator

P20701.

GermOnline

ENSG00000005844. Homo sapiens.

Family and domain databases

InterPro

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]

Pfam

PF01839. FG-GAP. 1 hit.
PF00357. Integrin_alpha. 1 hit.
PF08441. Integrin_alpha2. 1 hit.
PF00092. VWA. 1 hit.
[Graphical view]

PRINTS

PR01185. INTEGRINA.

SMART

SM00191. Int_alpha. 5 hits.
SM00327. VWA. 1 hit.
[Graphical view]

PROSITE

PS51470. FG_GAP. 7 hits.
PS00242. INTEGRIN_ALPHA. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P20701.

ChEMBL

CHEMBL1803.

DrugBank

DB00095. Efalizumab.

EvolutionaryTrace

P20701.

GenomeRNAi

3683.

NextBio

14415.

SOURCE

Search...

Entry information

Entry name

ITAL_HUMAN

Accession

Primary (citable) accession number: P20701
Secondary accession number(s): O43746 , Q45H73, Q96HB1, Q9UBC8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 7, 2006
Last modified:	May 29, 2013
This is version 151 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.