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Reviewed, UniProtKB/Swiss-Prot P05107 (ITB2_HUMAN)

Last modified September 23, 2008. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Integrin beta-2
Alternative name(s):
    Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta
    Complement receptor C3 subunit beta
    CD_antigen=CD18
Gene names
Name: ITGB2
Synonyms: CD18, MFI7
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length769 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Integrin alpha-L/beta-2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are receptors for the iC3b fragment of the third complement component and for fibrinogen. Integrin alpha-X/beta-2 recognizes the sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2 recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-D/beta-2 is a receptor for ICAM3 and VCAM1.

Subunit structure

Heterodimer of an alpha and a beta subunit. Beta-2 associates with either alpha-L, alpha-M, alpha-X or alpha-D. Interacts with COPS5 and RANBP9.

Subcellular location

Membrane; Single-pass type I membrane protein.

Post-translational modification

Both Ser-745 and Ser-756 become phosphorylated when T-cells are exposed to phorbol esters. Phosphorylation on Thr-758 (but not on Ser-756) allows interaction with 14-3-3 proteins.

Involvement in disease

Defects in ITGB2 are the cause of leukocyte adhesion deficiency type I (LAD1) [MIM:116920]. LAD1 patients have recurrent bacterial infections and their leukocytes are deficient in a wide range of adhesion-dependent functions.

Sequence similarities

Belongs to the integrin beta chain family.

Contains 1 VWFA domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SYKP434051EBI-300173,EBI-78302

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical view

Molecule processing

Signal peptide1 – 2222
Chain23 – 769747Integrin beta-2

Regions

Topological domain23 – 700678Extracellular Potential
Transmembrane701 – 72323 Potential
Topological domain724 – 76946Cytoplasmic Potential
Domain124 – 363240VWFA
Repeat449 – 49648I
Repeat497 – 54044II
Repeat541 – 58141III
Repeat582 – 61736IV
Region449 – 617169Cysteine-rich tandem repeats
Motif397 – 3993Cell attachment site Potential

Amino acid modifications

Modified residue231Pyrrolidone carboxylic acid
Modified residue7451Phosphoserine; by PKC
Modified residue7561Phosphoserine
Modified residue7581Phosphothreonine; by PKC; in vitro
Modified residue7591Phosphothreonine Potential
Modified residue7601Phosphothreonine; by PKC/PRKCA; in vitro
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation2121N-linked (GlcNAc...)
Glycosylation2541N-linked (GlcNAc...) Potential
Glycosylation5011N-linked (GlcNAc...) Potential
Glycosylation6421N-linked (GlcNAc...) Potential
Disulfide bond25 ↔ 447 By similarity
Disulfide bond33 ↔ 43 By similarity
Disulfide bond36 ↔ 73 By similarity
Disulfide bond46 ↔ 62 By similarity
Disulfide bond191 ↔ 198 By similarity
Disulfide bond246 ↔ 286 By similarity
Disulfide bond386 ↔ 400 By similarity
Disulfide bond420 ↔ 662 By similarity
Disulfide bond445 ↔ 449 By similarity
Disulfide bond459 ↔ 470 By similarity
Disulfide bond467 ↔ 506 By similarity
Disulfide bond472 ↔ 481 By similarity
Disulfide bond483 ↔ 497 By similarity
Disulfide bond512 ↔ 517 By similarity
Disulfide bond514 ↔ 549 By similarity
Disulfide bond519 ↔ 534 By similarity
Disulfide bond536 ↔ 541 By similarity
Disulfide bond557 ↔ 562 By similarity
Disulfide bond559 ↔ 590 By similarity
Disulfide bond564 ↔ 573 By similarity
Disulfide bond575 ↔ 582 By similarity
Disulfide bond596 ↔ 601 By similarity
Disulfide bond598 ↔ 643 By similarity
Disulfide bond603 ↔ 612 By similarity
Disulfide bond615 ↔ 618 By similarity
Disulfide bond622 ↔ 631 By similarity
Disulfide bond628 ↔ 695 By similarity
Disulfide bond647 ↔ 670 By similarity

Natural variations

Natural variant1281D → N in LAD1.
Natural variant1381S → P in LAD1.
Natural variant1491L → P in LAD1.
Natural variant1691G → R in LAD1.
Natural variant1781P → L in LAD1.
Natural variant1961K → T in LAD1.
Natural variant2731G → R in LAD1.
Natural variant2841G → S in LAD1.
Natural variant3511N → S in LAD1.
Natural variant3541Q → H: dbSNP rs235330.
Natural variant5861R → W in LAD1. dbSNP rs5030672.
Natural variant5931R → C in LAD1.

Experimental info

Sequence conflict1991Q → P in CAA68266. Ref.5

Secondary structure

........................................................ 769
Helix Strand Turn

Details...