ITB2_CAPHI
ID ITB2_CAPHI Reviewed; 770 AA.
AC Q5VI41;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Integrin beta-2;
DE AltName: Full=Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta;
DE AltName: Full=Complement receptor C3 subunit beta;
DE AltName: CD_antigen=CD18;
DE Flags: Precursor;
GN Name=ITGB2; Synonyms=CD18;
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15513736; DOI=10.1080/09687680412331282785;
RA Zecchinon L., Fett T., Baise E., Desmecht D.;
RT "Characterization of the caprine (Capra hircus) beta-2 integrin CD18-
RT encoding cDNA and identification of mutations potentially responsible for
RT the ruminant-specific virulence of Mannheimia haemolytica.";
RL Mol. Membr. Biol. 21:289-295(2004).
CC -!- FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3
CC and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted
CC form of ubiquitin-like protein ISG15; the interaction is mediated by
CC ITGAL. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b
CC fragment of the third complement component and for fibrinogen. Integrin
CC ITGAX/ITGB2 recognizes the sequence G-P-R in fibrinogen alpha-chain.
CC Integrin ITGAM/ITGB2 recognizes P1 and P2 peptides of fibrinogen gamma
CC chain. Integrin ITGAM/ITGB2 is also a receptor for factor X. Integrin
CC ITGAD/ITGB2 is a receptor for ICAM3 and VCAM1. Contributes to natural
CC killer cell cytotoxicity. Involved in leukocyte adhesion and
CC transmigration of leukocytes including T-cells and neutrophils.
CC Triggers neutrophil transmigration during lung injury through
CC PTK2B/PYK2-mediated activation. Integrin ITGAL/ITGB2 in association
CC with ICAM3, contributes to apoptotic neutrophil phagocytosis by
CC macrophages. In association with alpha subunit ITGAM/CD11b, required
CC for CD177-PRTN3-mediated activation of TNF primed neutrophils.
CC {ECO:0000250|UniProtKB:P05107}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The ITGB2 beta
CC subunit associates with the ITGAL, ITGAM, ITGAX or ITGAD alpah
CC subunits. Found in a complex with CD177 and ITGAM/CD11b. Interacts with
CC FGR. Interacts with COPS5 and RANBP9. Interacts with FLNA (via filamin
CC repeats 4, 9, 12, 17, 19, 21, and 23). Interacts with THBD.
CC {ECO:0000250|UniProtKB:P05107, ECO:0000250|UniProtKB:P11835}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05107};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05107}.
CC Membrane raft {ECO:0000250|UniProtKB:P05107}; Single-pass type I
CC membrane protein {ECO:0000250|UniProtKB:P05107}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; AY452481; AAS09915.1; -; mRNA.
DR RefSeq; NP_001272467.1; NM_001285538.1.
DR AlphaFoldDB; Q5VI41; -.
DR SMR; Q5VI41; -.
DR STRING; 9925.ENSCHIP00000012357; -.
DR Ensembl; ENSCHIT00000020136; ENSCHIP00000012346; ENSCHIG00000014136.
DR GeneID; 100861185; -.
DR KEGG; chx:100861185; -.
DR CTD; 3689; -.
DR GeneTree; ENSGT01030000234611; -.
DR OMA; FGQYCEC; -.
DR OrthoDB; 473040at2759; -.
DR Proteomes; UP000291000; Chromosome 1.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISS:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR015439; Integrin_bsu-2.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR012896; Integrin_bsu_tail.
DR InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; PTHR10082; 1.
DR PANTHER; PTHR10082:SF15; PTHR10082:SF15; 1.
DR Pfam; PF08725; Integrin_b_cyt; 1.
DR Pfam; PF07965; Integrin_B_tail; 1.
DR Pfam; PF00362; Integrin_beta; 1.
DR Pfam; PF17205; PSI_integrin; 1.
DR PIRSF; PIRSF002512; Integrin_B; 1.
DR PRINTS; PR01186; INTEGRINB.
DR SMART; SM00187; INB; 1.
DR SMART; SM01241; Integrin_b_cyt; 1.
DR SMART; SM01242; Integrin_B_tail; 1.
DR SMART; SM00423; PSI; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF69179; SSF69179; 1.
DR SUPFAM; SSF69687; SSF69687; 1.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein;
KW Integrin; Membrane; Metal-binding; Phagocytosis; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..770
FT /note="Integrin beta-2"
FT /id="PRO_0000273709"
FT TOPO_DOM 23..701
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 702..724
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..770
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 124..363
FT /note="VWFA"
FT REPEAT 449..496
FT /note="I"
FT REPEAT 497..540
FT /note="II"
FT REPEAT 541..581
FT /note="III"
FT REPEAT 582..617
FT /note="IV"
FT REGION 449..617
FT /note="Cysteine-rich tandem repeats"
FT MOTIF 397..399
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 142
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 347
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT MOD_RES 23
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 759
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 761
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 501
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 642
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 25..43
FT /evidence="ECO:0000250"
FT DISULFID 33..447
FT /evidence="ECO:0000250"
FT DISULFID 36..62
FT /evidence="ECO:0000250"
FT DISULFID 46..73
FT /evidence="ECO:0000250"
FT DISULFID 191..198
FT /evidence="ECO:0000250"
FT DISULFID 246..286
FT /evidence="ECO:0000250"
FT DISULFID 386..400
FT /evidence="ECO:0000250"
FT DISULFID 420..445
FT /evidence="ECO:0000250"
FT DISULFID 449..467
FT /evidence="ECO:0000250"
FT DISULFID 459..470
FT /evidence="ECO:0000250"
FT DISULFID 472..481
FT /evidence="ECO:0000250"
FT DISULFID 483..514
FT /evidence="ECO:0000250"
FT DISULFID 497..512
FT /evidence="ECO:0000250"
FT DISULFID 506..517
FT /evidence="ECO:0000250"
FT DISULFID 519..534
FT /evidence="ECO:0000250"
FT DISULFID 536..559
FT /evidence="ECO:0000250"
FT DISULFID 541..557
FT /evidence="ECO:0000250"
FT DISULFID 549..562
FT /evidence="ECO:0000250"
FT DISULFID 564..573
FT /evidence="ECO:0000250"
FT DISULFID 575..598
FT /evidence="ECO:0000250"
FT DISULFID 582..596
FT /evidence="ECO:0000250"
FT DISULFID 590..601
FT /evidence="ECO:0000250"
FT DISULFID 603..612
FT /evidence="ECO:0000250"
FT DISULFID 615..618
FT /evidence="ECO:0000250"
FT DISULFID 622..663
FT /evidence="ECO:0000250"
FT DISULFID 628..647
FT /evidence="ECO:0000250"
FT DISULFID 631..643
FT /evidence="ECO:0000250"
FT DISULFID 671..696
FT /evidence="ECO:0000250"
SQ SEQUENCE 770 AA; 84391 MW; 65BBE5BE9EE9B91F CRC64;
MLPQRPQLLL LAGLLALQSV LSQECTKYKV STCRDCIESG PGCAWCQKLN FTGQGEPDST
RCDTRAQLLS KGCPADDIME PKSLAETRQS QAGKQKQLSP EEVTLYLRPG QAAAFNVTFQ
RAKGYPIDLY YLMDLSYSMV DDLANVKKLG GDLLRALNDI TESGRIGFGS FVDKTVLPFV
NTHPEKLRNP CPNKEKQCQP PFAFRHVLKL TDNSKQFETE VGKQLISGNL DAPEGGLDAM
MQVAACPEEI GWRNVTRLLV FATDDGFHFA GDGKLGAILT PNDGRCHLED NLYKSSNEFD
YPSVGQLAHK LAESNIQPIF AVTKKMVKTY EKLTEIIPKS AVGELSEDSK NVVELIKSAY
NKLSSRVFLD HNTLPDTLKV AYDSFCSNGV SQVDQPRGDC DGVQINVPIT FQVKVTATEC
IQEQSFTIRA LGFTDTVTVR VLPQCECQCR DASRDRSVCG GRGSMECGVC RCDAGYIGKN
CECQTHGRSS QELEGSCRKD NSSIICSGLG DCICGQCVCH TSDVPNKKIY GQFCECDNVN
CERYDGQVCG GEKRGLCFCG TCRCNEQHEG SACQCLKSTQ GCLNLDGVEC SGRGRCRCNV
CQCDPGYQPP LCIDCPGCPV PCAGFAPCTE CLKFDKGPFA KNCSAACGQT KLLSSPVPGG
RKCKERDSEG CWMTYTLVQR DGRNRYDVHV DDMLECVKGP NIAAIVGGTV GGVVLVGILL
LVIWKALTHL SDLREYHRFE KEKLKSQWNN DNPLFKSATT TVMNPKFAES
