ITB2_PIG
ID ITB2_PIG Reviewed; 769 AA.
AC P53714;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 135.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Lee J.K., Schook L.B., Rutherford M.S.;
RT "Molecular cloning and characterization of the porcine CD18 leukocyte
RT adhesion molecule.";
RL Xenotransplantation 3:222-230(1996).
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 alpha-L/beta-2 in association
CC with ICAM3, contributes to apoptotic neutrophil phagocytosis by
CC macrophages. {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 alpha
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}.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- SIMILARITY: Belongs to the integrin beta chain family. {ECO:0000305}.
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DR EMBL; U13941; AAB16868.1; -; mRNA.
DR RefSeq; NP_999073.1; NM_213908.1.
DR AlphaFoldDB; P53714; -.
DR SMR; P53714; -.
DR STRING; 9823.ENSSSCP00000028146; -.
DR PaxDb; P53714; -.
DR PeptideAtlas; P53714; -.
DR PRIDE; P53714; -.
DR GeneID; 396943; -.
DR KEGG; ssc:396943; -.
DR CTD; 3689; -.
DR eggNOG; KOG1226; Eukaryota.
DR InParanoid; P53714; -.
DR OrthoDB; 473040at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0008305; C:integrin complex; IEA:InterPro.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro.
DR GO; GO:0033627; P:cell adhesion mediated by integrin; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:AgBase.
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:0050766; P:positive regulation of phagocytosis; IMP:AgBase.
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; 3.
DR PROSITE; PS00243; INTEGRIN_BETA; 3.
PE 2: Evidence at transcript level;
KW Calcium; Cell adhesion; Disulfide bond; Glycoprotein; Integrin; Membrane;
KW Metal-binding; Phagocytosis; Phosphoprotein; Pyrrolidone carboxylic acid;
KW Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000250"
FT CHAIN 23..769
FT /note="Integrin beta-2"
FT /id="PRO_0000016343"
FT TOPO_DOM 23..700
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 701..723
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 724..769
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 745
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 758
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P05107"
FT MOD_RES 760
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..662
FT /evidence="ECO:0000250"
FT DISULFID 628..647
FT /evidence="ECO:0000250"
FT DISULFID 631..643
FT /evidence="ECO:0000250"
FT DISULFID 670..695
FT /evidence="ECO:0000250"
SQ SEQUENCE 769 AA; 84790 MW; FDD606CEEE850449 CRC64;
MLCRCSPLLL LVGLLTLRSA LSQECAKYKV STCRDCIESG PGCAWCQKLN FSGQGEPDSV
RCDTREQLLA KGCVADDIVD PRSLAETQED QAGGQKQLSP QKVTLYLRPG QAATFNVTFR
RAKGYPIDLY YLMDLSYSML DDLINVKKLG GDLLRALNEI TESGRIGFGS FVDKTVLPFV
NTHPEKLRNP CPNKEKECQA PFAFRHVLKL TDNSNQFQTE VGKQLISGNL DAPEGGLDAM
MQVAACPEEI GWRNVTRLLV FATDDGFHFA GDGKLGAILT PNDGRCHLED NLYKSSNEFD
YPSVGQLAHK LAESNIQPIF AVTKKMVKTY EKLTDIIPKS AVGELSEDSS NVLELIKNAY
NKLSSRVFLD HNALPDTLKV TYDSFCSNGV SQVNQPRGDC DGVQINVPIT FQVKVTASEC
IQEQSFVIRA LGFTDTVTVR VLPQCECRCG DSSKERTLCG NKGSMECGVC RCDAGYIGKH
CECQTQGRSS QELEGSCRKD NSSIICSGLG DCICGQCVCH TSDVPNKKIY GQFCECDNMN
CERFDGQVCG GEKRGLCFCS TCRCQEGFEG SACQCLKSTQ GCLNLQGVEC SGRGRCRCNV
CQCDFGYQPP LCTDCPSCQV PCARYAKCAE CLKFDTGPFA KNCSAECGTT KLLPSRMSGR
KCNERDSEGC WMTYFLVQRD GRDNYDLHVE ETRECVKGPN IAAIVGGTVG GVVLVGIFLL
VIWKVLTHLS DLREYKRFEK EKLKSQWNND NPLFKSATTT VMNPKFAER
