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Integrin beta-2 (Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta) (Complement receptor C3 subunit beta) (CD antigen CD18)

 ITB2_PIG                Reviewed;         769 AA.
P53714;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
10-MAY-2017, entry version 117.
RecName: Full=Integrin beta-2;
AltName: Full=Cell surface adhesion glycoproteins LFA-1/CR3/p150,95 subunit beta;
AltName: Full=Complement receptor C3 subunit beta;
AltName: CD_antigen=CD18;
Flags: Precursor;
Name=ITGB2; Synonyms=CD18;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Lee J.K., Schook L.B., Rutherford M.S.;
"Molecular cloning and characterization of the porcine CD18 leukocyte
adhesion molecule.";
Xenotransplantation 3:222-230(1996).
-!- 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. Contributes to natural
killer cell cytotoxicity. Involved in leukocyte adhesion and
transmigration of leukocytes including T-cells and neutrophils.
Triggers neutrophil transmigration during lung injury through
PTK2B/PYK2-mediated activation. Integrin alpha-L/beta-2 in
association with ICAM3, contributes to apoptotic neutrophil
phagocytosis by macrophages. {ECO:0000250|UniProtKB:P05107}.
-!- SUBUNIT: 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. Interacts with FGR. Interacts
with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23).
Interacts with THBD. {ECO:0000250|UniProtKB:P05107}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- SIMILARITY: Belongs to the integrin beta chain family.
{ECO:0000305}.
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EMBL; U13941; AAB16868.1; -; mRNA.
RefSeq; NP_999073.1; NM_213908.1.
UniGene; Ssc.14561; -.
ProteinModelPortal; P53714; -.
SMR; P53714; -.
STRING; 9823.ENSSSCP00000028146; -.
PaxDb; P53714; -.
PeptideAtlas; P53714; -.
PRIDE; P53714; -.
GeneID; 396943; -.
KEGG; ssc:396943; -.
CTD; 3689; -.
eggNOG; KOG1226; Eukaryota.
eggNOG; ENOG410XP60; LUCA.
HOVERGEN; HBG006190; -.
InParanoid; P53714; -.
KO; K06464; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0008305; C:integrin complex; IEA:InterPro.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004872; F:receptor activity; IEA:InterPro.
GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro.
GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:AgBase.
GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:AgBase.
GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
Gene3D; 1.20.5.630; -; 1.
InterPro; IPR033760; Integrin_beta_N.
InterPro; IPR015812; Integrin_bsu.
InterPro; IPR015439; Integrin_bsu-2.
InterPro; IPR014836; Integrin_bsu_cyt_dom.
InterPro; IPR012896; Integrin_bsu_tail.
InterPro; IPR002369; Integrin_bsu_VWA.
InterPro; IPR032695; Integrin_dom.
InterPro; IPR016201; PSI.
InterPro; IPR002035; VWF_A.
PANTHER; PTHR10082; PTHR10082; 1.
PANTHER; PTHR10082:SF47; PTHR10082:SF47; 1.
Pfam; PF08725; Integrin_b_cyt; 1.
Pfam; PF07965; Integrin_B_tail; 1.
Pfam; PF00362; Integrin_beta; 1.
Pfam; PF17205; PSI_integrin; 1.
PIRSF; PIRSF002512; Integrin_B; 1.
PRINTS; PR01186; INTEGRINB.
SMART; SM00187; INB; 1.
SMART; SM01241; Integrin_b_cyt; 1.
SMART; SM01242; Integrin_B_tail; 1.
SMART; SM00423; PSI; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF69179; SSF69179; 1.
SUPFAM; SSF69687; SSF69687; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS00243; INTEGRIN_BETA; 3.
2: Evidence at transcript level;
Calcium; Cell adhesion; Complete proteome; Disulfide bond;
Glycoprotein; Integrin; Membrane; Metal-binding; Phagocytosis;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 22 {ECO:0000250}.
CHAIN 23 769 Integrin beta-2.
/FTId=PRO_0000016343.
TOPO_DOM 23 700 Extracellular. {ECO:0000255}.
TRANSMEM 701 723 Helical. {ECO:0000255}.
TOPO_DOM 724 769 Cytoplasmic. {ECO:0000255}.
DOMAIN 124 363 VWFA.
REPEAT 449 496 I.
REPEAT 497 540 II.
REPEAT 541 581 III.
REPEAT 582 617 IV.
REGION 449 617 Cysteine-rich tandem repeats.
MOTIF 397 399 Cell attachment site. {ECO:0000255}.
METAL 138 138 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 141 141 Calcium. {ECO:0000250}.
METAL 142 142 Calcium. {ECO:0000250}.
METAL 347 347 Calcium. {ECO:0000250}.
MOD_RES 745 745 Phosphoserine.
{ECO:0000250|UniProtKB:P05107}.
MOD_RES 756 756 Phosphoserine.
{ECO:0000250|UniProtKB:P05107}.
MOD_RES 758 758 Phosphothreonine.
{ECO:0000250|UniProtKB:P05107}.
MOD_RES 760 760 Phosphothreonine.
{ECO:0000250|UniProtKB:P05107}.
CARBOHYD 50 50 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 254 254 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 501 501 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 642 642 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 25 43 {ECO:0000250}.
DISULFID 33 447 {ECO:0000250}.
DISULFID 36 62 {ECO:0000250}.
DISULFID 46 73 {ECO:0000250}.
DISULFID 191 198 {ECO:0000250}.
DISULFID 246 286 {ECO:0000250}.
DISULFID 386 400 {ECO:0000250}.
DISULFID 420 445 {ECO:0000250}.
DISULFID 449 467 {ECO:0000250}.
DISULFID 459 470 {ECO:0000250}.
DISULFID 472 481 {ECO:0000250}.
DISULFID 483 514 {ECO:0000250}.
DISULFID 497 512 {ECO:0000250}.
DISULFID 506 517 {ECO:0000250}.
DISULFID 519 534 {ECO:0000250}.
DISULFID 536 559 {ECO:0000250}.
DISULFID 541 557 {ECO:0000250}.
DISULFID 549 562 {ECO:0000250}.
DISULFID 564 573 {ECO:0000250}.
DISULFID 575 598 {ECO:0000250}.
DISULFID 582 596 {ECO:0000250}.
DISULFID 590 601 {ECO:0000250}.
DISULFID 603 612 {ECO:0000250}.
DISULFID 615 618 {ECO:0000250}.
DISULFID 622 662 {ECO:0000250}.
DISULFID 628 647 {ECO:0000250}.
DISULFID 631 643 {ECO:0000250}.
DISULFID 670 695 {ECO:0000250}.
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


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