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Database: UniProt
Entry: P53714
LinkDB: P53714
Original site: P53714 
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   16-JAN-2019, entry version 123.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   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 alpha-L/beta-2 is a receptor for ICAM1, ICAM2,
CC       ICAM3 and ICAM4. Integrins alpha-M/beta-2 and alpha-X/beta-2 are
CC       receptors for the iC3b fragment of the third complement component
CC       and for fibrinogen. Integrin alpha-X/beta-2 recognizes the
CC       sequence G-P-R in fibrinogen alpha-chain. Integrin alpha-M/beta-2
CC       recognizes P1 and P2 peptides of fibrinogen gamma chain. Integrin
CC       alpha-M/beta-2 is also a receptor for factor X. Integrin alpha-
CC       D/beta-2 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
CC       association with ICAM3, contributes to apoptotic neutrophil
CC       phagocytosis by macrophages. {ECO:0000250|UniProtKB:P05107}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. Beta-2
CC       associates with either alpha-L, alpha-M, alpha-X or alpha-D.
CC       Interacts with COPS5 and RANBP9. Interacts with FGR. Interacts
CC       with FLNA (via filamin repeats 4, 9, 12, 17, 19, 21, and 23).
CC       Interacts with THBD. {ECO:0000250|UniProtKB:P05107}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; U13941; AAB16868.1; -; mRNA.
DR   RefSeq; NP_999073.1; NM_213908.1.
DR   UniGene; Ssc.14561; -.
DR   ProteinModelPortal; 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   eggNOG; ENOG410XP60; LUCA.
DR   HOVERGEN; HBG006190; -.
DR   InParanoid; P53714; -.
DR   KO; K06464; -.
DR   OrthoDB; 473040at2759; -.
DR   Proteomes; UP000008227; Unplaced.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
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:0050766; P:positive regulation of phagocytosis; IMP:AgBase.
DR   GO; GO:0031623; P:receptor internalization; ISS:UniProtKB.
DR   Gene3D; 1.20.5.630; -; 1.
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; IPR037076; Integrin_bsu_cyt_dom_sf.
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; Complete proteome; Disulfide bond;
KW   Glycoprotein; Integrin; Membrane; Metal-binding; Phagocytosis;
KW   Phosphoprotein; Pyrrolidone carboxylic acid; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22       {ECO:0000250}.
FT   CHAIN        23    769       Integrin beta-2.
FT                                /FTId=PRO_0000016343.
FT   TOPO_DOM     23    700       Extracellular. {ECO:0000255}.
FT   TRANSMEM    701    723       Helical. {ECO:0000255}.
FT   TOPO_DOM    724    769       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      124    363       VWFA.
FT   REPEAT      449    496       I.
FT   REPEAT      497    540       II.
FT   REPEAT      541    581       III.
FT   REPEAT      582    617       IV.
FT   REGION      449    617       Cysteine-rich tandem repeats.
FT   MOTIF       397    399       Cell attachment site. {ECO:0000255}.
FT   METAL       138    138       Calcium; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   METAL       141    141       Calcium. {ECO:0000250}.
FT   METAL       142    142       Calcium. {ECO:0000250}.
FT   METAL       347    347       Calcium. {ECO:0000250}.
FT   MOD_RES      23     23       Pyrrolidone carboxylic acid.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     745    745       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     756    756       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     758    758       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     760    760       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   CARBOHYD     50     50       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    116    116       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    254    254       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    501    501       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    642    642       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     25     43       {ECO:0000250}.
FT   DISULFID     33    447       {ECO:0000250}.
FT   DISULFID     36     62       {ECO:0000250}.
FT   DISULFID     46     73       {ECO:0000250}.
FT   DISULFID    191    198       {ECO:0000250}.
FT   DISULFID    246    286       {ECO:0000250}.
FT   DISULFID    386    400       {ECO:0000250}.
FT   DISULFID    420    445       {ECO:0000250}.
FT   DISULFID    449    467       {ECO:0000250}.
FT   DISULFID    459    470       {ECO:0000250}.
FT   DISULFID    472    481       {ECO:0000250}.
FT   DISULFID    483    514       {ECO:0000250}.
FT   DISULFID    497    512       {ECO:0000250}.
FT   DISULFID    506    517       {ECO:0000250}.
FT   DISULFID    519    534       {ECO:0000250}.
FT   DISULFID    536    559       {ECO:0000250}.
FT   DISULFID    541    557       {ECO:0000250}.
FT   DISULFID    549    562       {ECO:0000250}.
FT   DISULFID    564    573       {ECO:0000250}.
FT   DISULFID    575    598       {ECO:0000250}.
FT   DISULFID    582    596       {ECO:0000250}.
FT   DISULFID    590    601       {ECO:0000250}.
FT   DISULFID    603    612       {ECO:0000250}.
FT   DISULFID    615    618       {ECO:0000250}.
FT   DISULFID    622    662       {ECO:0000250}.
FT   DISULFID    628    647       {ECO:0000250}.
FT   DISULFID    631    643       {ECO:0000250}.
FT   DISULFID    670    695       {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
//
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