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Database: UniProt
Entry: Q6ECI6
LinkDB: Q6ECI6
Original site: Q6ECI6 
ID   ITB2_SHEEP              Reviewed;         770 AA.
AC   Q6ECI6;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   16-JAN-2019, entry version 83.
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   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=15256254; DOI=10.1016/j.gene.2004.03.011;
RA   Zecchinon L., Fett T., Baise E., Desmecht D.;
RT   "Molecular cloning and characterisation of the CD18 partner in ovine
RT   (Ovis aries) beta2-integrins.";
RL   Gene 334:47-52(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Dassanayake R.P., Srikumaran S.;
RT   "Mannheimia haemolytica leukotoxin-induced cytolysis of ovine
RT   leukocytes is mediated by CD18, the beta subunit of beta-2
RT   integrins.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2,
CC       ICAM3 and ICAM4. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are
CC       receptors for the iC3b fragment of the third complement component
CC       and for fibrinogen. Integrin ITGAX/ITGB2 recognizes the sequence
CC       G-P-R in fibrinogen alpha-chain. Integrin ITGAM/ITGB2 recognizes
CC       P1 and P2 peptides of fibrinogen gamma chain. Integrin ITGAM/ITGB2
CC       is also a receptor for factor X. Integrin ITGAD/ITGB2 is a
CC       receptor for ICAM3 and VCAM1. Contributes to natural killer cell
CC       cytotoxicity. Involved in leukocyte adhesion and transmigration of
CC       leukocytes including T-cells and neutrophils. Triggers neutrophil
CC       transmigration during lung injury through PTK2B/PYK2-mediated
CC       activation. Integrin ITGAL/ITGB2 in association with ICAM3,
CC       contributes to apoptotic neutrophil phagocytosis by macrophages.
CC       In association with alpha subunit ITGAM/CD11b, required for CD177-
CC       PRTN3-mediated activation of TNF primed neutrophils.
CC       {ECO:0000250|UniProtKB:P05107}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. ITGB2
CC       associates with either ITGAL, ITGAM, ITGAX or ITGAD. Found in a
CC       complex with CD177 and ITGAM/CD11b. Interacts with FGR. Interacts
CC       with COPS5 and RANBP9. Interacts with FLNA (via filamin repeats 4,
CC       9, 12, 17, 19, 21, and 23). {ECO:0000250|UniProtKB:P05107,
CC       ECO:0000250|UniProtKB:P11835}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:P05107}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P05107}. Membrane raft
CC       {ECO:0000250|UniProtKB:P05107}; Single-pass type I membrane
CC       protein {ECO:0000250|UniProtKB:P05107}.
CC   -!- SIMILARITY: Belongs to the integrin beta chain family.
CC       {ECO:0000305}.
DR   EMBL; AY484425; AAS55864.1; -; mRNA.
DR   EMBL; AY484426; AAS55865.1; -; mRNA.
DR   EMBL; DQ470837; ABE98168.1; -; mRNA.
DR   RefSeq; NP_001009485.1; NM_001009485.1.
DR   UniGene; Oar.3170; -.
DR   ProteinModelPortal; Q6ECI6; -.
DR   SMR; Q6ECI6; -.
DR   PRIDE; Q6ECI6; -.
DR   GeneID; 494433; -.
DR   KEGG; oas:494433; -.
DR   CTD; 3689; -.
DR   HOVERGEN; HBG006190; -.
DR   KO; K06464; -.
DR   OrthoDB; 473040at2759; -.
DR   Proteomes; UP000002356; Unplaced.
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: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; Complete proteome;
KW   Disulfide bond; Glycoprotein; Integrin; Membrane; Metal-binding;
KW   Phagocytosis; Phosphoprotein; Pyrrolidone carboxylic acid; Receptor;
KW   Reference proteome; Repeat; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     22       {ECO:0000250}.
FT   CHAIN        23    770       Integrin beta-2.
FT                                /FTId=PRO_0000273711.
FT   TOPO_DOM     23    701       Extracellular. {ECO:0000255}.
FT   TRANSMEM    702    724       Helical. {ECO:0000255}.
FT   TOPO_DOM    725    770       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     746    746       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     757    757       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     759    759       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P05107}.
FT   MOD_RES     761    761       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    663       {ECO:0000250}.
FT   DISULFID    628    647       {ECO:0000250}.
FT   DISULFID    631    643       {ECO:0000250}.
FT   DISULFID    671    696       {ECO:0000250}.
SQ   SEQUENCE   770 AA;  84366 MW;  67F5CECB23018C31 CRC64;
     MLPQRPQLLL LAGLLSLQSV LSQECTKYKV STCRDCIESG PGCAWCQKLN FTGQGEPDST
     RCDTRAQLLS KGCPADDIME PKSLAETRQS QAGKQKQLSP EEVTLYLRPG QAAAFNVTFQ
     RAKGYPIDLY YLMDLSYSMV DDLANVKKLG GDLLRALNDI TESGRIGFGS FVDKTVLPFV
     NTHPEKLRNP CPNKEKECQP 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 EASRDRSVCG GRGSMECGVC RCDAGYIGKN
     CECQTHGRSS QELEGSCRKD NSSIICSGLG DCICGQCVCH TSDVPNKKIY GQFCECDNVN
     CERYDGQVCG GDKRGLCFCG TCRCNDQHEG SACQCLKSTQ GCLNLDGVEC SGRGRCRCNV
     CQCDPGYQPP LCIDCPGCPV PCAGFAPCTE CLKFDKGPFA KNCSAACGQT KLLSSPVPGG
     RKCKERDSEG CWMTYTLVQR DGRNRYDVHV DDMLECVKGP NIAAIVGGTV GGVVLVGILL
     LAIWKALTHL SDLREYHRFE KEKLKSQWNN DNPLFKSATT TVMNPKFAES
//
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