ID   Q4KLK5_RAT              Unreviewed;       316 AA.
AC   Q4KLK5;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=Itgb2 protein {ECO:0000313|EMBL:AAH99151.1};
GN   Name=Itgb2 {ECO:0000313|EMBL:AAH99151.1, ECO:0000313|RGD:1305581};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAH99151.1};
RN   [1] {ECO:0000313|EMBL:AAH99151.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Spleen {ECO:0000313|EMBL:AAH99151.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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DR   EMBL; BC099151; AAH99151.1; -; mRNA.
DR   AlphaFoldDB; Q4KLK5; -.
DR   SMR; Q4KLK5; -.
DR   UCSC; RGD:1305581; rat.
DR   AGR; RGD:1305581; -.
DR   RGD; 1305581; Itgb2.
DR   PhylomeDB; Q4KLK5; -.
DR   GO; GO:0009986; C:cell surface; IDA:RGD.
DR   GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR   GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR   GO; GO:0034687; C:integrin alphaL-beta2 complex; ISO:RGD.
DR   GO; GO:0034688; C:integrin alphaM-beta2 complex; ISO:RGD.
DR   GO; GO:0008305; C:integrin complex; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0045121; C:membrane raft; ISO:RGD.
DR   GO; GO:0044853; C:plasma membrane raft; ISO:RGD.
DR   GO; GO:0043235; C:receptor complex; ISO:RGD.
DR   GO; GO:0001540; F:amyloid-beta binding; ISO:RGD.
DR   GO; GO:0050839; F:cell adhesion molecule binding; ISO:RGD.
DR   GO; GO:0001851; F:complement component C3b binding; ISO:RGD.
DR   GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
DR   GO; GO:0030369; F:ICAM-3 receptor activity; ISO:RGD.
DR   GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0050798; P:activated T cell proliferation; ISO:RGD.
DR   GO; GO:0097242; P:amyloid-beta clearance; ISO:RGD.
DR   GO; GO:0007155; P:cell adhesion; ISO:RGD.
DR   GO; GO:0098609; P:cell-cell adhesion; IMP:RGD.
DR   GO; GO:0007160; P:cell-matrix adhesion; ISO:RGD.
DR   GO; GO:0045123; P:cellular extravasation; IMP:RGD.
DR   GO; GO:0071404; P:cellular response to low-density lipoprotein particle stimulus; ISO:RGD.
DR   GO; GO:0035987; P:endodermal cell differentiation; ISO:RGD.
DR   GO; GO:0043542; P:endothelial cell migration; IMP:RGD.
DR   GO; GO:0034113; P:heterotypic cell-cell adhesion; ISO:RGD.
DR   GO; GO:0007229; P:integrin-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0007159; P:leukocyte cell-cell adhesion; IMP:RGD.
DR   GO; GO:0002523; P:leukocyte migration involved in inflammatory response; IMP:RGD.
DR   GO; GO:0030593; P:neutrophil chemotaxis; ISO:RGD.
DR   GO; GO:1990266; P:neutrophil migration; ISO:RGD.
DR   GO; GO:0006911; P:phagocytosis, engulfment; ISO:RGD.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR   GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:RGD.
DR   GO; GO:0043315; P:positive regulation of neutrophil degranulation; ISO:RGD.
DR   GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IMP:RGD.
DR   GO; GO:0032930; P:positive regulation of superoxide anion generation; ISO:RGD.
DR   GO; GO:0043113; P:receptor clustering; ISO:RGD.
DR   GO; GO:0031623; P:receptor internalization; ISO:RGD.
DR   GO; GO:0006898; P:receptor-mediated endocytosis; ISO:RGD.
DR   GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISO:RGD.
DR   Gene3D; 4.10.1240.30; -; 1.
DR   Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   InterPro; IPR015812; Integrin_bsu.
DR   InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR   InterPro; IPR012896; Integrin_bsu_tail.
DR   InterPro; IPR036349; Integrin_bsu_tail_dom_sf.
DR   PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR   PANTHER; PTHR10082:SF15; INTEGRIN BETA-2; 1.
DR   Pfam; PF08725; Integrin_b_cyt; 1.
DR   Pfam; PF07965; Integrin_B_tail; 1.
DR   PRINTS; PR01186; INTEGRINB.
DR   SMART; SM01241; Integrin_b_cyt; 1.
DR   SMART; SM01242; Integrin_B_tail; 1.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   SUPFAM; SSF69687; Integrin beta tail domain; 1.
DR   PROSITE; PS00243; INTEGRIN_BETA; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        248..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          170..247
FT                   /note="Integrin beta subunit tail"
FT                   /evidence="ECO:0000259|SMART:SM01242"
FT   DOMAIN          271..316
FT                   /note="Integrin beta subunit cytoplasmic"
FT                   /evidence="ECO:0000259|SMART:SM01241"
SQ   SEQUENCE   316 AA;  34629 MW;  822785BF31B6F2A4 CRC64;
     MGVPIPGADL SATLPHHTRC ESGYIGKNCE CQTQGRSSQE LEGNCRKDNS SIVCSGLGDC
     ICGQCVCHTS DIPNKVIFGQ YCECDNFNCE RYDGQVCGGL KRGSCSCGQC NCKEGFEGSA
     CQCQRSTTGC LNARLVECSG RGRCQCNRCI CEKGYQPPLC EECPGCPLPC STYVFCAECL
     KFDKGPFQKN CSVQCANVTL QTVPFKKKPC KERDSEGCWI TYTLQQKDGN AYNIHVDDDR
     ECVKGPNVAA IIGGTVAGVV LIGVLLLVIW KALTHLTDLN EYRRFEKEKL KSQWNNDNPL
     FKSATTTVMN PKFAES
//