ID D3DSM0_HUMAN Unreviewed; 712 AA. AC D3DSM0; A8MYE6; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 16-JAN-2019, entry version 69. DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633}; GN Name=ITGB2 {ECO:0000313|EMBL:EAX09384.1, GN ECO:0000313|Ensembl:ENSP00000380952}; GN ORFNames=hCG_401305 {ECO:0000313|EMBL:EAX09384.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:EAX09384.1}; RN [1] {ECO:0000313|Ensembl:ENSP00000380952, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=10830953; DOI=10.1038/35012518; RG Chromosome 21 mapping and sequencing consortium; RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., RA Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., RA Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K., RA Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D., RA Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W., RA Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S., RA Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E., RA Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P., RA Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H., RA Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E., RA Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F., RA Lehrach H., Reinhardt R., Yaspo M.-L.; RT "The DNA sequence of human chromosome 21."; RL Nature 405:311-319(2000). RN [2] {ECO:0000313|EMBL:EAX09384.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., RA Amanatides P., Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., RA Kodira C.D., Zheng X.H., Chen L., Skupski M., Subramanian G., RA Thomas P.D., Zhang J., Gabor Miklos G.L., Nelson C., Broder S., RA Clark A.G., Nadeau J., McKusick V.A., Zinder N., Levine A.J., RA Roberts R.J., Simon M., Slayman C., Hunkapiller M., Bolanos R., RA Delcher A., Dew I., Fasulo D., Flanigan M., Florea L., Halpern A., RA Hannenhalli S., Kravitz S., Levy S., Mobarry C., Reinert K., RA Remington K., Abu-Threideh J., Beasley E., Biddick K., Bonazzi V., RA Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., RA Guan P., Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., RA Lai Z., Lei Y., Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., RA Milshina N., Moore H.M., Naik A.K., Narayan V.A., Neelam B., RA Nusskern D., Rusch D.B., Salzberg S., Shao W., Shue B., Sun J., RA Wang Z., Wang A., Wang X., Wang J., Wei M., Wides R., Xiao C., Yan C., RA Yao A., Ye J., Zhan M., Zhang W., Zhang H., Zhao Q., Zheng L., RA Zhong F., Zhong W., Zhu S., Zhao S., Gilbert D., Baumhueter S., RA Spier G., Carter C., Cravchik A., Woodage T., Ali F., An H., Awe A., RA Baldwin D., Baden H., Barnstead M., Barrow I., Beeson K., Busam D., RA Carver A., Center A., Cheng M.L., Curry L., Danaher S., Davenport L., RA Desilets R., Dietz S., Dodson K., Doup L., Ferriera S., Garg N., RA Gluecksmann A., Hart B., Haynes J., Haynes C., Heiner C., Hladun S., RA Hostin D., Houck J., Howland T., Ibegwam C., Johnson J., Kalush F., RA Kline L., Koduru S., Love A., Mann F., May D., McCawley S., RA McIntosh T., McMullen I., Moy M., Moy L., Murphy B., Nelson K., RA Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., RA Tse S., Vech C., Wang G., Wetter J., Williams S., Williams M., RA Windsor S., Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., RA Guigo R., Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., RA Mi H., Lazareva B., Hatton T., Narechania A., Diemer K., RA Muruganujan A., Guo N., Sato S., Bafna V., Istrail S., Lippert R., RA Schwartz R., Walenz B., Yooseph S., Allen D., Basu A., Baxendale J., RA Blick L., Caminha M., Carnes-Stine J., Caulk P., Chiang Y.H., RA Coyne M., Dahlke C., Mays A., Dombroski M., Donnelly M., Ely D., RA Esparham S., Fosler C., Gire H., Glanowski S., Glasser K., Glodek A., RA Gorokhov M., Graham K., Gropman B., Harris M., Heil J., Henderson S., RA Hoover J., Jennings D., Jordan C., Jordan J., Kasha J., Kagan L., RA Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., Ma D., Majoros W., RA McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., Nodell M., RA Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [3] {ECO:0000313|EMBL:EAX09384.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0000313|Ensembl:ENSP00000380952} RP IDENTIFICATION. RG Ensembl; RL Submitted (JUL-2011) to UniProtKB. RN [5] {ECO:0000213|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., RA Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|RuleBase:RU000633}; CC Single-pass type I membrane protein CC {ECO:0000256|RuleBase:RU000633}. CC -!- SIMILARITY: Belongs to the integrin beta chain family. CC {ECO:0000256|RuleBase:RU000633}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AL773603; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL844907; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL844908; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; KC877928; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471079; EAX09383.1; -; Genomic_DNA. DR EMBL; CH471079; EAX09384.1; -; Genomic_DNA. DR UniGene; Hs.375957; -. DR jPOST; D3DSM0; -. DR PRIDE; D3DSM0; -. DR Ensembl; ENST00000397854; ENSP00000380952; ENSG00000160255. DR UCSC; uc010gpw.4; human. DR EuPathDB; HostDB:ENSG00000160255.16; -. DR HGNC; HGNC:6155; ITGB2. DR OpenTargets; ENSG00000160255; -. DR GeneTree; ENSGT00940000157111; -. DR HOGENOM; HOG000252936; -. DR HOVERGEN; HBG006190; -. DR ChiTaRS; ITGB2; human. DR Proteomes; UP000005640; Chromosome 21. DR Bgee; ENSG00000160255; Expressed in 187 organ(s), highest expression level in blood. DR ExpressionAtlas; D3DSM0; baseline and differential. DR GO; GO:0008305; C:integrin complex; IEA:InterPro. DR GO; GO:0038023; F:signaling receptor activity; IEA:InterPro. DR GO; GO:0007160; P:cell-matrix adhesion; IEA:InterPro. DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW. 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; 2. DR PANTHER; PTHR10082:SF15; PTHR10082:SF15; 2. 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; 2. 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; PS00243; INTEGRIN_BETA; 1. PE 1: Evidence at protein level; KW Cell adhesion {ECO:0000256|RuleBase:RU000633}; KW Complete proteome {ECO:0000313|Proteomes:UP000005640}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1}; KW Integrin {ECO:0000256|RuleBase:RU000633, KW ECO:0000256|SAAS:SAAS00895071, ECO:0000313|EMBL:EAX09384.1}; KW Membrane {ECO:0000256|SAAS:SAAS00895947, ECO:0000256|SAM:Phobius}; KW Proteomics identification {ECO:0000213|EPD:D3DSM0, KW ECO:0000213|MaxQB:D3DSM0, ECO:0000213|PeptideAtlas:D3DSM0}; KW Receptor {ECO:0000313|EMBL:EAX09384.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|SAAS:SAAS00895947, KW ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAAS:SAAS00895947, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1 22 {ECO:0000256|SAM:SignalP}. FT CHAIN 23 712 Integrin beta. {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5014569739. FT TRANSMEM 644 670 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 24 74 PSI. {ECO:0000259|SMART:SM00423}. FT DOMAIN 32 390 INB. {ECO:0000259|SMART:SM00187}. FT DOMAIN 565 643 Integrin_B_tail. FT {ECO:0000259|SMART:SM01242}. FT DOMAIN 667 712 Integrin_b_cyt. FT {ECO:0000259|SMART:SM01241}. FT DISULFID 134 141 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 189 229 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 363 605 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 388 392 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 410 449 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 415 424 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 426 440 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 455 460 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 457 492 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 462 477 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 479 484 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 500 505 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 502 533 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 507 516 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 539 544 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 541 586 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 546 555 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 558 561 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 565 574 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 571 638 {ECO:0000256|PIRSR:PIRSR002512-1}. FT DISULFID 590 613 {ECO:0000256|PIRSR:PIRSR002512-1}. SQ SEQUENCE 712 AA; 78354 MW; 9F9D372A27AE6C0F CRC64; MLGLRPPLLA LVGLLSLGCV LSQECTKFKV SSCRECIESG PGCTWCQKLN FTGPGDPDSI RCDTRPQLLM RGCAADDIMD PTSLAETQED HNGGQKQLSP QKVTLYLRPG FGSFVDKTVL PFVNTHPDKL RNPCPNKEKE CQPPFAFRHV LKLTNNSNQF QTEVGKQLIS GNLDAPEGGL DAMMQVAACP EEIGWRNVTR LLVFATDDGF HFAGDGKLGA ILTPNDGRCH LEDNLYKRSN EFDYPSVGQL AHKLAENNIQ PIFAVTSRMV KTYEKLTEII PKSAVGELSE DSSNVVHLIK NAYNKLSSRV FLDHNALPDT LKVTYDSFCS NGVTHRNQPR GDCDGVQINV PITFQVKVTA TECIQEQSFV IRALGFTDIV TVQVLPQCEC RCRDQSRDRS LCHGKGFLEC GICRCDTGYI GKNCECQTQG RSSQELEGSC RKDNNSIICS GLGDCVCGQC LCHTSDVPGK LIYGQYCECD TINCERYNGQ VCGGPGRGLC FCGKCRCHPG FEGSACQCER TTEGCLNPRR VECSGRGRCR CNVCECHSGY QLPLCQECPG CPSPCGKYIS CAECLKFEKG PFGKNCSAAC PGLQLSNNPV KGRTCKERDS EGCWVAYTLE QQDGMDRYLI YVDESRECVA GPNIAAIVGG TVAGIVLIGI LLLVIWKALI HLSDLREYRR FEKEKLKSQW NNDNPLFKSA TTTVMNPKFA ES //