ID B4GJH0_DROPE Unreviewed; 767 AA.
AC B4GJH0;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 96.
DE RecName: Full=Integrin beta {ECO:0000256|RuleBase:RU000633};
GN Name=Dper\GL25882 {ECO:0000313|EMBL:EDW36786.1};
GN ORFNames=Dper_GL25882 {ECO:0000313|EMBL:EDW36786.1};
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234 {ECO:0000313|Proteomes:UP000008744};
RN [1] {ECO:0000313|EMBL:EDW36786.1, ECO:0000313|Proteomes:UP000008744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49
RC {ECO:0000313|Proteomes:UP000008744};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU000633};
CC Single-pass type I membrane protein {ECO:0000256|RuleBase:RU000633}.
CC Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004479}.
CC -!- SIMILARITY: Belongs to the integrin beta chain family.
CC {ECO:0000256|ARBA:ARBA00007449, ECO:0000256|RuleBase:RU000633}.
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DR EMBL; CH479184; EDW36786.1; -; Genomic_DNA.
DR RefSeq; XP_002018590.1; XM_002018554.1.
DR AlphaFoldDB; B4GJH0; -.
DR STRING; 7234.B4GJH0; -.
DR EnsemblMetazoa; FBtr0191497; FBpp0189989; FBgn0163466.
DR GeneID; 6593369; -.
DR KEGG; dpe:6593369; -.
DR eggNOG; KOG1226; Eukaryota.
DR HOGENOM; CLU_011772_1_0_1; -.
DR OMA; KQGMGAC; -.
DR OrthoDB; 5475862at2759; -.
DR PhylomeDB; B4GJH0; -.
DR Proteomes; UP000008744; Unassembled WGS sequence.
DR GO; GO:0008305; C:integrin complex; IEA:EnsemblMetazoa.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0043277; P:apoptotic cell clearance; IEA:EnsemblMetazoa.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:UniProt.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0035011; P:melanotic encapsulation of foreign target; IEA:EnsemblMetazoa.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:EnsemblMetazoa.
DR GO; GO:0045886; P:negative regulation of synaptic assembly at neuromuscular junction; IEA:EnsemblMetazoa.
DR Gene3D; 1.20.5.100; Cytochrome c1, transmembrane anchor, C-terminal; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 3.30.1680.10; ligand-binding face of the semaphorins, domain 2; 1.
DR Gene3D; 2.60.40.1510; ntegrin, alpha v. Chain A, domain 3; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR013111; EGF_extracell.
DR InterPro; IPR033760; Integrin_beta_N.
DR InterPro; IPR015812; Integrin_bsu.
DR InterPro; IPR014836; Integrin_bsu_cyt_dom.
DR InterPro; IPR002369; Integrin_bsu_VWA.
DR InterPro; IPR032695; Integrin_dom_sf.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR10082; INTEGRIN BETA SUBUNIT; 1.
DR PANTHER; PTHR10082:SF59; INTEGRIN BETA-NU; 1.
DR Pfam; PF07974; EGF_2; 2.
DR Pfam; PF08725; Integrin_b_cyt; 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; SM00327; VWA; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 2.
DR SUPFAM; SSF69179; Integrin domains; 1.
DR SUPFAM; SSF103575; Plexin repeat; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS00243; INTEGRIN_BETA; 2.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW Cell adhesion {ECO:0000256|ARBA:ARBA00022889,
KW ECO:0000256|RuleBase:RU000633};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR002512-1};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000256|ARBA:ARBA00023037, ECO:0000256|RuleBase:RU000633};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008744};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU000633};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 691..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 104..340
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DISULFID 6..16
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 9..41
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 19..30
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 165..172
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 220..261
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 451..499
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 456..465
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 505..510
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 512..521
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 523..526
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 536..541
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 538..569
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 543..552
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 554..561
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 575..580
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 582..591
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 602..611
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
FT DISULFID 608..686
FT /evidence="ECO:0000256|PIRSR:PIRSR002512-1"
SQ SEQUENCE 767 AA; 87395 MW; 67A3660F8D2D7CBC CRC64;
MHADSCERCL GAHLDCAWCT DKAYQVRWRC FARSQLLKFN CSENEIYENQ PVLDLLQERP
LKDYQTSDDQ AVQVTPQRAY LKLVKGNTQS IKLRYRTARN NPLDLYVLMD LTWTMRDDKE
TLEELGTQLT QTLRNLTENY RLGFGSFADK PTMPMVLPQF KENPCALVGA VCEPTYGYRH
QLSLTEDIRA FTAAVAGSKI TGNLDNLEGG LDALMQVIVC PKEIGWQQQA RKVVILVTDG
FMHLAGDGLL AGIIERNDRQ CHLNRAGEYT GSLEYDYPSL EEVYRELLRR KINVIFAVTK
EVVSTYRELS ALMKEISYVD ILSADSSNIL ELIKKSYESL IKRTQFDDNS PDFIHLEYYT
DCAGQFPTLR KRNYCNNLSL GKEIEFYVNV TLKEYPPNGV LTHKIRVEET SLNEYMELDV
ELQRPCPCQE EAEPQSEEGR FQCLDQGYLY CGMCVCDEGW TGTYCMCPTD HTNITTNEAL
LLQCREPNPD DGGRSAQVCS NRGECDCGSC NCDPGYTGDY CECRECQDCD EDRADCYCGK
CVCKYGWSGN RCNCKEDTDA CLGPTGELCS QRGTCDCGEC SCDDPFLGKF CEIDPEKDNK
LCQFYEPCVT CLIEQRQGMG ACDNLSEICT SLDSQERFTY SFVAELEADV RCLVRIVNKH
GIQCDSYFGY QVIDHANYLS IQATDCEPLD YVALFGFISG FTLLIGLLLI FLFIWCIRRK
DAREYARFEE EWAKRVSQEN PLYRDPVGRY VVPKALSTKF DENPFAS
//
