ID B4J8P6_DROGR Unreviewed; 1525 AA.
AC B4J8P6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 105.
DE SubName: Full=GH21371 {ECO:0000313|EMBL:EDW01313.1};
GN Name=Dgri\GH21371 {ECO:0000313|EMBL:EDW01313.1};
GN ORFNames=Dgri_GH21371 {ECO:0000313|EMBL:EDW01313.1};
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222 {ECO:0000313|Proteomes:UP000001070};
RN [1] {ECO:0000313|EMBL:EDW01313.1, ECO:0000313|Proteomes:UP000001070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000313|Proteomes:UP000001070};
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 -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins.
CC {ECO:0000256|RuleBase:RU004357}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell
CC membrane {ECO:0000256|RuleBase:RU003318}; Single-pass type I membrane
CC protein {ECO:0000256|RuleBase:RU003318}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; CH916367; EDW01313.1; -; Genomic_DNA.
DR RefSeq; XP_001986446.1; XM_001986410.1.
DR SMR; B4J8P6; -.
DR STRING; 7222.B4J8P6; -.
DR EnsemblMetazoa; FBtr0156785; FBpp0155277; FBgn0128833.
DR GeneID; 6559498; -.
DR KEGG; dgr:6559498; -.
DR eggNOG; KOG3594; Eukaryota.
DR HOGENOM; CLU_247555_0_0_1; -.
DR InParanoid; B4J8P6; -.
DR OMA; EQPENTY; -.
DR OrthoDB; 3667774at2759; -.
DR PhylomeDB; B4J8P6; -.
DR Proteomes; UP000001070; Unassembled WGS sequence.
DR GO; GO:0043296; C:apical junction complex; IEA:EnsemblMetazoa.
DR GO; GO:0016342; C:catenin complex; IEA:EnsemblMetazoa.
DR GO; GO:0005938; C:cell cortex; IEA:EnsemblMetazoa.
DR GO; GO:0030175; C:filopodium; IEA:EnsemblMetazoa.
DR GO; GO:0055037; C:recycling endosome; IEA:EnsemblMetazoa.
DR GO; GO:0005914; C:spot adherens junction; IEA:EnsemblMetazoa.
DR GO; GO:0008013; F:beta-catenin binding; IEA:EnsemblMetazoa.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017022; F:myosin binding; IEA:EnsemblMetazoa.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0045176; P:apical protein localization; IEA:EnsemblMetazoa.
DR GO; GO:0008356; P:asymmetric cell division; IEA:EnsemblMetazoa.
DR GO; GO:0007409; P:axonogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0007298; P:border follicle cell migration; IEA:EnsemblMetazoa.
DR GO; GO:0007420; P:brain development; IEA:EnsemblMetazoa.
DR GO; GO:0035147; P:branch fusion, open tracheal system; IEA:EnsemblMetazoa.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:EnsemblMetazoa.
DR GO; GO:0035212; P:cell competition in a multicellular organism; IEA:EnsemblMetazoa.
DR GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0030031; P:cell projection assembly; IEA:EnsemblMetazoa.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IEA:EnsemblMetazoa.
DR GO; GO:0050832; P:defense response to fungus; IEA:EnsemblMetazoa.
DR GO; GO:0071907; P:determination of digestive tract left/right asymmetry; IEA:EnsemblMetazoa.
DR GO; GO:0036099; P:female germ-line stem cell population maintenance; IEA:EnsemblMetazoa.
DR GO; GO:0008354; P:germ cell migration; IEA:EnsemblMetazoa.
DR GO; GO:0035262; P:gonad morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0007506; P:gonadal mesoderm development; IEA:EnsemblMetazoa.
DR GO; GO:0008258; P:head involution; IEA:EnsemblMetazoa.
DR GO; GO:0035099; P:hemocyte migration; IEA:EnsemblMetazoa.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:EnsemblMetazoa.
DR GO; GO:0001748; P:insect visual primordium development; IEA:EnsemblMetazoa.
DR GO; GO:0035160; P:maintenance of epithelial integrity, open tracheal system; IEA:EnsemblMetazoa.
DR GO; GO:0098730; P:male germline stem cell symmetric division; IEA:EnsemblMetazoa.
DR GO; GO:0016318; P:ommatidial rotation; IEA:EnsemblMetazoa.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:1903688; P:positive regulation of border follicle cell migration; IEA:EnsemblMetazoa.
DR GO; GO:0007435; P:salivary gland morphogenesis; IEA:EnsemblMetazoa.
DR GO; GO:0007379; P:segment specification; IEA:EnsemblMetazoa.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:EnsemblMetazoa.
DR GO; GO:0007370; P:ventral furrow formation; IEA:EnsemblMetazoa.
DR GO; GO:0042060; P:wound healing; IEA:EnsemblMetazoa.
DR GO; GO:0045186; P:zonula adherens assembly; IEA:EnsemblMetazoa.
DR CDD; cd11304; Cadherin_repeat; 6.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 7.
DR Gene3D; 2.10.25.10; Laminin; 1.
DR Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR InterPro; IPR039808; Cadherin.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR000233; Cadherin_Y-type_LIR.
DR InterPro; IPR027397; Catenin-bd_sf.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24027; CADHERIN-23; 1.
DR PANTHER; PTHR24027:SF422; NEURAL-CADHERIN 2-RELATED; 1.
DR Pfam; PF01049; CADH_Y-type_LIR; 1.
DR Pfam; PF00028; Cadherin; 4.
DR Pfam; PF02210; Laminin_G_2; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 7.
DR SMART; SM00282; LamG; 1.
DR SUPFAM; SSF49313; Cadherin-like; 8.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00232; CADHERIN_1; 4.
DR PROSITE; PS50268; CADHERIN_2; 7.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell adhesion {ECO:0000256|RuleBase:RU003318};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001070};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003318};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1345..1365
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 101..207
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 208..313
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 344..424
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 424..534
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 546..635
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 635..747
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 757..858
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1106..1140
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1141..1329
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1130..1139
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1525 AA; 171631 MW; F0DA5973B23815BF CRC64;
MSLQSNNNNN NNNKINNNNT INANPAQQQP HQQHKRKCRR QTTTTNTTTT NRTCPLLPRP
LLALGLIILL HIPALDALVS SSSPLRYDSF AGDNRKPAFK NCAEYAPSVK EEQPENTYVF
TVQAVDPDPN QEITYSLVQS AFDRPKFVIH PNSGVIMTAH TFDRDEPIHE KFVFVTVQAT
DNGLPPLDDV CTFNVTIEDI NDNPPVFNKA RYDESMSENT ILDAVVMSIS ASDFDDRNNS
IVEYEILRER DFQYFRIDKE SGIIYLHRPI DRRPGQTYTI NVRAYNIVPD PLQEAHIEVR
IRVVESSIKP PSFVDPIDEP IYLKEDLKNF SQPIATLRAV SNMPDKPEVI FELITGRTEP
TNNKNTFVFN QIGNEVTIKL GKMLDYEAIT DYTLTMSVRN TFELATEHQI KIKVEDVNDN
IPFFTEVKSG TILENEPPGT PVMQVRAFDM DGTPANNIIT FELADNTDYF AIDPQTGNIT
ALTTFDREER DFYNVKVSAT DNSPSSLFNN GDHNHGYQVF RISIGDKNDH KPHFQQTTYL
ADKLLEDANT NYEVIEVKAE DEDNASQIVY SIESGNVGDA FKIGLKTGKI TVNQRLDYET
ITEYELKVRA FDGIYDDYAT VVVKIEDVND NPPLFKKEYS ITIQEGPVQS NECILIIEAY
DPDIKDRTAD QHITYSIVKE DHKRLLTIDN SGCLRLIQPL DRDPPNGHKS WQVLISASDQ
DGVGTTLKSV KPVIITLEDI NDNAPFLINQ MPVIWQENRN PGQVVQLLAN DYDEPQNGPP
FTFGIDSDAS PDIKTKFSID NDYLFANVQF DREMQKEYFI PIRISDAGIP KQSSVSILHL
IIGDVNDNAM SEGSSRIFMY NYKGEAPDTD IGRVFVDDDD DWDLDDKHFQ WKSGIPHEQF
RLNPSTGMIT ILEGTSEGEY MLEFTVTEDS TLIPRHSVDA DVTVLVRELP EEAVDKSGSI
RFYNITKEEF ISVPRDVLAD DAFSLKDRLQ HSLAKLFNTS VSNVDVFTVL QNENRTLDVR
YSAHGSPYYA PEKLNGMVAQ TQQRLENDLD LQMLMVNIDE CLIERLKCES SCTNELHKSS
VPYMIYSNTS SFVGVNAFVQ AQCVCDALPP ISPCLNGGSR RYGENDACDC IDGFTGPHCE
LVSVGFYGNG YAFYEPISAC DNTRISLEIA PQHEQGLIMY LGPLNYNPLL PLTDFLSLEL
DKGYPVLSVD YGSGMVRIKH QHIQLQPGRS YQLDIILQRA SIEMTVDNCR LSTCMSLGAP
QGPNEFLNVN SPLQLGGTPV DLAQLGRQLN WTHTPNQQGF FGCVRNLTIN ERTYNLGMPS
LSRNIDSGCQ RAVAVAVSFG IDRNFIIAII TCIALLLIIL LAVVVQKKQK NGWHEKDIDD
IRETIINYED EGGGERDTDY DLNVLRTQPF YEEKLYKDPH ALHAAAGMRD PNDIPDIGDF
LGGKKENCDR DTGANTVDDV RHYAYEGDGN SDGSLSSLAS CTDDGDLNFD YLSNFGPRFR
KLADMYGEEP SDTDSNVDDD QGWRI
//