ID B4IWM4_DROGR Unreviewed; 2134 AA.
AC B4IWM4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=GH15312 {ECO:0000313|EMBL:EDV96250.1};
GN Name=Dgri\GH15312 {ECO:0000313|EMBL:EDV96250.1};
GN ORFNames=Dgri_GH15312 {ECO:0000313|EMBL:EDV96250.1};
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:EDV96250.1, 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).
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DR EMBL; CH916366; EDV96250.1; -; Genomic_DNA.
DR RefSeq; XP_001983902.1; XM_001983866.1.
DR SMR; B4IWM4; -.
DR STRING; 7222.B4IWM4; -.
DR eggNOG; KOG4261; Eukaryota.
DR HOGENOM; CLU_000364_1_1_1; -.
DR InParanoid; B4IWM4; -.
DR OMA; VDMTQHY; -.
DR PhylomeDB; B4IWM4; -.
DR Proteomes; UP000001070; Unassembled WGS sequence.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0005925; C:focal adhesion; IEA:InterPro.
DR GO; GO:0001726; C:ruffle; IEA:InterPro.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR GO; GO:0030182; P:neuron differentiation; IEA:UniProt.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd10569; FERM_C_Talin; 1.
DR CDD; cd17089; FERM_F0_TLN; 1.
DR CDD; cd17090; FERM_F1_TLN; 1.
DR CDD; cd12150; talin-RS; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.120.230; Alpha-catenin/vinculin-like; 5.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.20.1420.10; Talin, central domain; 6.
DR InterPro; IPR036723; Alpha-catenin/vinculin-like_sf.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR032425; FERM_f0.
DR InterPro; IPR035964; I/LWEQ_dom_sf.
DR InterPro; IPR002404; IRS_PTB.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR037438; Talin1/2-RS.
DR InterPro; IPR015224; Talin_cent.
DR InterPro; IPR036476; Talin_cent_sf.
DR InterPro; IPR049108; Talin_R4.
DR InterPro; IPR015009; Vinculin-bd_dom.
DR PANTHER; PTHR19981:SF1; RHEA, ISOFORM B; 1.
DR PANTHER; PTHR19981; TALIN; 1.
DR Pfam; PF16511; FERM_f0; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF02174; IRS; 1.
DR Pfam; PF09141; Talin_middle; 1.
DR Pfam; PF21692; Talin_R4; 2.
DR Pfam; PF08913; VBS; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM01244; IRS; 1.
DR SUPFAM; SSF109880; A middle domain of Talin 1; 1.
DR SUPFAM; SSF47220; alpha-catenin/vinculin-like; 4.
DR SUPFAM; SSF109885; I/LWEQ domain; 3.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000001070}.
FT DOMAIN 88..412
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1942..1963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1807..1855
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1942..1958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2134 AA; 231684 MW; A4330FDC6D6E1B5F CRC64;
MSTLSLRIQL EGGRVTKTIQ FQPNTTVFDA CKIIRDKFAE AVQGQPSEYG LFISDDQNQQ
GVWLEAGRTL GYYILHNQDT LEYRRKLRTL RVRMLDGAVK TILVDDTQPV SQLMVVICTK
IGITNHEEYG LVREDNEAQN ENLPDNKFGT LTLKRKFTEK DRDAKMESLR KKLKTDDEMN
WVDVGRTLRE QGIDESETVL LRRRFFFSDQ NIDSRDPVQL NLLYVQARDA ILDGTHPVTQ
DKACEFAGIQ VHIQFGPHNE AKHKPGFLDL KDFLPQSYVR VKNIEKKIFS EHKRHSELSE
IDAKVLYTKT ARELPTYGVT FFLVKEKMNG KNKLVPRLLG VTKDSVLRLD ERTKEILISW
PLTTVRRWGA SPNTFTLDFG DYANQYYSVQ TTEAEQIVQL IAGYIDIILK KKRTKDHFGI
EGDEGSTMVE ESVAPSKATF LQHETNRVEK LNLESLAHPG VMRPYDGERT FTQNEVQTVQ
YGAFVGQVNH AHQPPTSNEV RITSVNLTEP QRALHGYISA GQDVLIRADE ELRTKAPIQE
LGSDLRSIEW RENTLDTSKQ AVSSHVATMS AATAQIITAS HPDEVDTEAI SASVSQIAQT
IPEVTKEVRL IAALMENDTN GDQLLEAARN LCNAFSDLLK AAEPESKEPP QHLINAASRV
GEATTHVLST IAEEEAPESR DLHDMLLALA KAVANTTAAL VLRAKNIAAS CEDDEARNRV
IGAASQCALA TSQLVACAKV VAPTLHNAAC REQLEAAARN VARAVNSLCQ VCNEASNDPK
LKADLLDAAR DVSKSLMEML EHVKLSTREH ANRTSQELSP VENVIIGTDI LVSTNDPQEM
VRHARTLGQT TAQLIQSIKG EADQQEDADM QRRLLSAAKQ LADATTKLVE AARLCSSNPH
DSDNQNALRR AAEELREITT SAANTPAMKR NLIQRLEFCS KQAATAATQC ISAAQNAVQH
SQDHQTKESL LQDCKRVADT IPRLVTSVKT THAQPDDAHA QLNLIEAAEQ FIEPALQVSK
SSRALQPTVT DIPAATQLSK SALHLGQSVS ELHSVAQRTR DACGGQELES ALEAVRKLHH
VLDDTRQAAL AGQLRPLPGD TVENTADDLR KSAKNVGIAL SQLLSSVLQG QRSYAGAAGR
DTALALGDFT KSVHGVAATT QNPVIIDCAD DVVTSSAQLI EQAQRTLQGV SDPIALTQAG
RDVTSALSRT VDCIPGQREV DAALRNVSDL SEILSVSEFP PSNRPYAELQ SELKQVAEQL
SSAGGQIVQS YASPALLADS SQNFAANYRD LLSVSMQMAG QTQTDEPVRS QMIDSLRNVS
TQSCSLLSTA KSIAADPGQP NAKNLLHAAA RSVTESINQL VDASIQSAPG QKECDNAMRN
IEALRLMLDY PHEPINEMGY FDCVEQATSK SRNLGYAISE MINNAKQSQH VEFSQSVNNV
NDSIQGLMES SSQAAYLIGV SHPSSVAGRP GIIDKAQLTW AYQGIRQHCD IVSSSQSGKP
QMISALTVIA KHTSYLCSIC RQASMNTNNP VAKNEFIVLA KRVATATSDL VQDIKAIEEQ
PTGGSRDRLV EPLLEAVKAV SQYASSPEFI SIPAKISAEG RKAQEPVIQA GRGVIDGVVE
MVKAAKSLAL SPDNPPVWQQ LSMHSTPVSE SVKRLVDNIR DKAPGQAQCE QVLHTLGTCT
RELDGCALAV NAQGLSRRRD NNLHGFSGQT LNSAAELLDK LEPIRVAGKN NAEQLGHAVG
EISRYVVPMV NGAIGACTHI VHSQQQMSLI NQTKSVVESA TTLVQAAKDS AGNPRATQAH
PRLDEAIDGT LEAIQELQQT VEKINAETGI VTGLMEQVNR AITRLTDKRQ SLLNASYSDT
FVDYQTRMVA TAKEIARLSN EMNAKSSVEP AALPQLAVDM TQHYQLLTQD SVGASTTTTS
QDVAMRIRST VIDLGRSVSS MIQSSAGGAS PNDASAQKEI ARNTREVSEK VAQVLAALQA
GSRGTQACIN AAHTVSGIIG DLDTTIMFAT AGTLHSDGDG SFADHREHIL QTAKALVEDT
KVLVTGAAGT QDQLANAAQN AVSTITQLAE AVKRGACSLG SSQPDSQVMV INAVKDVASA
LGDLINCTKL ASGKPIHDPS MQGLKESARF SQFS
//