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Database: UniProt
Entry: B4ICX2_DROSE
LinkDB: B4ICX2_DROSE
Original site: B4ICX2_DROSE 
ID   B4ICX2_DROSE            Unreviewed;      1425 AA.
AC   B4ICX2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=GM16744 {ECO:0000313|EMBL:EDW45398.1};
GN   Name=Dsec\GM16744 {ECO:0000313|EMBL:EDW45398.1};
GN   ORFNames=Dsec_GM16744 {ECO:0000313|EMBL:EDW45398.1};
OS   Drosophila sechellia (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN   [1] {ECO:0000313|EMBL:EDW45398.1, ECO:0000313|Proteomes:UP000001292}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rob3c / Tucson 14021-0248.25
RC   {ECO:0000313|Proteomes:UP000001292};
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; CH480829; EDW45398.1; -; Genomic_DNA.
DR   RefSeq; XP_002041582.1; XM_002041546.1.
DR   SMR; B4ICX2; -.
DR   STRING; 7238.B4ICX2; -.
DR   EnsemblMetazoa; FBtr0199729; FBpp0198221; FBgn0171657.
DR   GeneID; 6617255; -.
DR   KEGG; dse:6617255; -.
DR   HOGENOM; CLU_003533_0_0_1; -.
DR   OMA; TDNKHTL; -.
DR   OrthoDB; 3795301at2759; -.
DR   PhylomeDB; B4ICX2; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0016327; C:apicolateral plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0005911; C:cell-cell junction; IEA:EnsemblMetazoa.
DR   GO; GO:0098592; C:cytoplasmic side of apical plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0036375; C:Kibra-Ex-Mer complex; IEA:EnsemblMetazoa.
DR   GO; GO:0120219; C:subapical part of cell; IEA:EnsemblMetazoa.
DR   GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:EnsemblMetazoa.
DR   GO; GO:0019900; F:kinase binding; IEA:EnsemblMetazoa.
DR   GO; GO:0007298; P:border follicle cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0001751; P:compound eye photoreceptor cell differentiation; IEA:EnsemblMetazoa.
DR   GO; GO:0032456; P:endocytic recycling; IEA:EnsemblMetazoa.
DR   GO; GO:0097009; P:energy homeostasis; IEA:EnsemblMetazoa.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:EnsemblMetazoa.
DR   GO; GO:0045571; P:negative regulation of imaginal disc growth; IEA:EnsemblMetazoa.
DR   GO; GO:0046621; P:negative regulation of organ growth; IEA:EnsemblMetazoa.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:EnsemblMetazoa.
DR   GO; GO:0035332; P:positive regulation of hippo signaling; IEA:EnsemblMetazoa.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:EnsemblMetazoa.
DR   GO; GO:0045595; P:regulation of cell differentiation; IEA:EnsemblMetazoa.
DR   GO; GO:0007096; P:regulation of exit from mitosis; IEA:EnsemblMetazoa.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd13185; FERM_C_FRMD1_FRMD6; 1.
DR   CDD; cd17101; FERM_F1_PTPN13_like; 1.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
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; IPR000299; FERM_domain.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR041781; FRMD6-FERM_C.
DR   InterPro; IPR047145; FRMD6-like.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR13429; FERM DOMAIN (PROTEIN4.1-EZRIN-RADIXIN-MOESIN) FAMILY; 1.
DR   PANTHER; PTHR13429:SF13; PROTEIN EXPANDED; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001292}.
FT   DOMAIN          26..399
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   REGION          176..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          520..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..732
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          816..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          939..964
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1001..1024
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1191..1273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1345..1398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        689..710
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..732
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        816..851
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        852..877
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1001..1021
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1196..1248
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1250..1264
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1345..1379
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1425 AA;  153330 MW;  676B956BE6F9EC66 CRC64;
     MRAFCTVSAP LEVCASSAEQ LSPGSRFLAL RLLGQQQPKT LYFLVDAKSR VREVYTQTCL
     HFATQGMLDT ELFGLAVLID GEYMFADPES KLSKYGPKSW RSSHTHGLDA NGRPLLELHF
     RVQFYIESPF MLKDETSRHN YYLQLRHNIL QRDLPREQAE QALVFLAGLA LQADLGDAPP
     GSSNSKDDSG EETLASPSNG GRGLSATTTL PKISKRANER MLRLSTYVAS TSKRETIPLP
     PTLPPNGADY YRIEDYLPSG LHTPWARSAM RACHREHLGM ATAEAELLYI QQACSLHETI
     NAHTYRMRLA KSEQGSGSAW FVVYAKGIKI LGGESNNSSS NPETTTFLWP NITKLSFERK
     KFEIRSGESR ITLYAASDEK NKLLLTLCKD THQWSMKLAA RLKEVSKREE EEAAESQRLH
     ASYACSRSLL LPYKSKNEQR ISVISSTSSN TTSGIVSDRV HSEDELEIMI NTPPAPLAAP
     STESLALAHL LDRPSVSRQT SSVGQMSLKD LEEQLAALSV RPQDASSNGA TIVTNSSVQK
     NSMGTTANDS STATDSPSSQ HNIGSQCSST CSTVVVTSPV NGAGSSSSGA PIPVHSTSSS
     LELGFSHTAQ NSALSETSPD DFLSTSAREE TESVSGASGV YTLAHGTPPT ETSGVYTMHS
     SELTGQSSEI AESEKSSHYG MFQPQKLDEA HVPHPDSVDG KKKEDFRPRS DSNVSTGSSF
     RGDGSDPTDN KHSLLSAEEL TNLIVGRGTY PSRKTVSSSL HSDCDYVTLP LGDQGEEEVD
     QPPAPPPPYS ARHEKTGLCG PPIAKPIPKP IAVVAPKPDS PPCSPPVPPA PLPAPPPAIR
     RRDPPPYSIS SKPRPTSLIS VSSLANPAPS AAGSMSSLKS EEVTARFITT RPQISILKAH
     TSLIPDGAKP SYAAPHHCSS VASSNGSVCS HQLSQQSLHN SNYAGGSQAS LHHHHVPSHH
     RHSGSAAIGI PIPYGLHKST ASLHHQQSCV LLPVIKPRQF LAPPPPSLPR QPPPPPPPNH
     HHLAGHLYGR EMAKKQLELY QQQLYSDVDY VIYPIQDPAV SQQEYLDAKQ GSLLAAMAQA
     APPPPHHPYL AMQVSPAIYR STPYLPVALS THSRYASTQN LSDTYVQLPG PGYSPLYSPS
     MVSLCSSYEP PPPPPLHPAA LAAAAAAGAS SSSSSMFARS RSDDNILNSL DLLPKGKRLP
     PPPPPPYVNR RLKKPPMPAP SEKPPPIPSK PIPSRISPIP PRKPPTLNPH HANSPLTKTS
     SGAQWAGERP RPDLGLGLGL NRGNNSILAQ LQASMAQSHA QAQAQALDIA LLREKSKHLD
     LPLISALCND RSLLKQTKVV INPKTGQEMP TSSAQPSGAT TNGVANSSAG TGTLSKARKG
     STVSHRHPQD KLPPLPVQQL AEANNYVIDP AVMMKQQQQQ HNKTS
//
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