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Database: UniProt
Entry: B4HFH7_DROSE
LinkDB: B4HFH7_DROSE
Original site: B4HFH7_DROSE 
ID   B4HFH7_DROSE            Unreviewed;      1903 AA.
AC   B4HFH7;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   SubName: Full=GM24683 {ECO:0000313|EMBL:EDW41208.1};
GN   Name=Dsec\GM24683 {ECO:0000313|EMBL:EDW41208.1};
GN   ORFNames=Dsec_GM24683 {ECO:0000313|EMBL:EDW41208.1};
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:EDW41208.1, 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).
CC   -!- SIMILARITY: Belongs to the TANC family.
CC       {ECO:0000256|ARBA:ARBA00038259}.
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DR   EMBL; CH480815; EDW41208.1; -; Genomic_DNA.
DR   RefSeq; XP_002030222.1; XM_002030186.1.
DR   SMR; B4HFH7; -.
DR   STRING; 7238.B4HFH7; -.
DR   EnsemblMetazoa; FBtr0207668; FBpp0206160; FBgn0179546.
DR   HOGENOM; CLU_001464_1_1_1; -.
DR   OMA; SGDHPHQ; -.
DR   PhylomeDB; B4HFH7; -.
DR   Proteomes; UP000001292; Unassembled WGS sequence.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:EnsemblMetazoa.
DR   GO; GO:0005911; C:cell-cell junction; IEA:EnsemblMetazoa.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0030018; C:Z disc; IEA:EnsemblMetazoa.
DR   GO; GO:0050839; F:cell adhesion molecule binding; IEA:EnsemblMetazoa.
DR   GO; GO:0008307; F:structural constituent of muscle; IEA:EnsemblMetazoa.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0061327; P:anterior Malpighian tubule development; IEA:EnsemblMetazoa.
DR   GO; GO:0007298; P:border follicle cell migration; IEA:EnsemblMetazoa.
DR   GO; GO:0007520; P:myoblast fusion; IEA:EnsemblMetazoa.
DR   GO; GO:0045214; P:sarcomere organization; IEA:EnsemblMetazoa.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR001841; Znf_RING.
DR   PANTHER; PTHR24166; ROLLING PEBBLES, ISOFORM B; 1.
DR   PANTHER; PTHR24166:SF55; ROLLING PEBBLES, ISOFORM B; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 5.
DR   PROSITE; PS50088; ANK_REPEAT; 7.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}; Reference proteome {ECO:0000313|Proteomes:UP000001292};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          327..364
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REPEAT          1380..1412
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1413..1445
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1524..1556
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1557..1582
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1591..1623
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1624..1656
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          1657..1689
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          123..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          552..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          809..831
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1824..1851
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        123..140
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..594
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        817..831
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1903 AA;  204982 MW;  4A039E0468100D45 CRC64;
     MPSLQQIAFA TEGDQSELQT PPLPINPPPK VMANGIVYGF RTRHLSCIEE NDSDSLHGSS
     IPHAYDMMQQ ADETFQKLNA NEEQDESGSE DGGLENMDDT IAMIDESRLL EADYLDELVA
     EEQLQEQDED EEESSDLVDS GNVEEDFWQP SFNRNDIMMT SVYGALNGSL TSEVTSTATP
     GYSECATPRK EAEPVYATPE KRRASNRSFD STCASLTSSL YGGSMNSSLD LKYSSLGGGD
     LVSGGISGTS TLRGTSVPPM DLSMMSSDGV SALDWGSASV SCVLDSGDGN PAEELNEEMA
     AKCLSAAESD LQSIRRLLEH DASGSVCPSC RISFDKGKRR KLIDTCGHER CYSCMFRNDQ
     CPMCMNSSLK DVDGANAQGY DTGIGGSTST IVSPLGSPQP QLRSHAQRNA ALARYMQQHR
     QESQSPDYHH RYASNGKLPR AAALSSNGNG FTTGTTQTVT VDVHHQLGGG GGAAAAAKQL
     MANGIGSGIS GHSRSSSLSH NIHAAAYSEL SAAPPAFATP PTRRRFFNHK NLRSALTGGS
     GGGSGVGGGV GGAGGVGGGH RRTASNGGCP IDTASILSGD HTHQHHHRDN QPEGKETNAL
     NTSTCSDSAV TRRRRKNVSN HNLKTSARHG ASSENRLNRL SLAGTSVYAG HLSSLVFGKI
     KSLWSVNSSN SSEAGLNQLA GSDTIDHHSS FLNEKLQKDQ LHARLGLLLN DPGSNGNSSS
     SGSGCEPISA HSTTSTTSSS GVGAASTTTS GSSQNVSPEQ TLASGAGMLS GSQLSVATSH
     GVKEDALSLC GKFKAGCSML HVYEALPSKS RKGNVRRSTR GQQGSSSSAS AASAVGSRVT
     ASSLAAVQLA LKPLFFEVPL QEPDPPYVGR QWLVQQLSNI LLGTETRVVL INGQPGTGKT
     AFCLQLVEYS CFGRRQMQDD PDGIYSQLQL GAHCERMRGL ASHMVGYHFC QADANLTCQV
     PDFVHSLAAQ LCQAPQLTAY RDYLLSEPHL QDILSVRECI ADAERVMKLA ILEPLAHLHR
     AGKIPAKVAV IVVDALCEAE YHRPDHGHTI ASFLAQLTPH FPAWLKLVAT VRTQMLELVK
     APSYTQLTLD SWASSQALQQ DMLDYIGARL ADSPEIRMNI GGGGGQNSQS GSQPQTKFVS
     HLQSLSRGSM LYAKLILDLI ARGQLVIKSS SYKVLPVSLA QIFLLHFNLR FPTARSFEQA
     APILNICLAA LYPLTLDEIY YSMEALSHGR EALSWPDFMQ RFKLLDGFLI KRLDNTYMFF
     HSSLREWLMR RDEGESNKFL CDARLGHAGI AFRLSRLQAP LSPQLTLELG HHMLKAHLYG
     GTSLTLLSPR DLQSYWLAGA ADNISSSLGA LRNVYSPNLK VSRLVLLAGA SPNHRTDYMG
     GAPILCIAAH EGILPMVSLL LEFGADVGLT NSQGCTPLIL AAMRGHCDVV RPLVAAGSSL
     GQLDITQRCA LVHAARMGHL SVVKYLLACD WSPRPQSQDV TRSVALQQAL IGAAAQAHCK
     ILEDLLDLNE TEFDLDVNGM EPSSGELALT AAARHGCVDV VGILISRGAQ IDARNRQGYS
     ALWLAVKEGH WSVVEHLLQR GALLDEPLGQ TRKTPLMIAA EEGHLELVDL LLARGAQREA
     QDHEGFTALS WACLRGHLAA AKTLIEHGCN RHHEDHNGRT ALDLAAYQGA ASLVLYILEQ
     GGNLEHIDVH GMRPLDRAIA CRNIQAVQVF LRKGAKLGPT TWSMAMGKPE ILVILLNKLL
     EDGNVLYRKN RFQEAAHRYQ YALRKISGLE QLLERNAIFA QLRTNLLLNL SRCKRKLNEL
     DASIDLATQA IAQKPHSYEG YYARAKARME LGALNEALVD ANEAMQQAAQ SGVLCEVVEV
     LKRIQTELLT RISISSEDQT GRMSNIGGGA SVTYESHHEI TDL
//
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