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Database: UniProt
Entry: A0A0Q9X585_DROMO
LinkDB: A0A0Q9X585_DROMO
Original site: A0A0Q9X585_DROMO 
ID   A0A0Q9X585_DROMO        Unreviewed;      2512 AA.
AC   A0A0Q9X585;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Uncharacterized protein, isoform F {ECO:0000313|EMBL:KRG00612.1};
GN   Name=Dmoj\GI23883 {ECO:0000313|EMBL:KRG00612.1};
GN   ORFNames=Dmoj_GI23883 {ECO:0000313|EMBL:KRG00612.1};
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230 {ECO:0000313|EMBL:KRG00612.1, ECO:0000313|Proteomes:UP000009192};
RN   [1] {ECO:0000313|EMBL:KRG00612.1, ECO:0000313|Proteomes:UP000009192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
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; CH933806; KRG00612.1; -; Genomic_DNA.
DR   RefSeq; XP_015021718.1; XM_015166232.1.
DR   SMR; A0A0Q9X585; -.
DR   EnsemblMetazoa; FBtr0423247; FBpp0381208; FBgn0146608.
DR   GeneID; 6572144; -.
DR   OrthoDB; 2891597at2759; -.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0045202; C:synapse; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd04031; C2A_RIM1alpha; 1.
DR   CDD; cd04028; C2B_RIM1alpha; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR010911; Rab_BD.
DR   InterPro; IPR039032; Rim-like.
DR   InterPro; IPR017455; Znf_FYVE-rel.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR12157:SF21; RAB3 INTERACTING MOLECULE, ISOFORM F; 1.
DR   PANTHER; PTHR12157; REGULATING SYNAPTIC MEMBRANE EXOCYTOSIS PROTEIN; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00239; C2; 2.
DR   SMART; SM00228; PDZ; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50916; RABBD; 1.
DR   PROSITE; PS50178; ZF_FYVE; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009192};
KW   Synapse {ECO:0000256|ARBA:ARBA00023018};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00091}.
FT   DOMAIN          4..130
FT                   /note="RabBD"
FT                   /evidence="ECO:0000259|PROSITE:PS50916"
FT   DOMAIN          68..118
FT                   /note="FYVE-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50178"
FT   DOMAIN          509..598
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          823..944
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          2362..2480
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   REGION          141..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          606..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          676..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..1036
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1078..1197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1875..1959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2009..2070
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2129..2164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2188..2304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          19..56
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        157..176
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..268
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..384
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..763
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        790..810
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        972..1011
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1018..1032
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1082..1096
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1153..1194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1908..1957
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2129..2161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2217..2233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2242..2279
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2512 AA;  272860 MW;  12A20F61178FC88E CRC64;
     MDEMPDLSHL TPHERMQIEN VLMRQKQEEE KQNEIMRRKQ DEVVTLEMQI RQRSEQQKKA
     GVELDATCHI CLKTKFADGV GHICHYCNIR CCARCGGKVT LRSNKVIWVC ILCRKKQELL
     SKTGQWINKT AVQQDGFIRR IEPDGSSDIS QQAIVDPRDS ADKRPKLERT RSAAEKENLP
     MQRAGSMLRR QYSQQEQPTN RRLSVSDSGM EPLSPGQQQM QQQQLPQRQR MQPMNPQQAQ
     QYQLQQQQLQ QQQQQQLGYG QQQHPQRSGA YPEDDPRYYQ GELDGLMRQH PHLAHPSQVQ
     QQPQQQQQQQ PQQQQPQQHL IPQQQRFNAR QQHMQQQQQQ QHQQQQQQQQ PQQQQQQRML
     QQQQPYQGSS THAQIHSQPA QLGGGSGYQK APPLTRNLTI SGGHAMDATT YNQQQQQQQQ
     RRSLAGAQYA SQQQRSFSSS EEEFQSHLMA AQAQAQVQGH TVTAGSDYDG NFGVVQSVQT
     NLSPGDLQIH ANNPVNWQTS ADNTRMIGHM ILRKYYDGED ILGLKVNGGQ PVGLGGPCRA
     IVEKVKRGSV ADVEGCIRPG DEIIEWNGRS LHNKSADEVY DIIDESRLDA QVELIVGRSL
     LLPSSGAGSV DSGSSSNVSP SSACSGSGSS VTRRSSANFP HSGLASSMAA SAVVSSGGRY
     LQRKAPGVEA LELHRDKPSV LITSPGSPDL HTGGSNNGLR HRGAGIGSCS QQSQRLEASS
     HNHSHSHSHS HSYSSHSHSS SGSGSNSGSS SNSSATVAAS GGVHSATTAG HHHHCHPTAA
     SPPSHAHALP HPHPHPHSHS HSHAHAHSHH GHGMGVTTQP IPIEGRLQLK LGYDQTTLQL
     IVTLVCATGL SLRQSGAGRN PYAKVFLLPD RSQKSKRRTK TVGTTCEPRW GQTFFYSGLR
     RSDLNGRQLE VTLWDYVRYG ANDFIGEVVI DLAHHVLDDE AEWYQLQPHQ DSSHLLRDEG
     SDVECLILTP TDHLSPPSTM SRLSDSDTTS ECDIDGTTPG ASISSMGSSA SPPLFELDLN
     ERRSRRDMSP QGRKRVAGMM ARDYRTVSGI GQSYHNQSSA TTAGYYRRGG ANGVGSAIGP
     GGMSLSQRSH SAAPSDNYHG HQGHPGTGYG YRSSSPRRGS LSPPDDRYID YPVLPIHGSP
     NAAAYGGGGS GASAAAQTPQ QQRFQSRSAT ATPTGSPKKR QLPQVPQTSR SAMLRDRLGQ
     DFDERLASGS RFGRHRTRQP HHQATYRSTG MGGWERHYTG LSDSDLQSMD TRMRPRHSLS
     PDKDFMGEFG DSDMESVVSV TSSAFSTQSE RPRTSRGLSF PRNWRNLFGA QSSILGGAVG
     GPVTGLKVYP VEHHRANTIE VDDCDYLSSG GGAHQLLLLE QLEQLQQLAA LAAADSPPNT
     AALGGFSGAA SAVPPPPTTI PLPMTAPQQV LVTDTNSGEL IEQFFVEPAL MAEETPLNLE
     PHEPHLLTHS VYYSPHLPNT FIQPPLDLYQ RRHNGRQLDH APTIATATAT ANATTHANHT
     YALPGFEQFK RYTTPVMNLF RSSTTAPPAS AHDHAHTVSS SPSSYVGYVR DHLDKSCSHC
     QNGSQPVVLS TNTALATPGL AIGACTDPCC LADAHPHPQH KPIAYPYSAE QLLRRPSLSM
     YQPASTSEPS LPTMDPDPMC GECVDQHFLG GLIGPQLNLG VVPTYHVHTP TATAHRRANS
     QLAPPPPLPT QSVLRLSRQL SEDALVSAVP IAEATARAQP TSILKKPKLD RRRMFHEGQS
     RSLDYDDLHT KSWGRRRIRY EDEVAPHELM PHAYHPSEEQ LPSSRRYGSE TNIRQSYMGA
     NVDAANPLSH SHFLVTDDKI VTITYDSDVG WTRRGVAPSL FRGPHRRGVD ARNHMSLDLQ
     RTSQQKLYGP AAPYMKRRRN LPHPPSAQNA HNFSPMEAIG GGVGGGGAQN SGTYNSNNHN
     SSHYTNHNSH AASSVSSVSQ FHNNQQQQQQ QPQSIRQKGK EGIIAVNGLL ASASEQLTKS
     SGGSGGATSA AATAAATGNI VCDGNNANNA SSSSFANPPQ QQQQQQHHGV ANQPITTTNA
     SPNKRAPSSI HNTTTTTTTT TTNDANNLTH DATSTNLTQQ QQQQPPNTCT NLITNATTNT
     SSIDAATTTT TTTTTITTAT TATTTATNTT TTTTTTNTNN TNEPNATTTT TNANTNANTD
     ADADADAPID VIDWDAIDAM LDDDFSEYDK EKNGANEPSG AKSVDGGGGT EEKADGSLSD
     TTTDRKKCGN VDQERSPKGG SGMGKKSNST SQLSATDQYQ AQYLGSSSAS GSSTSHHHIT
     LPPPHPYYQR QSRGSAGSIQ RSVEVPPVPA VTRYSAGSIH SISSSEGSSF SPSLRNDGAL
     NEFVDGLGPG QLVGRQVLGA PSLGDIQLSL CHQKGFLEVE VIRARGLQQK PSSKMLPAPY
     VKVYLVSGKR CIDKMKTSTA RRTLDPLYQQ QLVFKQSYSG CVLQVTVWGD YGRIEKKVFM
     GVAQIMLDDL NLSNIVIGWY KLFGTTSLVS CPTNIGLGSR RSSIASLDSL KL
//
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