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Database: UniProt
Entry: B4LDU2_DROVI
LinkDB: B4LDU2_DROVI
Original site: B4LDU2_DROVI 
ID   B4LDU2_DROVI            Unreviewed;      1500 AA.
AC   B4LDU2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   28-FEB-2018, entry version 74.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EDW68965.2};
GN   Name=Dvir\GJ12983 {ECO:0000313|EMBL:EDW68965.2};
GN   ORFNames=Dvir_GJ12983 {ECO:0000313|EMBL:EDW68965.2}, GJ12983
GN   {ECO:0000313|FlyBase:FBgn0200217};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
OC   Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
OC   Ephydroidea; Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:EDW68965.2, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:EDW68965.2, ECO:0000313|Proteomes:UP000008792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15010-1051.87 {ECO:0000313|Proteomes:UP000008792};
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.,
RA   Markow T.A., Kaufman T.C., Kellis M., Gelbart W., Iyer V.N.,
RA   Pollard D.A., Sackton T.B., Larracuente A.M., Singh N.D., Abad J.P.,
RA   Abt D.N., Adryan B., Aguade M., Akashi H., Anderson W.W.,
RA   Aquadro C.F., Ardell D.H., Arguello R., Artieri C.G., Barbash D.A.,
RA   Barker D., Barsanti P., Batterham P., Batzoglou S., Begun D.,
RA   Bhutkar A., Blanco E., Bosak S.A., Bradley R.K., Brand A.D.,
RA   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.,
RA   Daub J., David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H.,
RA   Edwards K., Eickbush T., Evans J.D., Filipski A., Findeiss S.,
RA   Freyhult E., Fulton L., Fulton R., Garcia A.C., Gardiner A.,
RA   Garfield D.A., Garvin B.E., Gibson G., Gilbert D., Gnerre S.,
RA   Godfrey J., Good R., Gotea V., Gravely B., Greenberg A.J.,
RA   Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A., Haerty W.,
RA   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.,
RA   Hubisz M.J., Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S.,
RA   Jeck W.R., Johnson J., Jones C.D., Jordan W.C., Karpen G.H.,
RA   Kataoka E., Keightley P.D., Kheradpour P., Kirkness E.F.,
RA   Koerich L.B., Kristiansen K., Kudrna D., Kulathinal R.J., Kumar S.,
RA   Kwok R., Lander E., Langley C.H., Lapoint R., Lazzaro B.P., Lee S.J.,
RA   Levesque L., Li R., Lin C.F., Lin M.F., Lindblad-Toh K., Llopart A.,
RA   Long M., Low L., Lozovsky E., Lu J., Luo M., Machado C.A.,
RA   Makalowski W., Marzo M., Matsuda M., Matzkin L., McAllister B.,
RA   McBride C.S., McKernan B., McKernan K., Mendez-Lago M., Minx P.,
RA   Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E., Negre B.,
RA   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.,
RA   Pesole G., Phillippy A.M., Ponting C.P., Pop M., Porcelli D.,
RA   Powell J.R., Prohaska S., Pruitt K., Puig M., Quesneville H.,
RA   Ram K.R., Rand D., Rasmussen M.D., Reed L.K., Reenan R., Reily A.,
RA   Remington K.A., Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H.,
RA   Rohde C., Rozas J., Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L.,
RA   Sanchez-Gracia A., Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C.,
RA   Schlenke T., Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M.,
RA   Sisneros N.B., Smith C.D., Smith T.F., Spieth J., Stage D.E.,
RA   Stark A., Stephan W., Strausberg R.L., Strempel S., Sturgill D.,
RA   Sutton G., Sutton G.G., Tao W., Teichmann S., Tobari Y.N.,
RA   Tomimura Y., Tsolas J.M., Valente V.L., Venter E., Venter J.C.,
RA   Vicario S., Vieira F.G., Vilella A.J., Villasante A., Walenz B.,
RA   Wang J., Wasserman M., Watts T., Wilson D., Wilson R.K., Wing R.A.,
RA   Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G., Yamamoto D.,
RA   Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E., Zhang P.,
RA   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.,
RA   An P., Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P.,
RA   Barry A., Bayul T., Berlin A., Bessette D., Bloom T., Blye J.,
RA   Boguslavskiy L., Bonnet C., Boukhgalter B., Bourzgui I., Brown A.,
RA   Cahill P., Channer S., Cheshatsang Y., Chuda L., Citroen M.,
RA   Collymore A., Cooke P., Costello M., D'Aco K., Daza R., De Haan G.,
RA   DeGray S., DeMaso C., Dhargay N., Dooley K., Dooley E., Doricent M.,
RA   Dorje P., Dorjee K., Dupes A., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Fisher S., Foley C.D., Franke A., Friedrich D.,
RA   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.,
RA   LeVine R., Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T.,
RA   Lokyitsang Y., Lubonja R., Lui A., MacDonald P., Magnisalis V.,
RA   Maru K., Matthews C., McCusker W., McDonough S., Mehta T., Meldrim J.,
RA   Meneus L., Mihai O., Mihalev A., Mihova T., Mittelman R., Mlenga V.,
RA   Montmayeur A., Mulrain L., Navidi A., Naylor J., Negash T., Nguyen T.,
RA   Nguyen N., Nicol R., Norbu C., Norbu N., Novod N., O'Neill B.,
RA   Osman S., Markiewicz E., Oyono O.L., Patti C., Phunkhang P.,
RA   Pierre F., Priest M., Raghuraman S., Rege F., Reyes R., Rise C.,
RA   Rogov P., Ross K., Ryan E., Settipalli S., Shea T., Sherpa N., Shi L.,
RA   Shih D., Sparrow T., Spaulding J., Stalker J., Stange-Thomann N.,
RA   Stavropoulos S., Stone C., Strader C., Tesfaye S., Thomson T.,
RA   Thoulutsang Y., Thoulutsang D., Topham K., Topping I., Tsamla T.,
RA   Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D., Zimmer A.,
RA   Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J., Chin C.,
RA   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; CH940647; EDW68965.2; -; Genomic_DNA.
DR   RefSeq; XP_002046623.2; XM_002046587.2.
DR   EnsemblMetazoa; FBtr0228908; FBpp0227400; FBgn0200217.
DR   GeneID; 6623338; -.
DR   KEGG; dvi:Dvir_GJ12983; -.
DR   FlyBase; FBgn0200217; Dvir\GJ12983.
DR   eggNOG; KOG2408; Eukaryota.
DR   eggNOG; ENOG410XPZ3; LUCA.
DR   InParanoid; B4LDU2; -.
DR   KO; K19511; -.
DR   OrthoDB; EOG091G0236; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   Bgee; FBgn0200217; -.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:EnsemblMetazoa.
DR   GO; GO:0006909; P:phagocytosis; IEA:EnsemblMetazoa.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd09826; peroxidasin_like; 1.
DR   Gene3D; 1.10.640.10; -; 1.
DR   Gene3D; 2.60.40.10; -; 4.
DR   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR010255; Haem_peroxidase.
DR   InterPro; IPR019791; Haem_peroxidase_animal.
DR   InterPro; IPR037120; Haem_peroxidase_sf.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR034828; Peroxidasin.
DR   InterPro; IPR034824; Peroxidasin_peroxidase.
DR   InterPro; IPR001007; VWF_dom.
DR   PANTHER; PTHR11475:SF58; PTHR11475:SF58; 3.
DR   Pfam; PF03098; An_peroxidase; 1.
DR   Pfam; PF07679; I-set; 3.
DR   Pfam; PF13855; LRR_8; 2.
DR   Pfam; PF00093; VWC; 1.
DR   PRINTS; PR00457; ANPEROXIDASE.
DR   SMART; SM00409; IG; 4.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00369; LRR_TYP; 5.
DR   SMART; SM00214; VWC; 1.
DR   SUPFAM; SSF48113; SSF48113; 1.
DR   SUPFAM; SSF48726; SSF48726; 4.
DR   PROSITE; PS50835; IG_LIKE; 4.
DR   PROSITE; PS51450; LRR; 6.
DR   PROSITE; PS50292; PEROXIDASE_3; 1.
DR   PROSITE; PS01208; VWFC_1; 1.
DR   PROSITE; PS50184; VWFC_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008792};
KW   Disulfide bond {ECO:0000256|SAAS:SAAS01003558};
KW   Leucine-rich repeat {ECO:0000256|SAAS:SAAS01000947};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008792};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     24       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        25   1500       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5006457112.
FT   DOMAIN      239    329       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      364    452       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      457    546       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN      554    592       Ig-like. {ECO:0000259|PROSITE:PS50835}.
FT   DOMAIN     1432   1493       VWFC. {ECO:0000259|PROSITE:PS50184}.
FT   COILED     1383   1410       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1500 AA;  168100 MW;  71DBB1DC7D4843A6 CRC64;
     MMHSLWPLTV LCLCLASLLQ LTAGQWVHCP AGCTCLARTV RCIRARLKVL PQLPQDTQVL
     DLRFNQFEEL PPMAFNGLGQ LTTLFLNDNQ LAYVHEDAFK GLTALRFLYL NKNQLSRLPA
     SIFQHLPRLE ALYLEDNDIW QLPAGLFDNL PHLHRLFLHN NKLNSLPQDM FNKLHSLKRL
     RLDGNPIDCN CGVYSLWRRW HLDAQRQLVS ITLTCAQPVA LQRQSFSSLT ESHFHCAKPQ
     LLVGPQDMLA SEGDTVDMLC EVAGQPRPEL IWMQNTNEIG VELAPHMLVL PSGALRINGV
     TPNDIGIYEC IARNEMGEIK SQPVRMLVSS NADNSLDSLH GHVENASGSN QVWAADVDAT
     PAPPRFIQQP QDQIVALHGA GHVLLDCAAS GWPQPDIQWF VNGRQLTQST SQLQLLANGS
     LALLQPSQLT AGTYRCEAHN RLGSVQATAR IEVKDLPEIL MAPQNQTIKL GKAFVLECDA
     DGNPLPSITW QFNGQPLASD GASADLLLEN ENTELVVSVA KQQHAGVYRC TASNENGEVS
     AEATIKVEQS QSPPRLAIEP SNLVAITGTT IELPCQAEQP EDGMQIVWRR DGRLIDPNVQ
     LTEKYCAAMS KQKPHKRNNV DLAPGDRYVR IAFAEAAKEI DLAINNTLDM LFSNRSTRGP
     PNYGELLRVF RFPTGQARQL ARAAEIYERT LVNIRKHVQR GDNLTMESEQ YEFRDLLSRE
     HLHLVAELSG CMEHREMPNC TDMCFHSRYR SIEGTCNNLM HPTWGASLTA FRRLAPPIYE
     NGFSMPVGWT KGLMYAGHPK PSARLVSTSL VATKDITPDA RITHMVMQWG QFLDHDLDHA
     IPSVSSESWD GVDCKKTCEF APPCYPIEVP PNDPRVKNRR CIDVVRSSAI CGSGMTSLFF
     DSVQHREQIN QLTSYIDASQ MYGYNTAFAQ ELRNLSSDEG LLRVGVHFPN QKDMLPFAAP
     QDGMDCRRNL DENQMNCFVS GDIRVNEQVG LLAMHTVWMR EHNRIAIKLR EINPHWDGDT
     LYQEARKIVG AQMQHITYKQ WLPLIIGESG MAQLGEYRGY DPQVNPSIAN EFATAALRFG
     HTIINPVLHR LNSSFQPIPQ GHLQLHKAFF APWRLAYEGG VDPLMRGMLA VPAKLKKPDQ
     NLNTELTEKL FQTAHAVALD LAAINIQRGR DHGIPGYNVY RKFCNLTVAA DFEDLAGEIT
     NADIRQKLRE LYGHPDNIDV WLGGILEDQV EGGKVGPLFQ CLLVEQFRRL RDGDRFYYEN
     PGVFLPEQLV QIKQANLGRV LCDVGDNFDQ VTENVFILAK HQGGYKPCED IPGINLYLWQ
     ECGNCNSLPP LFESFVPQTY TKRSQRRKRD AEQEVPTAES YDSPLEALYE VNEERVSGLE
     DLIGSFQKEL KKLHKKLRKL EDSCNAVDAE PVAQVVQLAP APQPAVVKPK RSHCVDDKGT
     TRLNNEVWTP DVCSKCNCFH GQVNCLRQQC GEVSCPPGIE PLTPPEACCP HCPVMSKPVD
//
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