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Database: UniProt
Entry: A0A0Q9WMK4_DROVI
LinkDB: A0A0Q9WMK4_DROVI
Original site: A0A0Q9WMK4_DROVI 
ID   A0A0Q9WMK4_DROVI        Unreviewed;      2100 AA.
AC   A0A0Q9WMK4;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Uncharacterized protein, isoform B {ECO:0000313|EMBL:KRF81653.1};
GN   Name=Dvir\GJ17499 {ECO:0000313|EMBL:KRF81653.1};
GN   ORFNames=Dvir_GJ17499 {ECO:0000313|EMBL:KRF81653.1};
OS   Drosophila virilis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7244 {ECO:0000313|EMBL:KRF81653.1, ECO:0000313|Proteomes:UP000008792};
RN   [1] {ECO:0000313|EMBL:KRF81653.1, 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., 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   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; CH940649; KRF81653.1; -; Genomic_DNA.
DR   RefSeq; XP_015028417.1; XM_015172931.1.
DR   STRING; 7244.A0A0Q9WMK4; -.
DR   EnsemblMetazoa; FBtr0441827; FBpp0398337; FBgn0204669.
DR   GeneID; 6628873; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3509; Eukaryota.
DR   InParanoid; A0A0Q9WMK4; -.
DR   OrthoDB; 101939at2759; -.
DR   Proteomes; UP000008792; Unassembled WGS sequence.
DR   GO; GO:0009986; C:cell surface; IEA:EnsemblMetazoa.
DR   GO; GO:0031012; C:extracellular matrix; IEA:EnsemblMetazoa.
DR   GO; GO:0005615; C:extracellular space; IEA:EnsemblMetazoa.
DR   GO; GO:0097730; C:non-motile cilium; IEA:EnsemblMetazoa.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005201; F:extracellular matrix structural constituent; IEA:EnsemblMetazoa.
DR   GO; GO:0000902; P:cell morphogenesis; IEA:EnsemblMetazoa.
DR   GO; GO:0042052; P:rhabdomere development; IEA:EnsemblMetazoa.
DR   GO; GO:0010378; P:temperature compensation of the circadian clock; IEA:EnsemblMetazoa.
DR   CDD; cd00054; EGF_CA; 10.
DR   CDD; cd00110; LamG; 4.
DR   Gene3D; 2.60.120.200; -; 4.
DR   Gene3D; 2.10.25.10; Laminin; 12.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR001791; Laminin_G.
DR   PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR   PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR   Pfam; PF00008; EGF; 7.
DR   Pfam; PF12661; hEGF; 1.
DR   Pfam; PF02210; Laminin_G_2; 4.
DR   PRINTS; PR00010; EGFBLOOD.
DR   SMART; SM00181; EGF; 14.
DR   SMART; SM00179; EGF_CA; 10.
DR   SMART; SM00282; LamG; 4.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 4.
DR   SUPFAM; SSF57196; EGF/Laminin; 9.
DR   PROSITE; PS00010; ASX_HYDROXYL; 4.
DR   PROSITE; PS00022; EGF_1; 13.
DR   PROSITE; PS01186; EGF_2; 7.
DR   PROSITE; PS50026; EGF_3; 13.
DR   PROSITE; PS01187; EGF_CA; 3.
DR   PROSITE; PS50025; LAM_G_DOMAIN; 4.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00076};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Reference proteome {ECO:0000313|Proteomes:UP000008792}.
FT   DOMAIN          165..201
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          203..239
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          241..277
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          279..319
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          321..357
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          359..395
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          397..434
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          946..982
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          993..1194
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1237..1274
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1281..1477
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1473..1509
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1511..1549
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1620..1807
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   DOMAIN          1803..1840
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1841..1874
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1880..2090
FT                   /note="Laminin G"
FT                   /evidence="ECO:0000259|PROSITE:PS50025"
FT   REGION          540..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          854..943
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        553..572
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        580..653
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        854..892
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        915..930
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        169..179
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        191..200
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        229..238
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        267..276
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        309..318
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        347..356
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        385..394
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        424..433
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        972..981
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1264..1273
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1499..1508
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1539..1548
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1830..1839
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1864..1873
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ   SEQUENCE   2100 AA;  226394 MW;  8CB2CA54BABAAAD0 CRC64;
     MERENLKREL CRRRDVITNK CIKYAQSTTT ITTAATTTTT ATTTPLTANG TTTTGPILEV
     ALSSSTTKPL TDMQRNHLLK MPTKTATTAT ATATATTTAT KTKGLPTTVN CANSAAAAAA
     AAAAGATTTA QSIARTLRTL VHSCPQTGLL LTLCLSLSLV CVSQAGFACL SNPCVFGVCI
     DGLNSSYSCY CIDGYTGIQC QTNWDECWSG PCQNGGTCVD GVAYYNCTCP EGFSGSNCEE
     NVDECMSNPC QNGGLCRDRN NGYTCTCQPG YLGDHCEVDV AVCDTGTGAR CQHGGECIEG
     PGLEFSCECS AGWHGRICQE EINECASSPC QNGGVCVDKL AAYACACPMG YTGVNCEEEI
     LICADNPCQN NALCLMEENI PTCYCVPDYH GEKCEFQYDE CQLGPRCMNG GVCIDGVDTF
     SCSCPPLLTG MLCECLMVGE ESLDCNYTSP PTSAPPVVPV TPSMFPSTLA PPTVRPVTPP
     ETTMAPSTPP AAPVTTTPVV ELSSSSEEHF VGVKVTAAPP ESDSHSIDKD LTTSRPHLEV
     ELTPEMQPTA GPTTPPAGGS SSASSSEESH AIYTTIPPVP VPGVTSSSAE GSSEVVTSEE
     YTTVRRFDIS GSGGSSSSEE PTTTMRPTSP QRPSITIAVD YPSSGSSESV EQPMTVTTPG
     SIFVHRVTTF GTSISVDYAP TPTPYFPPET TLRATKSPLE ETTRHLWTEL PTTAAPFFTD
     YPAEVLITTH RTSAGRFTTV QPPTQQETTT APLDYEPASV ELTTAQAPHI VVTILEGNTT
     IPTTTYMPTM TTQRLQPQTA HATTELPLEW EPSTTQLPPA VTMPMPVEVT TSQTITTEDL
     LGPPVPPLMT IEPPRETTTP RAIPMPTEPP TLPSLPAATV PPTPPSTQSA QTMPPPTPAV
     HAYSTPGQPE LPAQTKPPVT ESSEESEGAN TVAIGSAGGG AEEKSGDVDC VKLGCYNGGT
     CVTTSEGSRC VCRFDRQGPL CELPIIIRNA AFSGDSYVSH RIYKDIPQHE ALDAVLPMHI
     QLKVRTRATN GLIMLAAAQG TKGGHYMALF LQKGLMQFQF SCGLQTMLLS ELETPVNTGH
     EITIRAELDF SRNYTHCNAS LLVNDTLAMS GDQPTWLKLL PPRLHTPEVI LNTWLHLGGA
     PQAPIGLIIE LPPAQSGTGF TGCLHTLRIN GQSREIFGDA LDGFGITECG SLACLSSPCR
     NGAACIKIES NELDANGDKA EKWKCKCPTG YMGPTCEISV CEDNPCQYGG TCVQFPGSGY
     LCLCPLGKHG HYCEHNLEVA LPSFSGSVNG LSSFVAYTVP VPLEYSLELS FKILPQTMSQ
     ISLLAFLGQS GYHDEKSDHL AVSFIQGYIM LTWNLGAGPR RIFTQKPIDF RLDAPRVPYE
     IKVGRIGRQA WLSVDGKFNI TGRSPGSVSR MDVLPILYLG GHEIANFNTL PHDLPLHSGF
     QGCIYDVQLK AGQVTVPLQE TRGVRGRGVG QCGTRECHRH ACQHDGACLQ HGATFTCICQ
     EGWYGPLCAQ ATNPCDSFNN KCYEEATCVP LVNGYECDCP VGRTGKNCEE EIRSLSDVSL
     TGRRSYLAVR WPYLYDGGDK LGAKRSQMVS YRNFTKKLMP PKPISTPSTH FVMKLLNEVE
     KQRSFSPVPL MGSKTFEEHH RVQFFFIEFQ LRPLSERGLL LYFGTLNNNQ DKKIGFVSLS
     LQGGVVEFRI SGPSNHVTVV RSVRMLAIGE WHKIKMAQRG RWLTLWVEGS ASSALAPSAE
     VLVEPDSLLF IGGLKDVSKL PHNAISGFPI PFRGCVRGLV VSGTRIVLNE TNIVESRNIR
     DCDGTACGGD SCESGGHCWL DEKLQPHCIC PDYAKGDRCE YSETCKLIPC KNNGRCLRSG
     RCSCPNGWGG FYCEIALSKP TTPSFRGNSY LILPPPRIPM KDKRRGPSLY ARPRETIQIS
     LNFSTIEPDG LLLWSEHNPV KFLGLGLENG HLKLANNLLG SNNDTVQAPA SGFVADGAWH
     GISVLLDRTR LELQLDGAVI FTERLPELSR RMTTTPTTSF QRRGSKEPTI SYEDIFYLGG
     FPNQDSVSMR TQGRFFEPFK GCLQDIQFGA EPKAVINDFS TYQGENIGSC DLHGDEPIIL
//
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