GenomeNet

Database: UniProt
Entry: B4KEC1_DROMO
LinkDB: B4KEC1_DROMO
Original site: B4KEC1_DROMO 
ID   B4KEC1_DROMO            Unreviewed;      2958 AA.
AC   B4KEC1;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 2.
DT   24-JAN-2024, entry version 117.
DE   RecName: Full=Multiple epidermal growth factor-like domains protein 8 {ECO:0008006|Google:ProtNLM};
GN   Name=Dmoj\GI17917 {ECO:0000313|EMBL:EDW12889.2};
GN   ORFNames=Dmoj_GI17917 {ECO:0000313|EMBL:EDW12889.2};
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:EDW12889.2, ECO:0000313|Proteomes:UP000009192};
RN   [1] {ECO:0000313|EMBL:EDW12889.2, 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).
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; CH933807; EDW12889.2; -; Genomic_DNA.
DR   RefSeq; XP_002003447.2; XM_002003411.2.
DR   EnsemblMetazoa; FBtr0168642; FBpp0167134; FBgn0140658.
DR   GeneID; 6577480; -.
DR   KEGG; dmo:Dmoj_GI17917; -.
DR   eggNOG; KOG1388; Eukaryota.
DR   HOGENOM; CLU_000612_0_0_1; -.
DR   InParanoid; B4KEC1; -.
DR   OrthoDB; 5471913at2759; -.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0048731; P:system development; IEA:UniProt.
DR   CDD; cd00041; CUB; 1.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00055; EGF_Lam; 4.
DR   Gene3D; 2.120.10.80; Kelch-type beta propeller; 3.
DR   Gene3D; 2.10.25.10; Laminin; 7.
DR   Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 2.
DR   InterPro; IPR000859; CUB_dom.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR015915; Kelch-typ_b-propeller.
DR   InterPro; IPR002049; LE_dom.
DR   InterPro; IPR016201; PSI.
DR   InterPro; IPR035914; Sperma_CUB_dom_sf.
DR   PANTHER; PTHR46093; ACYL-COA-BINDING DOMAIN-CONTAINING PROTEIN 5; 1.
DR   PANTHER; PTHR46093:SF3; MULTIPLE EGF-LIKE-DOMAINS 8; 1.
DR   Pfam; PF00431; CUB; 1.
DR   Pfam; PF07645; EGF_CA; 2.
DR   Pfam; PF13415; Kelch_3; 2.
DR   Pfam; PF13418; Kelch_4; 1.
DR   Pfam; PF13854; Kelch_5; 1.
DR   Pfam; PF00053; Laminin_EGF; 4.
DR   SMART; SM00042; CUB; 1.
DR   SMART; SM00181; EGF; 13.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00180; EGF_Lam; 4.
DR   SMART; SM00423; PSI; 9.
DR   SUPFAM; SSF57196; EGF/Laminin; 4.
DR   SUPFAM; SSF117281; Kelch motif; 3.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS00022; EGF_1; 2.
DR   PROSITE; PS01186; EGF_2; 3.
DR   PROSITE; PS50026; EGF_3; 3.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS01248; EGF_LAM_1; 3.
DR   PROSITE; PS50027; EGF_LAM_2; 3.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW   Laminin EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00460};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009192};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        2744..2766
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          45..157
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          155..186
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1215..1256
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          1291..1337
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1338..1388
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   DOMAIN          1390..1518
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          1516..1549
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          2328..2376
FT                   /note="Laminin EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50027"
FT   REGION          2834..2892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2834..2862
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2875..2892
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        159..169
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        176..185
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        1309..1318
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1321..1335
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1360..1369
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1372..1386
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        1539..1548
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT   DISULFID        2348..2357
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT   DISULFID        2360..2374
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ   SEQUENCE   2958 AA;  330227 MW;  A15C2256FF79E9C2 CRC64;
     MRLGCECESV IKMRRMYALL PTLTFWLISF QLPSQSDQLH ITAPCDRSRK VFTEPYGEIS
     DGPSGYNYTQ DSHCEWLIKA KNDSQFITLT FHSMGTECSY DYIYVYDGDS FNSTLLGSFS
     GRTQPQKLVA RSGSMLILMY SDTNYVLDGF RASYYISNCL NNCHNHGKCV GHQCVCHGEW
     VGPDCEDEAC PQKCGEHQGR GKCQKSICHC SPGYSGRLCD LSDNPPGSSW RWLATDAEGM
     TPRAAHSAIY MEDEDALYVF GGYDLNNVIS TLQIYRFSTS QWEDEWGIPL QSRRHFYHPQ
     KIDHTLLKAV LQHKNEDEAK LWGLTSDVSF FRNILYTLAE SNLHQRRTRS SLPLTTVNAN
     STDEELTEYL EDILEEVTDH KPHGRYGHAA DRVPGGFVIY GGKHANGSFY NDLWQYNNTE
     SGGKWKQMAV RSKLQPPALA RHTLTTALDY LYLFGGSVES GEFSSSIYRI RLPLSEDSQW
     QLVKPRGGKT LDVRLAAHST VYYGATNSLI VFGGIMTSLA RFSKLSDRIF AFQLDQLHWT
     EILYPRTALR DTNIPRERAF HTATISGNYM IVFGGYTHRH NKDEICYDNQ MYWYHLSCHI
     WINQVVSADD SLYPKHQGVF AHAAALRRNH TLLIVGGYHG NVNADLFAYE LPQVLRVENP
     LYNHNPEMAC RLHASHTACL SNPECGWCSA DSSCYGRTIG ANCTTNLQTT RCPGICPSLG
     DCHSCLVHGT LWGGGNAAAF SVASKLGLNE CTWCVQNARC HYRADNYGMC GDSTGWWGEQ
     GTEIREPDMC TRNDRRPGLT YIKYNYPVNF TMPDYVGIVN ATMVDFASPP PTAYFEQRQE
     GEMLARLLGF VRPLQQWNNN NNSAIQVCSS YSSAVLRVGL GMNLDMLDNV TTQSSNQSYC
     SNVQLPSTEQ PFLIDFQARR RIGQNNIYNT YQKTKMELQH LHNGQLNAFT FEYLEPYYSG
     DCTQYNNCLH CLTDGSCSWC PLTSKCHLKS VNESAVCVAN DTDQGTHWAY LISQPSQCAN
     CSNYVTCRAC VSTPGNGECE WWLDDARCGR IGKSNSSVRS IAQCPRPCRE RRGCDQCLGE
     RGRCVWCEAS AQCFSFAVYT SEYQFGMCRE WIDKVSTPPI SPATGPSSAS ATPTTTLTMH
     PAPHRSLQQC KSCERHRNCT SCLRTLSCGW CFDRDNPIEG ICMQGDFSYS AGNCSLALNS
     SSQHDAEWAY AQCPDVDECG LGLHDCHKEA KCTNTQGSYN CHCRRGYVGD GRFSCVRTCY
     EFCQHGYCSG PPDYSCKCDL GWTGSDCGTS CGCNNHSTCL ERVGKCDQCQ AWTEGERCER
     CRQGSYGNAT ANIGCHPCEC NGHGNQDLGI CNVSHGECFC KDNTQGLKCD VCAPGYYGDP
     RDGGQCYYQC ESRGILTNIG RSAIGSYQSY RSPWGASLEV RECLWILQPK TLHADKSLLQ
     LEFQWNSLAM SCDENAVYIY DSLPDLTGAA QQNQLLAVVC EPYSAARIIE ARSSHVTVYY
     KQGSERRNFG FNALYSVKNC MAGSCMHPHI CDALQRCVCP VGYVGPRCEI EICPSNCHAK
     RLQGYCDTEY GRCICNNNNY AGADCGTLVQ RHHLVMTELF NTQLLSEALE HLRKTIPRFG
     HSVNADRRGS LWMFGGYSPS HGPLNDFRQF DTKNATWLQV TVESSTPEDR MPLGRYFHAA
     EIFVKKQNIY IYGGIGANSR LLSDFWLFSI QNQRWDQIEV DPSQGESPPA LAGHTLTHTR
     YQEHESLLLV GGLSLNKSRP LELWEFNLDT GRWVQLAAMG ARLPVLYGHS AVYHQETHSL
     YIFGGYAGEA QSKLYALDLN KLSWTELPTF KELNSPASLL PRARYFHSAV STEHYMIVYG
     GRTSPYNATD LLIAYVYACN QWVRLTDDVE LIGRLPVASY AEDMTIDPDS GAIYVIGGWD
     GSATQSHVTR INMPEDICQL WSGGKSMCRH YMGCSYCTIQ NTYSNSSHCF TQGRAPCANY
     NGTLVINNGP ACNDVWLASR NCSSFGSCSA CLAAWPIHQE LSPVCQWCDE CGIRGRCVPA
     GVDCARNSVW CEKELSVGVL GLCPLPQCHQ LDCETCMLHS EQCHWARNDM GHVECIAREL
     VEKNAYHLVD QCPPPCHTHS NCSSCLQSAP DAVATDCKWS TMLNTCLSPS AQPLLCAGGV
     CGLVLESTEL ERCPEPCHVY TQCSTCLEHA HCGWCAREGF NGDGICTEGA LEHRQEHPSG
     STCDIIYSSW RNDSQLTHAD VVSWHYVQCP AENECENGHH NCDPVSEQCI DLDTPTPGYK
     CVCATGYREE KNSCLPVCSQ GCVRGNCVRP DECKCDFGYV GENCSIQCLC NGHSNCESSS
     RLDICLKCHN NTMGEQCEKC QPLFVGNPRE GHACQPCLDY CHGHSDVCVA YDADPAVFNM
     TRSELELILP EGPAHNATCL RCANHTAGDR CDSCLLGYFR GSEDLHKQCR PCQCHGHGNI
     CDAVTGEKCN CANNTESDAT CIAGGGKNSA QLCWSVQCSK CRDSYAGNPT DGHQCYKQIT
     VESRMCFDAK PIEECKSKPA ALKPGQTVFF VIQPRFMNVD IRIIIDVTQG ELDVFMSPQD
     DSFIVETNQT TGYHEIFLDN RYNWGPKTER QHPLNIALPR HDNVTLQKLF APERRTGSNG
     PTMGASSSSN NFYVPHLHDC RSHGGHTFVV QDQFAKDLST HVTLNQCNTL LRLFGLKNRL
     VLTLPQHAHN LSATRFFIAL RASSGPEPSY GSVVFRQDQL HIDLFVFFSV FFSCFFLFLA
     LCVIVWKVKQ AADLRRARRQ HVVQMLHLAK RPFAQIFLAA SSLDMDNSPP ATSASTTRQM
     RQRARQALLL QQQQHLQRET QLHNQPTPST AHSSSHSRTH GPTHSSHSSH THTHIHGQGH
     YTSSSSSSSR PVQPTEIMLV AIEPTYDNLA AVGTVFVSLP GRSKAPLSIA LGSTLISYPR
     QYPLNARHFM RTQRHHQA
//
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