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
//