ID B4NPE9_DROWI Unreviewed; 2047 AA.
AC B4NPE9;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 2.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=EGF-like domain-containing protein {ECO:0000259|PROSITE:PS01186};
GN Name=Dwil\GK17732 {ECO:0000313|EMBL:EDW86389.2};
GN ORFNames=Dwil_GK17732 {ECO:0000313|EMBL:EDW86389.2};
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260 {ECO:0000313|EMBL:EDW86389.2, ECO:0000313|Proteomes:UP000007798};
RN [1] {ECO:0000313|EMBL:EDW86389.2, ECO:0000313|Proteomes:UP000007798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000313|Proteomes:UP000007798};
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:PRU00124}.
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DR EMBL; CH964291; EDW86389.2; -; Genomic_DNA.
DR RefSeq; XP_002075403.2; XM_002075367.2.
DR STRING; 7260.B4NPE9; -.
DR EnsemblMetazoa; FBtr0421848; FBpp0379938; FBgn0219731.
DR GeneID; 6652924; -.
DR KEGG; dwi:6652924; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_000085_4_0_1; -.
DR InParanoid; B4NPE9; -.
DR OrthoDB; 3107655at2759; -.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0043679; C:axon terminus; IEA:EnsemblMetazoa.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:1990709; P:presynaptic active zone organization; IEA:EnsemblMetazoa.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00112; LDLa; 7.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 8.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 4.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
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; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR PANTHER; PTHR46513:SF13; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 4-LIKE PROTEIN; 1.
DR PANTHER; PTHR46513; VITELLOGENIN RECEPTOR-LIKE PROTEIN-RELATED-RELATED; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF14670; FXa_inhibition; 3.
DR Pfam; PF00057; Ldl_recept_a; 7.
DR Pfam; PF00058; Ldl_recept_b; 12.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 8.
DR SMART; SM00135; LY; 20.
DR SUPFAM; SSF57196; EGF/Laminin; 5.
DR SUPFAM; SSF57424; LDL receptor-like module; 8.
DR SUPFAM; SSF63825; YWTD domain; 4.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS51120; LDLRB; 15.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000007798};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..2047
FT /note="EGF-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006458522"
FT TRANSMEM 1932..1957
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 634..649
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 696..738
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 739..781
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 782..825
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 826..868
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1010..1052
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1053..1095
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1096..1139
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1140..1181
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1314..1356
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1357..1399
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1400..1443
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1444..1485
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1619..1662
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1663..1705
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 1706..1749
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 49..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1876..1924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2023..2047
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1897..1924
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 221..233
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 228..246
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 240..255
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 291..306
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 312..324
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 319..337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 331..346
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 351..363
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 358..376
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 370..385
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 420..435
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 442..454
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 449..467
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 461..476
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 487..499
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 494..512
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 506..521
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 551..566
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2047 AA; 230092 MW; 8FC657DC1ACA9CDB CRC64;
MYWTSLSFCS LVCVVWLCLG CGDSTRVFAE QIGADNGGDD IRWLTKSTQE HQNWQHQQGQ
LRSANKPTNH RASHDVEVLP PSGEDHDSDS ISDTSPQHKH DDDDDAESQE DGEDKLYGQV
FTLEPTVPIK SGGNAGATST GDTPKFRNVG AQGGRSDLYG VRESDRQSNT RGRDGFIGAA
SNKQKSFRPF AHRGVVHDDP SQLGQPGEGY SAPPSDCQNP CDELQWQCSN CQCIDLHARC
NREVQCTDGS DEYDCDNNGD MMSKLQKECE QSGLHVMCPK TFRCINKEWL CDGDDDCGDY
SDETHCGART NCTEDQFECQ NGFCIPRPWL CDGENDCKDF SDEAHCNRTS CTEEHFACND
GYCISLAFRC DGERDCDDNS DEYKCAAVIN SCPEGEFKCR GGLGGAGGPS GQCILNRFRC
DGDNDCGDWS DEENCPQKPS QCTSNEYKCT DGTCIPKRWK CDKEQDCDGG EDENDCGNMS
SEHSLTCGPD EFTCHNGRCI LRTWLCDGYP DCSSAEDEVD CHLQCDAGQF LCPAKKNITN
LKICVHQKHV CDGQNDCPLG EDEVNCPEEQ ICPDHKQCEQ LCIKTARGRD ECACRLGYLM
NENKVNCTDI DECQYLTSPV CSQKCHNTQG SFVCSCESGY ILRPDLRTCK ALGGAMTLLV
ANRWDIRRVT LSNNRYTAIV KGLHNAIALD FHQRKGLLFW SDVSTDVIKM VYMNGTRVRD
VIKWGLESPG GIAVDWIHDL LFWTDSGTRR VEVSNFQGNL RTVIASNDLD KPRAIVIHPG
EALAFWSDWG PNPKIERAHM DGSQRQVIIS KGVTWPNGLA IDYPNHKIYW ADAKQHAIEC
SNLDGSDRIK ILSTHLPHPF ALTIFEDTMY WTDWNTKTVS AANKINGKGF RSVHENFHFP
MDIHAYHPAR QPDYPDRCQK DRRGLRGGCS HLCLPNKTSR RCGCPIGLSL KDDGKTCKSA
ADKLVLVARR KDIRLRQLNN KPAEPNEIDM IVPLDNLKHA VALDWCSDTD FIYWTDVERS
SINKAHLNGS YQQRVVHSNL VSPVGLALDW ITDKLYWTDP STNRIEVATT NGKMRTLLVW
EKLDKPRDIV VNPIDGLMFW SDWGEEAMIE RANMDGHNRV IISSKKLIWP NGLAIDYDKS
KLYFVDGGTK TLENMNFDGT GRKIIINNLG HPFGLDVSDG RVYWTDWDTK SAMSADKLTG
KGISTVIANS SDLMDIRVFH RTRRRVFNAC DKQNGGCSHL CLLNPTSYTC ACAVGVQLRE
DKRTCSEGPT KYILFAHRID IRQISLDFDH LIDVVLPLPP ISNAVALDVD RATGYIYWSD
TIENVIMSSS PDGLHVHKVI GESLENPDGL VVDSIGRTIY WADAGRHTIE VANLDGSNRH
VIAYKDLESP RGLALDYEAG LLFWTDWGHY RKIERSHLDG NDRSRIVTAN LGWPNGLSLD
LKSKRIYWVD ARLKTIDSCD YTGNQRKLIM SSLHHPYALS LTEDYIYWTD WKSKALHMAD
RRNISAKRDV MTNIDGLMDI KVITKHQPLA DNVCGRNNGG CSHLCLRNPS GFTCQCPIGL
RLRENSTTEC QNLPDDYLLI ALRSGIGMIS LNSGDYMDVV LPISGVHGAV VLDYHYRNNW
LFFADVNLDV IRRVNLLNFT DNKVIVSTDL LTPNGIAVDW IAENLYWSDT DRKVIEVSRL
DGSCRKKLIE DGLGDPRSLI VHPKKAYLFW SDWDSPSKIE RSYLDGSNRT AIVTSGVGFP
TGLTIDFTNR RLLWADALDD NIGQVDFNGK RRQTIVPYAP HPFGLTMLEN NIYWTDWYNK
SVYRSQRAPR IGYSNPFEVR DALSGALDIR AVSIHRQAKS WNQCAQDNGG CSHLCFYRAT
DYVCACPDRP DFNNKRPCST KPKELVQTRL ESDQQPEYSD EFTDDSTPPD PDDGINDVGD
EEDSPVDNER EFFVLVALGV VIVMVVIIVL VIFMLAFNTN RKKSKRNSRG SSRSVLTFSN
PNYNVDGTPM EPKTNIWKRF KYDKNHERPG VYEERSLTTE TASSSLFVPT PSPSTKTMQL
TTLSTIT
//
