ID B3MZU7_DROAN Unreviewed; 1958 AA.
AC B3MZU7;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE SubName: Full=Uncharacterized protein, isoform A {ECO:0000313|EMBL:EDV33898.1};
GN Name=Dana\GF19243 {ECO:0000313|EMBL:EDV33898.1};
GN Synonyms=dana_GLEANR_20956 {ECO:0000313|EMBL:EDV33898.1};
GN ORFNames=GF19243 {ECO:0000313|EMBL:EDV33898.1};
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217 {ECO:0000313|EMBL:EDV33898.1, ECO:0000313|Proteomes:UP000007801};
RN [1] {ECO:0000313|EMBL:EDV33898.1, ECO:0000313|Proteomes:UP000007801}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000313|Proteomes:UP000007801};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH902635; EDV33898.1; -; Genomic_DNA.
DR RefSeq; XP_001966853.1; XM_001966817.2.
DR STRING; 7217.B3MZU7; -.
DR EnsemblMetazoa; FBtr0123943; FBpp0122435; FBgn0096254.
DR GeneID; 6502005; -.
DR KEGG; dan:6502005; -.
DR eggNOG; KOG1215; Eukaryota.
DR HOGENOM; CLU_000085_5_0_1; -.
DR InParanoid; B3MZU7; -.
DR OMA; ECLTMAH; -.
DR OrthoDB; 2877710at2759; -.
DR PhylomeDB; B3MZU7; -.
DR Proteomes; UP000007801; Unassembled WGS sequence.
DR GO; GO:0030135; C:coated vesicle; IEA:EnsemblMetazoa.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00112; LDLa; 13.
DR Gene3D; 2.10.25.10; Laminin; 4.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 13.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 3.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR026823; cEGF.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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; PTHR22722; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED PROTEIN 2-RELATED; 1.
DR PANTHER; PTHR22722:SF14; MEGALIN, ISOFORM A; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00057; Ldl_recept_a; 12.
DR Pfam; PF00058; Ldl_recept_b; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 3.
DR SMART; SM00192; LDLa; 13.
DR SMART; SM00135; LY; 9.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 12.
DR SUPFAM; SSF63825; YWTD domain; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS01209; LDLRA_1; 7.
DR PROSITE; PS50068; LDLRA_2; 13.
DR PROSITE; PS51120; LDLRB; 3.
PE 4: Predicted;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; 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:UP000007801};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1799..1822
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 305..342
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT REPEAT 445..489
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 533..576
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 579..621
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1936..1958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 92..104
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 99..117
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 111..126
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 153..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 226..238
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 246..261
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1032..1050
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1044..1059
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1091..1106
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1115..1127
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1122..1140
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1134..1149
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1156..1168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1163..1181
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1196..1208
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1203..1221
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1215..1230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1261..1276
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1300..1315
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1958 AA; 216640 MW; 5CE0345AD4224FAE CRC64;
MFPRVEEHFH SLESQEEIAG PGPKMRAGGG QRFNLTSIAN QTRARHLAKS PRIAQNGYGH
GCGVGHGCVA AMLLLCGAIL ATAAGSQDAG TCEAGQFRCR DGGCILLAKM CDGHGDCKDG
TDELDCDYRL CREPHWFPCA PPHGACLAVE IMCNGIDNCP GGEDELNCPG RTLFPQRRRN
CSSSEWTCQQ DRTCLPLELM CDGRADCSDR SDELAGCERQ KTEANCPPEG HLCPNGRCLR
RRQWLCDGHD DCGDGSDEKG CENLCQPQMG KFMCRNKEAC LPLSDACDGH RDCSDDSDEA
EGCHSPPDCK TKKCPPNATC HMMPSGGAEC HCPVGFRQAK FEDKCVDIDE CQESEQEQRD
VCSQKCENQS GGFQCVCDEG YHLARDNRTC RAMATSSSTD QAPLLLYTTQ MTVMGMHLQE
DNDRNHVFLV AGNLTKVIGV AYDGSHIYWT NIQNEAESLV RAKGDGSQAE TLLTSGLDAP
EDLAVDWLTQ NIYFSDNAMR HIAVCSHDGL NCAVLVTQDV HQPRSLALWP QRGLMFWTDW
GVRPMIARAS MDGTRSRPIV SDNIHWPNGI ALDMHQQQGR IYWVDAKLGS VQTVRIDGSG
RRTILDGVLK HPYGLALFED QLFWSDWVTK SVHSCHKFTG KGHRVLAKDR TIYAVHVYHP
AKQPQSSHGC QTASCSHFCL LAEPEAGGHS CACPDGMRLA ADQQRCIRTE KRQRLFIGMQ
RVLLEIEHTA FGRHSVSASH VLDGFIDEMV FNPVNGSLII ADNRQRIIFE YHPAVKYMER
LVSNLGNVSA LAFDHLSRNI YWADAEKGVV ELLSLQTRER ALIRLFPGQE WPVGLAVVPG
EGHLYVLLKS RRRSHIDRIP LSGKGEQVHV VEDDLGDDDF KLAVDPETHT LFWSDSDLGR
ISYTDYRTVQ PQIFRGKLRR PYALALVQQD LFWSEMNSNG IYWAHKNNLG PRKRINVEPK
DGPVSAPRMI PLAASSLPPR DSHPCQQQNG GCSHICVGEG AYHTVCLCPA GFVFRDAGNR
TCMEALDCEF RCGSGECLTM AHRCNGHRDC LDSSDETDCD EEHRRRTKVM CSGRQFACHS
GDQCVDKERR CDGRKDCQDQ SDEQHCEKFD KTKKCHAHQH ACDNGKCVDA SLRCDGMNDC
GDDSDEMHCG DSAVGCEEGM FRCSSGSCLP AGWECDGKID CSDGSDEHDK CGRRSCPPEM
HRCLLGQCLD KKLICNGHND CGDGSDELNC SDEAKSNLSC PAEKFQCTSN PRICLPGRTR
CNGTAECPRG EDEADCGDMC GIEEFQCRSG GQCIRREFRC DGDRDCTDGS DELACELVIK
NRNQTEGIRP EASPSGRPCR ASLFDCRDGQ ECVDMSRVCN GFPDCSNGMD EGPQCTTACS
KSSCQHKCRA TPSGAICSCH DGYRLDGDQR SCVDVDECQE QQPCAQLCEN TLGSYQCQCH
ADFMLRQDRV SCKSLHAASA LLFTSYNEVR NMTEQPVMLE VAWSANDSRI SGFDVDVKRQ
VGYFSSEEDG LLYQIDLKNK QRIRGLAVDA PTKLSLDWAT GNVYILSGGS GALEVQVCSF
EAGMCGRIVK VKSPRHLKHL AVDGYHSRLF YVALRSESLG HSQSELHMSR LDGSRHELLL
QRSDSYVSAL TTDPHQQLLY FVDLHTRTLE RMPYRPRNGP QRRPEVMLQK SNALLQPSGL
SVFENHVYLV NLGAKEAVRC RMYGSRVCNF INLNVLNAQD VVVAAASRQP QPAAHPCVHA
HCRGMCIQAD YGYECMCGHQ KVAEGEHCPH GSGNEVFLES KYSASESSPS SSDNQGTSFH
WWLALLILAI GSLVAGLGYM YFQYRRRGHR DLNINLHFQN PLATLARADP KATESSAVVE
FAPEQGYGSE EPASQPPAGM AAPNVFQRFM RSRQSRDDPM ATELLLDTPR ASTVHSLEGG
RQRIGVPDIL VAEFEDTAPP DCPAGQYGGR FPGDDPHA
//
