ID B4ICD0_DROSE Unreviewed; 1071 AA.
AC B4ICD0;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=GM10225 {ECO:0000313|EMBL:EDW45026.1};
GN Name=Dsec\GM10225 {ECO:0000313|EMBL:EDW45026.1};
GN ORFNames=Dsec_GM10225 {ECO:0000313|EMBL:EDW45026.1};
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238 {ECO:0000313|Proteomes:UP000001292};
RN [1] {ECO:0000313|EMBL:EDW45026.1, ECO:0000313|Proteomes:UP000001292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25
RC {ECO:0000313|Proteomes:UP000001292};
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; CH480828; EDW45026.1; -; Genomic_DNA.
DR RefSeq; XP_002041288.1; XM_002041252.1.
DR AlphaFoldDB; B4ICD0; -.
DR STRING; 7238.B4ICD0; -.
DR EnsemblMetazoa; FBtr0193210; FBpp0191702; FBgn0165176.
DR HOGENOM; CLU_008163_2_0_1; -.
DR OMA; MPDAGTH; -.
DR PhylomeDB; B4ICD0; -.
DR Proteomes; UP000001292; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:EnsemblMetazoa.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0071813; F:lipoprotein particle binding; IEA:EnsemblMetazoa.
DR GO; GO:0016319; P:mushroom body development; IEA:EnsemblMetazoa.
DR GO; GO:0032370; P:positive regulation of lipid transport; IEA:EnsemblMetazoa.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IEA:EnsemblMetazoa.
DR CDD; cd00054; EGF_CA; 2.
DR CDD; cd00112; LDLa; 8.
DR Gene3D; 2.10.25.10; Laminin; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 9.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
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; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR PANTHER; PTHR24270:SF8; VERY LOW-DENSITY LIPOPROTEIN RECEPTOR; 1.
DR Pfam; PF12662; cEGF; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00057; Ldl_recept_a; 9.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00192; LDLa; 9.
DR SMART; SM00135; LY; 5.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 9.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS01209; LDLRA_1; 5.
DR PROSITE; PS50068; LDLRA_2; 9.
DR PROSITE; PS51120; LDLRB; 4.
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:UP000001292};
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 990..1015
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 589..604
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT REPEAT 692..735
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 736..778
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 779..822
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 823..867
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REGION 17..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 195..207
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 202..220
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 238..250
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 245..263
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 298..313
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 340..355
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 359..371
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 366..384
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 378..393
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 399..411
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 406..424
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 484..496
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 491..509
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 503..518
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 535..553
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1071 AA; 117655 MW; 26A444FBC26CE873 CRC64;
MATTCMPHFT EYFQTTTQSE LPTNESANSS SGSSGSSSGC REPSKTSGFF YSASTHYQSK
VQQLISFSFT SSFHLLFITC ILSISKFCNA AAVNAAHVTA ATPTPSEIMH NLSGAALLER
LKASTLGPTL DQLKHLAPAA ANSISPGTGS GMGIGMGSFG SSINSVLNGN PLKFLNVSGK
IGTPLDISLG LSNYCEEKQF QCSTGQCIPI RFVCDGSSDC PDHSDERLEE CKFTESTCSR
DHFRCGNGKC IPQRWVCDQE NDCADGTDES TSLCRGLCSS LMLMCKNGEQ CIHRQSMCDG
DQDCRDGSDE LECGRSQTCS PEEFACKSGE GECIPLSWMC DQNKDCRDGS DEAQCNRTCR
SDEFTCGNGR CIQNRFECDD DDDCGDGSDE KNCREKPKCG SDSFDCKNGQ CISNLWVCDG
DFDCRNGEDE MQNCTVSLLN FCQAGEFQCS DKISCLQKSW VCDGEADCPD GEDESQSNCV
KVSCRPDQFQ CNDHSCIAGH LTCNGKGDCA DGSDEIMCAI SATPRTCNAT TEFDCGGGLC
IPNAKVCNRR KDCPNGEDEP AGKCGINECS SKNGGCMHQC VNLEVGYRCE CQDGYKLDAD
QHTCVDIDEC ETPGICSQVC VNEIGSFKCE CEAGYMRLLK NHTRCKASEG HASLLLSRRH
DIRKIALDRP EMTSIVNSTK AATALDFVFR TGMIFWSDVA TQSIYKAPID EGNDRTVVLT
KSSVTSDGLA VDWIYNHVYF TDTHKCTIEL TNFEGSMGKV LIKDSLDIPR SIALDPIEGW
MYWSDWGASP RIERAGMDGS HRTAIITYDV KWPNGITLDL VQKRLYWVDG KLNTILSSNY
DGSQRQQVLY SSEYLRHPFS ITTFEDYVYW TDWGKQAVFK ANKFNGMYVE PVTATHMLEH
PMVVHVYHPY RQPDGVNHCQ SVNGHCSHLC LPAPRINERS PRISCACPTG LKLMPDGLMC
VEDLGTKTES NRTDTTNQVH KSDAKSENDY VGIALNVIAS LAGTALVASV IFVVYRRCTR
AVNSMNFENP VYHKTTEDHF SLEKNVTPHM FATAPDEEAN NPLFQPGTEC V
//
