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Database: UniProt
Entry: B4Q837_DROSI
LinkDB: B4Q837_DROSI
Original site: B4Q837_DROSI 
ID   B4Q837_DROSI            Unreviewed;       690 AA.
AC   B4Q837;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=GD23151 {ECO:0000313|EMBL:EDX03459.1};
GN   Name=Dsim\GD23151 {ECO:0000313|EMBL:EDX03459.1};
GN   ORFNames=Dsim_GD23151 {ECO:0000313|EMBL:EDX03459.1}, Dsimw501_GD23151
GN   {ECO:0000313|EMBL:KMY87666.1};
OS   Drosophila simulans (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7240 {ECO:0000313|EMBL:EDX03459.1, ECO:0000313|Proteomes:UP000000304};
RN   [1] {ECO:0000313|EMBL:EDX03459.1, ECO:0000313|Proteomes:UP000000304}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDX03459.1}, and mosaic
RC   {ECO:0000313|Proteomes:UP000000304};
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).
RN   [2] {ECO:0000313|EMBL:EDX03459.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mixed {ECO:0000313|EMBL:EDX03459.1}, and W501
RC   {ECO:0000313|EMBL:KMY87666.1};
RG   FlyBase;
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:KMY87666.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W501 {ECO:0000313|EMBL:KMY87666.1};
RX   PubMed=22936249; DOI=10.1101/gr.141689.112;
RA   Hu T.T., Eisen M.B., Thornton K.R., Andolfatto P.;
RT   "A second-generation assembly of the Drosophila simulans genome provides
RT   new insights into patterns of lineage-specific divergence.";
RL   Genome Res. 23:89-98(2013).
RN   [4] {ECO:0000313|EMBL:KMY87666.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=W501 {ECO:0000313|EMBL:KMY87666.1};
RA   Hu T., Eisen M.B., Thornton K.R., Andolfatto P.;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR   EMBL; CM000361; EDX03459.1; -; Genomic_DNA.
DR   EMBL; CM002910; KMY87666.1; -; Genomic_DNA.
DR   RefSeq; XP_002077874.1; XM_002077838.2.
DR   AlphaFoldDB; B4Q837; -.
DR   MEROPS; S01.168; -.
DR   EnsemblMetazoa; FBtr0223061; FBpp0221553; FBgn0194541.
DR   GeneID; 6730704; -.
DR   KEGG; dsi:Dsimw501_GD23151; -.
DR   HOGENOM; CLU_399161_0_0_1; -.
DR   OMA; NWYNNET; -.
DR   OrthoDB; 5397966at2759; -.
DR   Proteomes; UP000000304; Chromosome 2l.
DR   Proteomes; UP000035880; Chromosome 2L.
DR   Bgee; FBgn0194541; Expressed in male reproductive system and 1 other cell type or tissue.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00033; CCP; 1.
DR   CDD; cd00112; LDLa; 4.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   PANTHER; PTHR24270:SF61; CD320 ANTIGEN; 1.
DR   PANTHER; PTHR24270; LOW-DENSITY LIPOPROTEIN RECEPTOR-RELATED; 1.
DR   Pfam; PF00057; Ldl_recept_a; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 4.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 4.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01209; LDLRA_1; 1.
DR   PROSITE; PS50068; LDLRA_2; 4.
DR   PROSITE; PS50923; SUSHI; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}; Hydrolase {ECO:0000313|EMBL:KMY87666.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000304};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..690
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014299431"
FT   DOMAIN          375..435
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          456..683
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        79..97
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        131..149
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        172..190
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        377..420
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   690 AA;  77306 MW;  B61C2EEEE57150C6 CRC64;
     MSHPLLRFEG VLLALMFIWF LGLSDGCDED EEFECPEDGR CIPIDGLCDA KPDCLYASDE
     SFTVCKVHLS DMMADKYHCA TGAAIPGRLA CNGIVDCSDG SDELPQVCGS DPGKLEERFR
     GNCTGQKDLE CLPGECVPHS AKCDNVIDCS NGRDESLEIC MQTCEENKCF QCANGVLLDS
     KDLCDNKMDC LDGSDELSNV CGNAINWKEV PPAACHETLE HRFSNRTVFQ RRNALRFVYA
     NQAAEVQCWN SDRKSWNVCM NNGSWHHDFP PCIGKPVNRN PDTNGTNGCP INWYNNETMI
     IINWNDDGES IALPPIRNSR VTFRCLEDLT FLPYEFKDKP ITCQANKTWI EMDFHPRCTN
     LCSPEQISEM YSLTPRCYNG DNGSPINCQD KYSLVPNTHV KFECASGFIH KTSDPMRVKC
     TEDGEWEGLR DLCEKQERHC NYECNHRLNY SEVTMSKGGD ATDSLQASWL VPIYKWNSTT
     SRHEFVCTGN LIRLDIVLTA AHCLNDRNSR PENFLVGPTG NRSASMDPKY LHRVRNLEVY
     GAYSKINHIY DVGIVVLERR MDFKQDQRIV CLPYNVGSHL DLIGDAMVSS WNSDGYLATV
     YGRLSEPRNG DLNVVLHDGY TLCKGDSGSG VITTCGLDNH KCLVAVVSRN VGSGDHGTFC
     SNNVTAATLI SPHLQDYIQQ LIRNNINCPE
//
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