ID B4PJQ4_DROYA Unreviewed; 2606 AA.
AC B4PJQ4;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Peptidase S1 domain-containing protein {ECO:0000259|PROSITE:PS50240};
GN Name=Dyak\GE20478 {ECO:0000313|EMBL:EDW93653.1};
GN ORFNames=Dyak_GE20478 {ECO:0000313|EMBL:EDW93653.1};
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245 {ECO:0000313|EMBL:EDW93653.1, ECO:0000313|Proteomes:UP000002282};
RN [1] {ECO:0000313|EMBL:EDW93653.1, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01
RC {ECO:0000313|Proteomes:UP000002282};
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:EDW93653.1, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 / Tucson 14021-0261.01
RC {ECO:0000313|Proteomes:UP000002282};
RX PubMed=17550304; DOI=10.1371/journal.pbio.0050152;
RA Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., Roote J.,
RA Ashburner M., Bergman C.M.;
RT "Principles of genome evolution in the Drosophila melanogaster species
RT group.";
RL PLoS Biol. 5:E152-E152(2007).
CC -!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
CC {ECO:0000256|ARBA:ARBA00024195}.
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; CM000159; EDW93653.1; -; Genomic_DNA.
DR RefSeq; XP_002093941.1; XM_002093905.2.
DR MEROPS; S01.013; -.
DR EnsemblMetazoa; FBtr0266996; FBpp0265488; FBgn0237793.
DR GeneID; 6533215; -.
DR KEGG; dya:Dyak_GE20478; -.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_228608_0_0_1; -.
DR OMA; DCMSAFL; -.
DR OrthoDB; 3035825at2759; -.
DR PhylomeDB; B4PJQ4; -.
DR Proteomes; UP000002282; Chromosome 3L.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0098595; C:perivitelline space; IEA:EnsemblMetazoa.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:EnsemblMetazoa.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IEA:EnsemblMetazoa.
DR GO; GO:0007343; P:egg activation; IEA:EnsemblMetazoa.
DR GO; GO:0007306; P:egg chorion assembly; IEA:EnsemblMetazoa.
DR GO; GO:0016540; P:protein autoprocessing; IEA:EnsemblMetazoa.
DR GO; GO:0160032; P:Toll receptor ligand protein activation cascade; IEA:EnsemblMetazoa.
DR GO; GO:0031638; P:zymogen activation; IEA:EnsemblMetazoa.
DR CDD; cd00112; LDLa; 8.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.128.620; -; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 6.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 3.
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; IPR015420; Peptidase_S1A_nudel.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24258:SF151; SERINE PROTEASE NUDEL; 1.
DR PANTHER; PTHR24258; SERINE PROTEASE-RELATED; 1.
DR Pfam; PF09342; DUF1986; 1.
DR Pfam; PF00057; Ldl_recept_a; 3.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00192; LDLa; 9.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 2.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 8.
DR PROSITE; PS50240; TRYPSIN_DOM; 2.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
KW Hydrolase {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:EDW93653.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|RuleBase:RU363034};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1140..1378
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DOMAIN 2017..2291
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 265..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1506..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1673..1693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 907..922
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 984..999
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1391..1403
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1410..1425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1748..1763
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1786..1801
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2305..2323
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 2432..2447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 2606 AA; 290588 MW; 2D116DB45B122B5A CRC64;
MNYNMDEMEA TRLLRHPRRW WSIGFGKRMV AISVLVIIVL LFSLIYHGLV VEKIDQVQQI
AALNARHQVL FNQPFEEDQS ALIVSPQTLH FKLLDEDMNK DMEDSKNRRR KHLKQMLVKF
RLNKKHRMRR DLHGLDLLDP VRMEANLQHL YSKLRTKRAR EALSQLEHEF VRCKKHTPQD
CMSAFLRMYK MAKEVTEKME KMKAIMREQQ PKLESSMESN EEKGTFTPAD LIQVTTAETT
TPAVNVAEKP ARTKIKPSRI SWIIDGHDHD ESPVYTDGAP KKETTKAPGT TTALVENTTT
KVEATESLTV ESTTEKISWI LDHFEKPQEI LRTTEGPGQR IIRNVTTTSM KSELETETTN
SDHVRTTESG LVLNITTDGP LETRNTTAQR KLSFDWILDG EENVEPEVKT TNPTTTTATS
GTLETTIVTT ELPKITFDWI IDGREVVEPQ DTTTEAAGTT AGQRKMPFDW IIDGEEVVEP
HDNATTTTIA TTVAISTTEL NERLHNTTAY PTKPKPVKFD WIIDGGEASG EVSSSSTSQP
KLTTRQAISN SDSPRSPHPL DNPTSIENML ESFEQHEAEK PILRVLNGNE SSSSSSQNVT
DGYERQLWLK KFEDQASPNQ NELIDTFGTA LDAKVLDKMG PKINPLNGHT WNAADAQILS
LCERVALRMR NKVASISDGE TKEKGETFTA SPSVQFTSRA PGGFPVSGET MKASAQFMFN
PNFGMPSIPV CFYMTPANFR MPMWSNTPTF MGMQGAHFGG SSNPGAGIFF VPQQFGPSGN
FFGGSGGSGA GGQGANIFSK NASPQKPSNG QQQQVYCSYM QNQAGQGAAQ SQTSSQQQQG
GQTAFSNANF KMRHANQSSA ANQQGQIIYA SYAGLPQQPI QERSRCPEPD QLSCFGQQEC
IAASKWCDNV VDCSDGSDES ACTCADRVDE DRLCDGYEDC PMGEDELGCF GCEPLAYSCY
DNPEDFAKRN RSTISMCYNR LERCDGFMNC LNGRDEKQCS MLVTDVADHM SHGASASEGY
LYHNYRGDWH PVCNNGEKWA ASACEMDVNS RMGHSAFLNV SFQSLTLPGP FIEPSLQAGV
HFAQACHGRN SHDSLVDHVA YVKCPPMQCG LPSKTSMLEH SKRAKRTVSD SKEIVGDGRI
VGGSYTSALQ WPFVVAIYRN GKFHCGGTIY SDRWIISAAH CVINYGKYFY EVRAGLLRRT
SYSPATQIQP VSHVVVHQAY ERRSMRNDLS LLRLLNPLQF NRWVKPICLP DKGRTTLGDD
WIWGPVENTL CTVVGWGAIR EKGPSSDPMR QVVVPIRKKC TDPEDQASED ICAGDPDGGR
DACQGDSGGP LFCRSVSSPD EFYLAGVVSH GNGCARPQEF GVYTRVTLYL DWLEMATTPQ
LLPKLQPLQL CPGFICVWGG KRCIAKRQRC DRNVDCLGGE DEVGCTYNFL PDMVGGVRQN
FSTTTESDYH PEKSKMREII PIEDEDLKAE QDDEELWEST TSLEQIETTE GPMDFALTEQ
VTLTTSDDIS VTEETTSTDF TVSDPATSPS TLMPSTGNPS TSLPSTSAPP NFAPTNMETS
TLVSTTIESQ ASTLPTTVAQ TSTMPTSTED LKKLTDLVTE FIESTTFEAT MDVVTTTPSL
TTTEPPKTAT TEGVKDTTTT EDTTTTSSIV TFTTTPLATI STTIPTTVTT LAPTTTTESA
KTTTTQSSSA HSQNDHVQIP NKFVCKKMPQ IVDIMMRCDR KVDCEDGTDE LECTCRDYLK
GSLKSLICDG KADCEDLTDE QDCLECQSNE FRCPLSKTCL PLSKRCDNEV DCKFKEDEKD
CFALTNGHDV HFDVHQQPKF SSTGIFSRNG HGVWRVVCAH ETGYHEHQAN TADAVCALLG
FKGAHYFNSS EFVSQQEMHP ITPELKGGRN RMAARIHSML GDNIQFTENE VIIPELGPPS
AARPEKDRLL PRKCVGIYVE CNPYSNKTTP LKTFSAGQAV KEKPIEQVPV LSPTIETHNT
PNVHFKPQIP AVVVNKKDEI LDRLDKLIKS KKNKTILVNE ELHEAIEELH WPWLADVYMN
GDLWCIGVLI DKHWVMVHES CLSGIDLETH YVSVLLGGGK TKRSAHRSNH EQIRRVDCFE
GVPKSNVLLL HLERPVRFTH HVLPTFLPDS SHQNQSDARQ CISVLHDDAT GRIKTVAITR
IHNATNCDSC YKLQEKQPPA HLMRLLNVSA EDMASISEEV ELINGVAPTE LPAITKFTSC
NQFGLKNVSD SHHNPSDQGV LVCRDSHTGW FPTALFNYNN SDCHSFKQPF GIRTLELVYK
SLQDIIDKPS CKMLLPAPEC TTHRCLLGTC LPQAAMCNGR YDCHDGSDED ETKCRQQKQQ
CAPGEMKCRS SFKCVPKSKF CDHISDCEDM TDEPTICSCF TYLQATDPSK ICDGKRNCWD
KSDESSVLCN CTADHFQCSS SPEDCIPRDF VCDKEKDCPN GEDERYCFGI EHPLHLQKKD
FWSNSQHTQP EKAPQYGQVI EQTYGIWHTK CFPKSKPPQV DEVREICKKL GYNPYRQPSY
RLIDDEENKA VHTYELADRQ GRSFSNESLM GKYRDSTKAL IISKFSPLQL NDRLTLFLKS
SRPIAELVRW NATDSSMCYR LEIRCA
//
