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Database: UniProt
Entry: D6W6H7_TRICA
LinkDB: D6W6H7_TRICA
Original site: D6W6H7_TRICA 
ID   D6W6H7_TRICA            Unreviewed;      1233 AA.
AC   D6W6H7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 2.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Serine protease P54 {ECO:0000313|EMBL:EFA11570.2};
GN   Name=AUGUSTUS-3.0.2_04654 {ECO:0000313|EMBL:EFA11570.2};
GN   ORFNames=TcasGA2_TC004654 {ECO:0000313|EMBL:EFA11570.2};
OS   Tribolium castaneum (Red flour beetle).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC   Tenebrionidae; Tenebrionidae incertae sedis; Tribolium.
OX   NCBI_TaxID=7070 {ECO:0000313|EMBL:EFA11570.2, ECO:0000313|Proteomes:UP000007266};
RN   [1] {ECO:0000313|EMBL:EFA11570.2, ECO:0000313|Proteomes:UP000007266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA11570.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=18362917; DOI=10.1038/nature06784;
RG   Tribolium Genome Sequencing Consortium;
RA   Richards S., Gibbs R.A., Weinstock G.M., Brown S.J., Denell R.,
RA   Beeman R.W., Gibbs R., Beeman R.W., Brown S.J., Bucher G., Friedrich M.,
RA   Grimmelikhuijzen C.J., Klingler M., Lorenzen M., Richards S., Roth S.,
RA   Schroder R., Tautz D., Zdobnov E.M., Muzny D., Gibbs R.A., Weinstock G.M.,
RA   Attaway T., Bell S., Buhay C.J., Chandrabose M.N., Chavez D.,
RA   Clerk-Blankenburg K.P., Cree A., Dao M., Davis C., Chacko J., Dinh H.,
RA   Dugan-Rocha S., Fowler G., Garner T.T., Garnes J., Gnirke A., Hawes A.,
RA   Hernandez J., Hines S., Holder M., Hume J., Jhangiani S.N., Joshi V.,
RA   Khan Z.M., Jackson L., Kovar C., Kowis A., Lee S., Lewis L.R., Margolis J.,
RA   Morgan M., Nazareth L.V., Nguyen N., Okwuonu G., Parker D., Richards S.,
RA   Ruiz S.J., Santibanez J., Savard J., Scherer S.E., Schneider B.,
RA   Sodergren E., Tautz D., Vattahil S., Villasana D., White C.S., Wright R.,
RA   Park Y., Beeman R.W., Lord J., Oppert B., Lorenzen M., Brown S., Wang L.,
RA   Savard J., Tautz D., Richards S., Weinstock G., Gibbs R.A., Liu Y.,
RA   Worley K., Weinstock G., Elsik C.G., Reese J.T., Elhaik E., Landan G.,
RA   Graur D., Arensburger P., Atkinson P., Beeman R.W., Beidler J., Brown S.J.,
RA   Demuth J.P., Drury D.W., Du Y.Z., Fujiwara H., Lorenzen M., Maselli V.,
RA   Osanai M., Park Y., Robertson H.M., Tu Z., Wang J.J., Wang S., Richards S.,
RA   Song H., Zhang L., Sodergren E., Werner D., Stanke M., Morgenstern B.,
RA   Solovyev V., Kosarev P., Brown G., Chen H.C., Ermolaeva O., Hlavina W.,
RA   Kapustin Y., Kiryutin B., Kitts P., Maglott D., Pruitt K., Sapojnikov V.,
RA   Souvorov A., Mackey A.J., Waterhouse R.M., Wyder S., Zdobnov E.M.,
RA   Zdobnov E.M., Wyder S., Kriventseva E.V., Kadowaki T., Bork P., Aranda M.,
RA   Bao R., Beermann A., Berns N., Bolognesi R., Bonneton F., Bopp D.,
RA   Brown S.J., Bucher G., Butts T., Chaumot A., Denell R.E., Ferrier D.E.,
RA   Friedrich M., Gordon C.M., Jindra M., Klingler M., Lan Q., Lattorff H.M.,
RA   Laudet V., von Levetsow C., Liu Z., Lutz R., Lynch J.A., da Fonseca R.N.,
RA   Posnien N., Reuter R., Roth S., Savard J., Schinko J.B., Schmitt C.,
RA   Schoppmeier M., Schroder R., Shippy T.D., Simonnet F., Marques-Souza H.,
RA   Tautz D., Tomoyasu Y., Trauner J., Van der Zee M., Vervoort M.,
RA   Wittkopp N., Wimmer E.A., Yang X., Jones A.K., Sattelle D.B., Ebert P.R.,
RA   Nelson D., Scott J.G., Beeman R.W., Muthukrishnan S., Kramer K.J.,
RA   Arakane Y., Beeman R.W., Zhu Q., Hogenkamp D., Dixit R., Oppert B.,
RA   Jiang H., Zou Z., Marshall J., Elpidina E., Vinokurov K., Oppert C.,
RA   Zou Z., Evans J., Lu Z., Zhao P., Sumathipala N., Altincicek B.,
RA   Vilcinskas A., Williams M., Hultmark D., Hetru C., Jiang H.,
RA   Grimmelikhuijzen C.J., Hauser F., Cazzamali G., Williamson M., Park Y.,
RA   Li B., Tanaka Y., Predel R., Neupert S., Schachtner J., Verleyen P.,
RA   Raible F., Bork P., Friedrich M., Walden K.K., Robertson H.M., Angeli S.,
RA   Foret S., Bucher G., Schuetz S., Maleszka R., Wimmer E.A., Beeman R.W.,
RA   Lorenzen M., Tomoyasu Y., Miller S.C., Grossmann D., Bucher G.;
RT   "The genome of the model beetle and pest Tribolium castaneum.";
RL   Nature 452:949-955(2008).
RN   [2] {ECO:0000313|EMBL:EFA11570.2, ECO:0000313|Proteomes:UP000007266}
RP   GENOME REANNOTATION.
RC   STRAIN=Georgia GA2 {ECO:0000313|EMBL:EFA11570.2,
RC   ECO:0000313|Proteomes:UP000007266};
RX   PubMed=19820115; DOI=10.1093/nar/gkp807;
RA   Kim H.S., Murphy T., Xia J., Caragea D., Park Y., Beeman R.W.,
RA   Lorenzen M.D., Butcher S., Manak J.R., Brown S.J.;
RT   "BeetleBase in 2010: revisions to provide comprehensive genomic information
RT   for Tribolium castaneum.";
RL   Nucleic Acids Res. 38:D437-D442(2010).
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; KQ971307; EFA11570.2; -; Genomic_DNA.
DR   AlphaFoldDB; D6W6H7; -.
DR   STRING; 7070.D6W6H7; -.
DR   MEROPS; S01.156; -.
DR   EnsemblMetazoa; TC004654_001; TC004654_001; TC004654.
DR   HOGENOM; CLU_003273_0_0_1; -.
DR   InParanoid; D6W6H7; -.
DR   OMA; CNMLVEC; -.
DR   Proteomes; UP000007266; Linkage group 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 3.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF7; HYALIN; 1.
DR   Pfam; PF00057; Ldl_recept_a; 3.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00192; LDLa; 3.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 3.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01209; LDLRA_1; 2.
DR   PROSITE; PS50068; LDLRA_2; 3.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|RuleBase:RU363034, ECO:0000313|EMBL:EFA11570.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007266};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          950..1188
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          298..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        716..728
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        723..741
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        735..750
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        804..819
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1206..1224
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1218..1233
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   1233 AA;  137576 MW;  8C8C0189E27A4DF9 CRC64;
     MPVCNRRSTP SVHTLWQERM SPRSCTERKS RGRLCSVALA IASFLVFVAV LSIAGMALYM
     GALHTEPPSS NNIISFSCSA KILRGDRFTG ALQEKARRYR LQLETLYQRS VLGPALTSCI
     VEKFGNDTVT VFFKLAFNKK KISKNVSNLE KTIRDILITD AISRKPVFRM IRFDPKSIEI
     KQIRDVDTYQ RSATKPKDTK NKTSVVLKTP RKNTTLTTTL PVKKKTDEIE IKEEDLPVVQ
     GSFKISKTDA DITEKKTENV STPKPKITTQ ATKTTTIKET SVTSALYKIA AIEKLSKTST
     GTPSTSTTTK NPLFSNPQVF NEQPWIPIIP DLTPITVPTT KPPQIPPKQP IYTSFTNPSL
     SYHNIDMEPL GSTSLKGHPI PVNKIPQVTE PSVFETSKKP TENSGFVEIE TVKYVPGSSG
     DKMKQQNMLK NLSSIFHDLA STLKIPEMNV SKNETFLGVA DEDSVGEGQV EVVEADEETL
     MMQTTKLPLV TLIPVKSNSG IGRPLRKRPF RNEENSTGDV SVENRSFPGS TRLNDFSALE
     KNPLKFIETE VVTSVSSEVN KVKLNKNQLE DFKIVGVLNF ATEASDTSEE LLRNPKMDPQ
     SNRTEVLRKH EPSSEITVYA TNSSVSSNRK EANFNILTPE KLKQLSEISK IHDNLTVIDK
     EPVISNKAIS SSYTVNHSGF KILTKTFNKI DELPKDTKLN GYNNLAFTAI SNKTECGNLT
     IKCGDGQCLP ETTKCNQLID CNDGKDEQDC NCADYLRSQY LLRKICDGVV DCWDYSDENQ
     CEWCEPQQYV CSNSKMCIDK TKICDGLRDC PQGDDERQCV TIAENIDAAD EFPYTSEGLL
     MVRKFGSWGK LCVENLRNLV FPILDLGKAV CKSMTYQFLD SVKSVTETDE RTPSRYFEMD
     YTFENSSKYS LSFSETGCET RKVVRVRCQA LECGARPQAV KHIARRAYRI VGGGNAGLGS
     WPWQAALYKE GEFQCGATLL SDTWLVSAGH CFYHSQDEHW VARLGALRRG TALPSPYEQL
     RPITRIIVHP GYVDSGFIND ISLLKMEFPV IFSDYVRPIC LPPPGQMVPD GRLCTVVGWG
     QLFEVGRIFP DTLQEVLVPV ISTAECRKRT VFLPLYKITD DMFCAGYERG GRDACLGDSG
     GPLMCPEPDG KWLLQGITSN GYGCARANRP GVYTKVANYV TWIEAHMSRD DHNSTKKKSV
     CLGHRCPLGE CLPKSRLCNG YIECSDGSDE RDC
//
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