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Database: UniProt
Entry: A0A067RUA7_ZOONE
LinkDB: A0A067RUA7_ZOONE
Original site: A0A067RUA7_ZOONE 
ID   A0A067RUA7_ZOONE        Unreviewed;      2359 AA.
AC   A0A067RUA7;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Serine protease nudel {ECO:0000313|EMBL:KDR24395.1};
GN   ORFNames=L798_04348 {ECO:0000313|EMBL:KDR24395.1};
OS   Zootermopsis nevadensis (Dampwood termite).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC   Termopsidae; Zootermopsis.
OX   NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR24395.1, ECO:0000313|Proteomes:UP000027135};
RN   [1] {ECO:0000313|EMBL:KDR24395.1, ECO:0000313|Proteomes:UP000027135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Whole organism {ECO:0000313|EMBL:KDR24395.1};
RX   PubMed=24845553; DOI=10.1038/ncomms4636;
RA   Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA   Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA   Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA   Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA   Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA   Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA   Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA   Liebig J.;
RT   "Molecular traces of alternative social organization in a termite genome.";
RL   Nat. Commun. 5:3636-3636(2014).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC       pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR   EMBL; KK852415; KDR24395.1; -; Genomic_DNA.
DR   STRING; 136037.A0A067RUA7; -.
DR   EnsemblMetazoa; KDR24395; KDR24395; L798_04348.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; A0A067RUA7; -.
DR   OMA; SATWISH; -.
DR   Proteomes; UP000027135; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 3.30.70.960; SEA domain; 1.
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; IPR000082; SEA_dom.
DR   InterPro; IPR036364; SEA_dom_sf.
DR   InterPro; IPR001190; SRCR.
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; PF01390; SEA; 1.
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; SSF82671; SEA domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01209; LDLRA_1; 2.
DR   PROSITE; PS50068; LDLRA_2; 3.
DR   PROSITE; PS50024; SEA; 1.
DR   PROSITE; PS50287; SRCR_2; 1.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW   ECO:0000256|RuleBase:RU363034};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022968}.
FT   DOMAIN          11..133
FT                   /note="SEA"
FT                   /evidence="ECO:0000259|PROSITE:PS50024"
FT   DOMAIN          1937..2055
FT                   /note="SRCR"
FT                   /evidence="ECO:0000259|PROSITE:PS50287"
FT   DOMAIN          2077..2313
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   REGION          176..202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          370..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..587
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          745..765
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          906..928
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1055..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1244..1348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1560..1585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1600..1620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..272
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..587
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..759
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1244..1328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        1835..1853
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1847..1862
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        1916..1931
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2331..2349
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        2343..2358
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   2359 AA;  259904 MW;  8A7A90964DE9B0F5 CRC64;
     MGALRIDTNK PELVFDGSVC VTSGDNFVPS LGNNSSTAFK EMALKYQNMI DRVYQRSQIR
     PAYKKCVIEK FENGSLIVFF RLYLDRRKIP RNSQNIEETA RDILVNELIA PRTAAFKNIQ
     IDASSIFIKR SMDDAVTGPI EGMPKKKPSG NRTLQMHNGV IRKTITENTS ILNKTNESST
     VSKQENSEMK VTNTKDLKTK TQEAEGEAIP IIEGTVVITK IKETMEKPSD IPSMLKEGRN
     VTSSNADISS GESKSDNDTI SKASGNSGNK ADRDTKGNSK HVLNSTAGIA STSEINPMEQ
     NTQMKPQTDD KFSLENDDRN PIRPKIHPSY ISSKKQSTQN YDKFNLGDET ITKFSTTDVV
     RKDFIGTKQD YQGQNTGRPS GTVNGLDGKI SHDGNDTLVI KTGEKDVLLM GSPEDFTANP
     LNLKTNTYSD HYHTHATSGL TSDLWNIDSR STPIPNTKPT NLKATGAIHN YTDTEVTSQH
     FQESFLHIVD PPQIQSDEPW RPIMPHYTKH SLKPDNDDIG TGMAEVVVIP PSAVENKKTN
     EGHYHDNRYS SRLGQPAPTH KLQESSLGGY GSFSLHSDPQ ESQPDDTISR VSLHVVGSGS
     VSGENPETSI LHTTSGGGII IRKQHQPVMA ATFLPPHTIP LTYTTSEPPS MRQSIANPFT
     IPELPILHQF HDVDAILKAS PIKNAQPSAT WISHQYKHFQ GDFTVNTNSR NPDLYKGSVS
     SSNQQWIEGL NDTRSIVKPQ YSSHRESFPV RHHHQPPWAD TGNRARPENS KIPFKDTDIP
     SAVTSVESPL PRMPENKSMK VQLATLNPMG DSVADTSFSI VTLIPVRSNS GVGRPLRPRP
     KLPSHISIQI KNENEPMNVT LNYEYTLRHK VGDSGYSSPT PPIASGPVNG VQQYEVSHKR
     QNNLAGSTNK SEEAMINSNQ PTTEAPQQEV GITKMDHKSQ SSGFKYSTQS QIFSRITSSA
     SQQISTLTSH SPVTRSSTPV PKTNTVLTSI NVTQTEVAPV FSAIRPVPAA SIKKSASEKI
     MTMPPAKGTN LATSSTVTQI TATTSPLRKI ITTQQPSTEV KPNVTETLPP TSITTSAQTT
     IGTSPSSTSY ALTAMLNESS LANAASNTNH KSQINKTFTD QTKNVTHVVE NMIKIASVST
     LNQRPSEGEV QKNITAGITN SNNMKIKEIN VTNTSTSPTP SPHQQILTTK TTPSHLTHKN
     TVTAPKNSHS TVPLSAQPAI RHTTPSEFIP VIVIQDLPDD TWYKNNPNKQ KANVSSSVST
     LKAQSSTSNV PDGTGSQIEN ITRSTNVISS ASSLRTSELR NNGNSSEKGI SQNISMTISQ
     LQGDNNSSKE KPESVKENMR NTTPQPNITT PQAVILHTDI VTTTSIEISF GENASKVIIS
     PLNTSQSPNT VDNTITPNIS SDRHNTENIT TSKQVDSNLS SIMDLPITLP TSVTETTFTH
     KVKETRRQPK MKLTNTYAST FKNMRLEERM MDSTGNMKMK DEMYTDLPMS QITDVTDTTT
     TLNIFGRKEN GTNNTIIMVT KSEPENYNYS TIFYESRTVF EINSATESSI SENYTFDQIS
     SEEKELNSTT DSTTPENYGS EQFSSAEEDI ILPQTNASSN LTKEASPQRE EELPFTSTQS
     TVAQELTMQK VHEEIIPTTE EMSTALYEDS TPNEIYSPKD GLTNTSNEAL ETFTNFTVTK
     VTASSSKQDK QPPDDFEMSD DDVMLLLSVT RKNSFMSEEA VNTLSKYANV HTAISSNNVT
     KDSQNNIYED HNKISNKTTE SYVSDKITNN MAEEAKLSTK AILLHGSNNH AGIPILTKIY
     NKAPQQFSEK QATTEEGSPD LVNTAGCPSN QSLRCGDGEC ISSLSRCNQL VDCSDGIDEQ
     SCTCADYLKA QFLTRKLCDG IVDCWDFSDE NNCEWCSPGQ FVCPNSQVCV DQHRLCDGAR
     DCPYGDDEKQ CVTVAQNEAT AGDFPYNSEG YLMVRKQGRW GKLCLQNFDN VVARSQSAWE
     VADLGRAVCK AMTYSDFERV NRTIDTGSSS RADNSHYFEL TYSSDVNNNN SQPRSSLSFQ
     DTQCNQKEVV HISCRDLQCG IRPQAINQWA NSRHSRIVGG GNAAPGSWPW QAALYKEGEF
     QCGATLIADR WLVSAGHCFY HALDDYWVAR LGALRRGSSF PSPYEQLRPV SHIILHPGYV
     DAGFLNDISL LRLREPVQFS DFVRPVCLPP VPIRDGRLCT VVGWGQLFEV GRIFPDTLQE
     VQLPIISTAE CRKRTLFLPL YRVTDNMFCA GFDRGGRDAC LGDSGGPLMC QEKDGHWSLY
     GVTSNGYGCA RANRPGVYTK VANYVPWLQA AMVQQLSSLR DSKTQCKGHR CPLGECLPLT
     RVCNGFMECS DGSDEKGCW
//
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