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
//