ID A0A0V1MB62_9BILA Unreviewed; 1279 AA.
AC A0A0V1MB62;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Papilin {ECO:0000313|EMBL:KRZ68847.1};
DE Flags: Fragment;
GN Name=Ppn {ECO:0000313|EMBL:KRZ68847.1};
GN ORFNames=T10_9326 {ECO:0000313|EMBL:KRZ68847.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ68847.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ68847.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ68847.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ68847.1}.
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DR EMBL; JYDO01000152; KRZ68847.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1MB62; -.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 7.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 8.
DR InterPro; IPR006150; Cys_repeat_1.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR028150; Lustrin_cystein.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF217; PROTEIN CBG23496; 1.
DR Pfam; PF00014; Kunitz_BPTI; 8.
DR Pfam; PF14625; Lustrin_cystein; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 8.
DR SMART; SM00289; WR1; 2.
DR SUPFAM; SSF57362; BPTI-like; 8.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 6.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 8.
PE 4: Predicted;
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 185..235
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 300..350
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 455..505
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 509..559
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 623..673
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 665..715
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 730..780
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 959..1009
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 117..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 814..834
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1020..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1073
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ68847.1"
SQ SEQUENCE 1279 AA; 144203 MW; 49406F6D6DE0847D CRC64;
LLRFQNFTPT TFKQLSLLLY IFYRMAQVQN VVLFSVQVLL LYLNFVNAEE NACFRQQFQS
ACSGGNKLRI ALRYYVKDGR CVAYPASLCE GANEQKLDLF KTAAECERRC LNSNLADDDS
QQTPAPSKAS STSSSSEVSK EIPKVTKHVD IIRIRKIGRP TVPTVATVQP LLTSAPISNK
FSSQCSVAYD AGHCKNETQR WYFDFQLSKC KTFTYSGCGG NENNYRTEEE CEISCKEHHQ
PVCPKRTSPL VDTNGNLFDC FLQSCPNDFK CIYTSEKAYC CPDILNNEVA SNLKTRPALC
EQRKERGFCD LFELRFYYDV QLEECNYFFY GGCGGNQNNF KRLSDCKQTC GGRKDSTTRW
NQKQIAEKLI QLETTQGGEE EQKQQQQKSS EKKPELKQSR IVQDRDPDLI VVNTVSSVTV
KPAQQIVQTS FADRIEYGTR KPSTENSEDN KFQRCSQPAV KGHCSRRLRR WFWDARKNQC
VQFIYSGCGG NGNNFLTEKH CTDVCADPCM LPKKVGRCRG AFQRWYYDSS ANKCRKFIYG
GCDANENNFV GEEECISACV RGDSNSDTIG IDETDDNDYE TTDYTDEESK NTELVQRLKT
AVSLPAMKVN NNEDLFHPVP MGCLQPVETG NCDGVDVRWH YNKANHKCEA FVYTGCNGND
NNFASQLECV NGTCKESYNR WYYDRPKGAC KQFSYSGCGG NGNNFANEKE CLKMCNAQSE
IDYPASDDIC YRPLDVGFCN DEFIRWYYDP SIGDCKLFIF TGCGGNANSF SSSQECRRRC
VRVVHKSDQF KETTAKSDDL STTESISELE ESWNTTRSES EQETPDERDS KGDGQAVVHA
IIDKITKELK ENQTASTVGD LEETLVDLVA EGNTSVDLNT RDGRTIRLDK DSLTKICKQL
ARRIKVDMND EILQASREHS IPLVPVYTGE NGQHSEGQMP GSAIVFAMIN DERDPLAKCL
DELHPGRCSN YVERWYYDRG TKKCRSFQYG GCGGNRNHFY SKENCIFHCE RIADEVEKEY
EERKQAREDY DSEPEDIASP TSAPGYIPPG EKLTDSLSKD KDSTKKTKSK SALESSEKQA
NLKAPGFEPK NVFSGYKITP EPDVQQGPTK SLPQPPPLLH IMAPPTFPEQ EIRYIPGELM
QQEQQLYNNG HFPPPTISNS EFESSPPYAT PPISVMHSSP PPYLPYLQSV APTSAPLLSV
EPYGVASGRH HYNSRLPPPC ASGEVPVKNH DGSFLHCLPG QMTCPPDTSC YYNGLDYYCC
SQAPDQSVKQ YMPSTAKPY
//
