ID A0A0V1H0D2_9BILA Unreviewed; 1316 AA.
AC A0A0V1H0D2;
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:KRZ03476.1};
DE Flags: Fragment;
GN Name=Ppn {ECO:0000313|EMBL:KRZ03476.1};
GN ORFNames=T11_18153 {ECO:0000313|EMBL:KRZ03476.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ03476.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ03476.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ03476.1};
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:KRZ03476.1}.
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DR EMBL; JYDP01000192; KRZ03476.1; -; Genomic_DNA.
DR Proteomes; UP000055024; 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:UP000055024};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 186..236
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 301..351
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 456..506
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 510..560
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 624..674
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 683..733
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 748..798
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 992..1042
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 117..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 374..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 823..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1053..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 832..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..867
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1053..1067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1087..1106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ03476.1"
SQ SEQUENCE 1316 AA; 148139 MW; 308B720CF30AB93A CRC64;
LLRFQNFIST TFKQLSLLLY IFYRMAQVQN VVLFSVQVLL LYLNFVNAEE NACFRQQFQS
ACSGGNKLRI ALRYYVKDGR CVAYPASLCE GANEQKLDLF KTAAECERRC LNSNLADDDS
QQTPAPSKAS SSSSSSSEVS KEIPKVTKHV DIIRIRKIGR PTVPTVATVQ PLLTSAPISN
KFSSQCSVAY DAGHCKNETQ RWYFDFQLSK CKTFTYSGCG GNENNYRTEE ECEISCKEHH
QPVCPKRTSP LVDTNGNLFD CFLQSCPNDF KCIYTSEKAY CCPDILNNEV ASNLKTRPAL
CEQRKERGFC DLFELRFYYD VQLEECNYFF YGGCGGNQNN FKRLSDCKQT CGGRKDSTTR
WNQKQIAEKL IQLETTQGGE EEQKQQQQKS SEKKPELKQS RIVQDRDPDL IVVNTVSSVT
VKPAQQIVQT SFADRIEYGT RKPSTENSED NKFQRCSQPA VKGHCSRRLR RWFWDARKNQ
CVQFIYSGCG GNGNNFLTEK HCTDVCADPC MLPKKVGRCR GAFQRWYYDS SANKCRKFIY
GGCDANENNF VGEEECISAC VRGDSNSDTI GIDETDDNDY ETTDYTDEES KNTELVQRLK
AAVSVPAMKV NNNEDLFHPV PMGCLQPVET GNCDGVDVRW HYNKANHKCE AFVYTGCNGN
DNNFASQLEC VNVCIERLPL NVCHHPVDKG TCKESYNRWY YDRPKGACKQ FSYSGCGGNG
NNFANEKECL KMCNAQSEID YPASDDICYR PLDVGFCNDE FIRWYYDPSI GDCKLFIFTG
CGGNANSFSS SQECRRRCVR GQKSETPTVP NVLQQVVHKS DQFKETTAKS DDLSTTESIS
ELEESWNTTR SESEQETPDE RDSKGDGQAV VHAIIDKITK ELKENQTAST VGDLEETLVD
LVAEGNTSVD LNTRDGRTIR LDKDSLTKIC KQLARRIKVD MNDEILQASR EHSIPLVPVY
TGENGQHSEG QMPGSAIVFA MINDERDPLA KCLDELHPGR CSNYVERWYY DRGTKKCRSF
QYGGCGGNRN HFYSKENCIF HCERIADEVE KEYEERKQAR EDYDSEPEDI ASPTSAPGYI
PPGEKLTDSL SKDKDSTKKT KSKSALESSE KQANLKAPGF EPKNVFSGYK ITPEPDVQPG
PTKSLPQPPP LLHIMAPPTF PEQEIRYIPG ELMQQEQQLY NNGHFPPPTI SNSEFESSPP
YATPPISVMH SSPPPYPTAQ VPYLQSVAPT SAPLLSVEPY GVASGRQHYN SRLPPPCASG
EVPVKNHDGS FLHCLPGQMT CPPDTSCYYN GLDYYCCSQA PDQSVKQYMP STAKPY
//
