ID A0A0V1DA67_TRIBR Unreviewed; 1767 AA.
AC A0A0V1DA67;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Papilin {ECO:0000313|EMBL:KRY58325.1};
GN Name=mig-6 {ECO:0000313|EMBL:KRY58325.1};
GN ORFNames=T03_17928 {ECO:0000313|EMBL:KRY58325.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY58325.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY58325.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY58325.1};
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00500}.
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:KRY58325.1}.
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DR EMBL; JYDI01000022; KRY58325.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 7.
DR CDD; cd00191; TY; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 7.
DR Gene3D; 4.10.800.10; Thyroglobulin type-1; 1.
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 InterPro; IPR000716; Thyroglobulin_1.
DR InterPro; IPR036857; Thyroglobulin_1_sf.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF352; TISSUE FACTOR PATHWAY INHIBITOR 2; 1.
DR Pfam; PF00014; Kunitz_BPTI; 7.
DR Pfam; PF14625; Lustrin_cystein; 3.
DR Pfam; PF00086; Thyroglobulin_1; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 7.
DR SMART; SM00211; TY; 1.
DR SMART; SM00289; WR1; 3.
DR SUPFAM; SSF57362; BPTI-like; 7.
DR SUPFAM; SSF57610; Thyroglobulin type-1 domain; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 5.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 7.
DR PROSITE; PS51162; THYROGLOBULIN_1_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00500}; Membrane {ECO:0000256|SAM:Phobius};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 121..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 298..371
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 448..498
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 525..575
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 729..780
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 845..899
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 914..964
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1294..1344
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1701..1758
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 612..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 612..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 978..1030
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 340..347
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1767 AA; 193264 MW; BD27C0E6ABE2C014 CRC64;
MQCSDDSRDA KVMPTTTCYD VSLLFLFAYT QACSAVMQQN MAIDSGHTGA ETVCRNRCQS
PQRFSSAGCD MQNPLRDIRR RNSALMGQRS ANCVKRHPLV GLFHNSEQAD KSARLLLPHR
IAPPSFLVVF SLVAGCSFLY NNISALGSDT SFCCVVVMYG IFLLTSVTCF NLLLISSSKE
IDPCERQPFQ ATCGSNTGRT IGRSQFVLRF YRRGDECVSY PYALCKGSNG QPELFKRKQD
CEQACIAGGG PSPDSGHTER PKKLTSANVF HQMTTSPRVE EKSIDSSEQT VKPSVRSLTK
CQQQRQLALK ANQANTDHVN IQTGVIYSCT ADGAFEEIQC HEHSQICWCV DKDGVEIAGT
RKQANEGRPD CRQKPIELQQ NKPSGPICGP GISPLLEQSG QIYNCFGRAC PKGYKCMMGP
TMAACCPASS ADDNQSASNL VQSTAKSCTL PKDRGTCNKF ELRFYYSTEF KECKYFFYGG
CGGNENNFKD LAECEKTCGK SSASSENVKP TTTSHQSTLP DINRCLHPKD SGPCNGRFIR
WYWNDERKLC EVFHYGGCKG SGNNFGSREE CLKECSPDNQ KKTKVTVVQP ATVEPIPFSV
RPQLPSHATP RVETVTVRPQ QISSPAKSPD ENVQKMENTV EVECKTKSCA PECLAITNGR
GCVECMCPDL TALQVTKPRT PPHTTTSTSH PTSSLQVHEK IDEIPLQPIS SSTKPVAKQP
VKNETVDKCL LPLDKGPCTG PVQPRWGFSS ETGRCEKFDY TGCGGNMNHF YSLKECNIHC
KAFLVIHPPG VHKSDDVSIK PHSTTTAETE KVTTSQASSI PTLTTVKPAV MVEQMKIAED
VDPVCSLPRD SGPCMDFMMK WLVGLFYNAV TGKCEQFQYG SCGGNSNNFD TEDMCKLRCV
SGAHALGVEI PAACSEEKDP GPCFGYIVRF YYNPRNMRCE VFVYGGCGGN SNNFETKEAC
NQICPVYEKV WRNTASEQAQ FTEPSLPIST KTPPDATDSE SSISTTTHET NNDVETKISE
MPTFFTHPGN TVSPMIHREP SVYQTPGAVM PGGVVENNYQ TTVLNMIGAP TIPNYVPEPY
EASAAVDGYN NVPSMPDYSV GSAQAETPTC PNGLPVRLGA DGQPVLCLPG KTQCPPSSGC
YFNGIDFFCC PEEEPQSFNF YLTAPPPQTL QPNSVDDTAD GYPLRRVTRG VEVTNAVKRS
AADDMHPEEV GMNMLPNLPL VSPLKAPSLG MPYDQQQAVP IPSGNEAYAN SQARPKELVN
GIFGPNSDYR PVVPQPPTLS AGMFSSAGKR SPYCDEPKNP GPCKGSHLRF YYDKTIDDCR
LFYYGGCQGN RNNFGTIDLC RQECVLRAKY TACPGGLLPL GGKISPVTCG ASAGGIECPE
DYVCHKGFFH ICCPKYVENR DLPAGAPGHL PDPPKMAPMP EEVEKSKDII TAEANRRGFG
VQKSDQQLRI VANATTVQQV QQQSQQLQDR GGPPMFAMIQ PRATSIDSVA NVQMQKSPIQ
HQMLLNASST ANQQVPMMQR SPVMSTAMPQ SNFAGHEQQM IQQNNLQQNA AVLNNPSVEK
SMFSDIAHVE SSLTPLPQGL PTTPVQMSPI AHQFQGKSNT VVQFQSSVHS ANLPVTPVSE
NVQTVQPSLP NHQPGTQPAL MSFPQTPSNV AESPTLFQSP QQQVQRMPAF GSQINVPQMP
MELTMNGISQ TPRPQLQTHT CHLPPDQGRR CSSSEQSPKS TVFYYFDISK NDCIILQYAG
CGGNANRFSS RNDCFRLCHQ GLPPLQP
//
