ID A0A0V0TXQ3_9BILA Unreviewed; 1584 AA.
AC A0A0V0TXQ3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Papilin {ECO:0000313|EMBL:KRX43781.1};
GN Name=mig-6 {ECO:0000313|EMBL:KRX43781.1};
GN ORFNames=T05_5107 {ECO:0000313|EMBL:KRX43781.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX43781.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX43781.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX43781.1};
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:KRX43781.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JYDJ01000111; KRX43781.1; -; Genomic_DNA.
DR Proteomes; UP000055048; Unassembled WGS sequence.
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:SF217; PROTEIN CBG23496; 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}; Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 141..214
FT /note="Thyroglobulin type-1"
FT /evidence="ECO:0000259|PROSITE:PS51162"
FT DOMAIN 291..341
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 368..418
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 572..623
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 688..738
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 753..803
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1111..1161
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1518..1575
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 119..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 183..190
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00500"
SQ SEQUENCE 1584 AA; 173225 MW; 6F6237910EB66061 CRC64;
MRNVMAKLNG NMKLTYAARS KEIDPCERQP FQATCGSNTG RTIGRSQFVL RFYRRGDECV
SYPYALCKGS NGQPELFKRK QDCEQACIAG GGPSPDSGHT ERPKKLTSAN VFHQMTTSPR
VEEKSIDSSE QTVKPSSVRS LTKCQQQRQL ALKANQANTD HVNIQTGVIY SCTADGAFEE
IQCHEHSQIC WCVDKDGVEI AGTRKQASEG RPDCRQKPIE LQQNKPSGPI CGPGISPLLE
QSGQIYNCFG RACPKGYKCM MGPTMAACCP ASSADDNQSA SNLVQSTAKS CTLPKDRGTC
NKFELRFYYS TEFKECKYFF YGGCGGNENN FKDLAECEKT CGKSSASSEN VKPTTTSHQS
TLPDINRCLH PKDSGPCNGR FIRWYWNDER KLCEVFHYGG CKGSGNNFGS REECLKECSP
DNQKKTKVTV VQPATVEPIP FSVRPQLASH ATPRVETVTV RPQQVSSPAK SPDENVQKME
NTVEVECKTK SCAPECLAIT NGRGCVECMC PDLTALQVTK PRTPPHTTTS TSHPTSSLQV
HEKIDEIPLQ PISSSTKPVA KQPVKNETVD KCLLPLDKGP CTGPVQPRWG FSSETGRCEK
FDYTGCGGNM NHFYSLKECN IHCKAFLVIH PPGVHKSDDV SIKPHSTTTA ETEKVTTSQA
SSIPTLTTVK PAVMVEQMKI AEDVDPVCSL PRDSGPCMDF MMKWFYNAVT GKCEQFQYGS
CGGNSNNFDT EDMCKLRCVS GAHALGVEIP AACSEEKDPG PCFGYIVRFY YNPRNMRCEV
FVYGGCGGNS NNFETKEACN QICPVYEKVW RNTASEQAQF TEPSLPISTK TPTDATDSES
SISTTTHETN NVIHREPSVY QTPGAVMPGG VVESNYQTTV LNMIGAPTIP NYVPEPYEAS
AAVDGYNNVP SMPDYSVGNA QAETPTCPNG LPVRLGADGQ PVLCLPGKTQ CPPSSGCYFN
GIDFFCCPEE EPQSFNFYLT APPPQTLQPN SVDDTADGYP LRRVTRGVEV TNAVKRSAAD
DMHPEEVGMN MLPNLPLVSP LKAPSLGMPY DQQQAVPIPS GNEAYANSQA RPKELVNGIF
GPNSDYRPVV PQPPTLSAGM FSSAGKRSPY CDEPKNPGPC KGSHLRFYYD KTIDDCRLFY
YGGCQGNRNN FGTIDLCRQE CVLRAKYTAC PGGLLPLGGK ISPVTCGASA GGIECPEDYV
CHKGFFHICC PKYVENRDLP AGAPGHLPDP PKMAPMPEEV EKSKDIITAE ANRRGFGVQK
SDQQLRIVAN ATTVQQVQQQ SQQLQDRGGP PMFAMIQPRA TSIDSVANVQ MQKSPIQHQM
LLNASSTANQ QVPMMQRSPV MSTAMPQSNF AGHEQQMIQQ NNLQQNAAVL NNPSVEKSMF
SDIAHVESSL TPSPQGLPTT PVQMSPIAHQ FQGKSNTVVQ FQSSVHSANL PVTPVSENVQ
TVQPSLPNHQ PETQPALMSF PQTPSNVAES PTLFQSSQQQ VQRMPAFGSQ INVPQMPMEL
TMNGISQTPR PQLQTHTCHL PPDQGRRCSS SEQTPKSTVF YYFDISKNDC IILQYAGCGG
NANRFSSRND CFRLCHQGLP PLQP
//
