ID A0A0V1P4K8_9BILA Unreviewed; 2078 AA.
AC A0A0V1P4K8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Papilin {ECO:0000313|EMBL:KRZ91181.1};
GN Name=mig-6 {ECO:0000313|EMBL:KRZ91181.1};
GN ORFNames=T08_4271 {ECO:0000313|EMBL:KRZ91181.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ91181.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ91181.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ91181.1};
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:KRZ91181.1}.
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; JYDM01000047; KRZ91181.1; -; Genomic_DNA.
DR STRING; 92180.A0A0V1P4K8; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR CDD; cd00109; Kunitz-type; 7.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 11.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 6.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF217; PROTEIN CBG23496; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00014; Kunitz_BPTI; 11.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 5.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00131; KU; 11.
DR SMART; SM00209; TSP1; 7.
DR SUPFAM; SSF57362; BPTI-like; 11.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 7.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 11.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 6.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1130..1180
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1189..1240
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1273..1323
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1331..1381
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1388..1436
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1492..1542
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1591..1641
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1682..1732
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1741..1791
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1804..1854
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1867..1918
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1939..2030
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2039..2078
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT DISULFID 72..101
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 76..106
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 87..91
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 2078 AA; 230181 MW; 9E29EC96AA898100 CRC64;
MWRKRNRSSA SQMQKQSGHW FRSPLDLVEH PLSRKARQAY AVFGAGESGL SVEGVGQEES
GPWEPWEVIR ECSRTCGGGV QIETRNCSGN CIGAKKRYVS CNIEPCPTET DFRAEQCAKY
NDKALEGKYY KWRPFTRALN KCELMCIPEG ENFYYKWAEK VIDGTRCDAF NYDICVEGFC
LPVGCDNKLG STLKEDLCRV CGGDGSTCKT VEGFFDESDL KPGYHDVIVI PTGATSIVIQ
ERKPTNNYLA LRNEAGKYWL NGHWKIDFPQ TIEVAGTMFE YERIKQNNVA FEKLYAKGPT
KEPVIVVLLR QTENSGIQYE FSVPLTESLP YQYTVGPWSA CSVTCGQGIQ ERTVQCTDRS
TKEIVDEEFC LNSTLPELNR TCSTVDCDPE WFVGEWEPCS ETCGDTGMQY RIVFCHQAMA
DGVKVSVRDG LCTKERPIFR QPCNRFSCPE WHVGPWSSCS SPCGEAFQYR SVTCRSEKEG
EEGQLLPGKA CHAPDEPTNR RLCNLGRCEG LNWHVTEWNL CEHCNDTTET RNVSCRDSSG
RIYSDDRCEG EKPIDERPCA TPIPCLYKWH ASQWSECSTK CGHGHQTRSV VCAIEEGNKL
IKMDELHCDP YVKPSSRQNC TNEEKCIGTY FTSEWDECSA PCGGGTQKRV VLCFDYDYRL
NPAMCDEDEK PADVQECNLQ NCTACNETEF GCCPDNSTAA SGPFLEGCSN CSLSEFGCCP
DNYTTADGAN FEGCMSEMNV TEEGIGLEND TAPMKPKQAN NCTENDAECC TEMFDEKTNT
STVQCTVRMC NLTNSENVTV EVPCMNITSN PDMSNDTDIL LSDTTATLFN ETDLFGNETL
GNETDVHCSK TEFGCCPDWV TPALGPDNLN CTNYELGDCS NNGTKYGCCP DNLTLARGPK
FEGCGDPICS ASLYGCCPDR RTIAFGPHYK GCDRSTFSCE SSPFGCCSDG KTAALGPKNK
GCEDNCVISK YGCCPDGVTL AKGPKNEGCG CSLSQFGCCP DGQSTAVGPG FAGCPETCAT
SRFGCCPDGK TYAKGSNYEG CPCRYTRFGC CPDGVTAALG PRHEGCDDCR LKEFGCCPDG
QKAAQGPAME GCFEIAEESP VITIPPPLRG PVSPEQIGKH YSEQKLTSSC TLPSETGECS
DYSLKWNFDP IEGVCRQFWY GGCGGNENRF ESEEDCKHVC VNPPDQGVCY LPKIPGTDAC
GSTTIRWYYD ITEGYCMQFY YHCNGNGNNF AEYDECMATC DNVGKALTVS PPATFSHQPE
ETGAESEEYE DVCELPVDTG PCRGKITQWY YEPAVGDCIT FTWGGCKGNS NRFASKELCE
AKCAKVIEDF CKLPKDSGPC DQYVAKWYYK HEEGTCGRFY YGGCHGNDNR FETMEECHEK
CASKADPCQL PSVSGPCAGR EMRYYWTGER CEQFTYGGCL GNSNNFQSLE QCQRRCGSKS
TQQHMPSSEE VKVLTSAVAG GAGGSVGHSG VFTVSRVDEA AESSRPDDSS ICNLPKDTGP
CRAYIPSFYF DRMTQQCQQF VYGGCQGNEN RFPTRSACEA ACGTVRHQNI IHGRPQEKPE
ESTTYENFNN EINDLDNSIE SDTYRSHVDY CNSSPEVGPC RDATTRWHYE PRRGECIEFV
YGGCGGNRNN FKTRQDCERV CAEFSDTEPA PFEKPLQSTS RPASSPAPRF YPLPTSALPD
LCLQSKDIGT CYGSLLNWYF DSERMLCTSF MYTGCGGNSN RFTSEEACER ACGAYRDQDV
CRMPPDEGPC LASVPKWSYN QERGECVSFV YGGCEGNGNR FSSKEECDNI CNPRRTSYLN
EDVCDLERDA GPCLDPISQW YFDRVSSACK LFTYGGCRGN ANRFNTKSEC EARCVQPAKL
TTTGSACELE FDSGPCQQSF LRKWYHDPRS HKCRPFAYGG CGGNDNRFDS EQECASACNA
AVSMSITDDD RKRTFEHAPV SVQVDSTRWT YQEGQTIVLN CRGGTDEMHH KNNVVWYKDN
RHVAADVSRR IEVQFNGSLT INSAKISDSG EYSCALLQPA GSFSSAVRVV VEAQRQESNN
ENCVDNPLLA NCRLVVSAGL CSHTYYGRYC CQSCRNVN
//
