ID A0A3S3PDX7_9ACAR Unreviewed; 2638 AA.
AC A0A3S3PDX7;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Papilin-like protein {ECO:0000313|EMBL:RWS17475.1};
DE Flags: Fragment;
GN ORFNames=B4U79_09027 {ECO:0000313|EMBL:RWS17475.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWS17475.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWS17475.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWS17475.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
CC -!- FUNCTION: Has antibacterial activity. {ECO:0000256|ARBA:ARBA00002878}.
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:RWS17475.1}.
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DR EMBL; NCKU01000069; RWS17475.1; -; Genomic_DNA.
DR Proteomes; UP000285301; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0044562; P:envenomation resulting in negative regulation of voltage-gated potassium channel activity in another organism; IEA:UniProt.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR CDD; cd00096; Ig; 1.
DR CDD; cd00109; Kunitz-type; 9.
DR CDD; cd22639; Kunitz_papilin_lacunin-like; 1.
DR CDD; cd00199; WAP; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 2.160.20.80; E3 ubiquitin-protein ligase SopA; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 10.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR036645; Elafin-like_sf.
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 InterPro; IPR008197; WAP_dom.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF179; PAPILIN; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00014; Kunitz_BPTI; 10.
DR Pfam; PF08686; PLAC; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00131; KU; 10.
DR SMART; SM00209; TSP1; 7.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF57362; BPTI-like; 10.
DR SUPFAM; SSF57256; Elafin-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 3.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 6.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 10.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 7.
DR PROSITE; PS51390; WAP; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Toxin {ECO:0000256|ARBA:ARBA00022656}.
FT DOMAIN 1487..1537
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1546..1596
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1605..1655
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1664..1714
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1729..1779
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1789..1839
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1858..1908
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1915..1965
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1985..2035
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2057..2107
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 2196..2245
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 2251..2342
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2352..2438
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2490..2583
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2587..2626
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 446..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1169..1213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2452..2486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2453..2467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2469..2486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 44..80
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 48..94
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 59..70
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RWS17475.1"
SQ SEQUENCE 2638 AA; 290307 MW; 5D6F20662B2B552D CRC64;
HIRDNYPSLR PKRQYIPQQN VTLGLHTRYP ESGPWGPWST SSACSRTCGG GVAFQTRICL
DTRSDGRNTC IGPSKKYFSC NIQVSTYKRK DFDCVPGTPD FRAEQCARFN SQPFENHYYN
WIPYTRAPNP CELNCMPKNE RFYYRQARKV VDGTKCYDDG SLDICVDGVC TPVGCDKQLG
SNLKEDICRV CGGDNSTCRV VKGVFDSNNL HIGYNDIILI PVGAVNIKVE EVQPTNNYLA
VRNLNGDYYL NGNWRIELPR ELKFAGTVFL YSRKPHGYVS PEMLRSLGPT TEPIFISLLS
QERNLGIRYE YAVPISAPQP PSQESYSWMF GDYGRCSRTC GGGQQRRAVY CARSLDRQRV
PEYLCDPRAR PEDIRVCNTN LCPPDWSVGE WSECRCPGVR YRVVFCQKSA ENGRDFIVAP
ADECKKQRER PEFLVLCEIR NCPPLPTVPH TMDADKKTTS IDPKKTTLTT GTDSSATGTE
TTKTDSARTD TSGTDTSGTD TSGTGTSRTD TTGTDTSGTG TTGTDTSGTG TTGTETSGTG
TTGTDTPGTG TTDTETSRTD TTGTDTSGTG KTGTDTSGTG TTGTDGSKTD TSGTTMKGTT
AGTKETTATD TTSDGTERKS TTGKTTGDTQ TTATDASTES SMVEVCTMVS KTAWKEDEWS
ECDARCGEGT KKRNVYCYDT EQNKTVNENL CDLMTRPNDT QECDEIPCEG VDWITSAWSD
CDSKCGSSIQ TRSVLCSTEE GKVYPDRLCQ ANRRPNDTQV CEKYAGCDAI WFTSEWSNCS
VQCGKGMKTR FVFCGRWDDD QILTANDSEC SSTPKPLSAT ECENEPCEAL WHAGPWEACP
LSCSENKERS RRAICIHLGD AECDETSQPP TMEPCLVEST ASDLMGNETS CDLDADEFMK
TDSCSKSTHG CCPDGVTPRK QNYENCPPID APDGCEATEF GCCGDNKTAA FGPFKKGCPV
DCNVTRYGCC EDGKTPANGT DFAGCGCETS KYGCCPDGET KVKGENNEGC EFVKVEPCEK
SKYGCCKDKE TQAKGPNMEG CDSGVDAPAD ELSGDDCIID GSGEGSTVGL CREKGTEAIT
TELVTAAPDC SNTTFGCCLD GITAAQGENY KGCEDQQTTA KQLCNETEFG CCPDNITAAK
GSDLEGCIEM TRSTMTDLTM MTDLTSTDGN FTETELSETE STGTGTTGTE STGTGSTGTE
STGTGTTGTE AIGTEITEAN ATDTTGLDLT DTTEANATLT SQMTDMTETT GMTESNATET
AGSTIGYETT EVDCAQSKFG CCADNTSTAT GPNGEGCPCH LLPFGCCPDR KTPAKGERYY
GCTCHEYPYG CCQDNYTPAR GPDFDGCLCD RMLYGCCPDG ITPRVGNDPD ACNCERTVHR
CCPDGKTPAK GPNYQGCPCE IMPFGCCADR KTPARGPESE GCPCNTLPHG CCPDGTTPAK
GPRYQGCECV KTPFGCCPDG VSVAFGPKFE GCPDGPDLDT KLSAEACSLP KERGSCRNYV
VKWYFDANYG GCTRFWYGGC EGNGNQFQSQ EECEKVCVSP QGTLACLLPK VRGPCEGNTI
YWYYDSQSKQ CGQFYYGGCL GNNNRFQTRE ACESLCVNPD LLDTCDQQPD HGPCRGTYTR
WYYDKRDSQC KQFVYGGCRG NKNNFESERE CRDTCGSMTP QEICRLPKAE GKCLGSYPRW
FYDYQTGTCQ EFTYSGCDGN RNRFVDKASC ETLCNRIKKP TVSRPEDKCM LEKSEGGCGR
NLLMWYFNKE RRRCEQFYYG GCEGNSNRFE SRNECEKTCL PPIREENVCL LEKEIGNCYN
FQERWYFDAE ERQCHRFYFS GCNGNGNNFA SFEECEAKCG MRQKPTEMSP TDFKVEYCFM
NADHGPCDRN EILWFYDKAD GVCKQFYYGG CEGNQNRFPS RKECETRCWN SQKICKLPKV
KGPCSGKFVQ WFYNEASNEC EEFQYGGCQG NANRFSSKEA CENQCQQKKE TSPEPSARVP
EVNICLHRPD PGPCKSYLPH FYYSSADNSC RMFIYGGCKG NENRFHTRKE CEDRCVIKSS
EAEEKDPTDE REKEVICRQP VDAGSCNQTY PRWYYDPPSY TCLPFVYGGC GGTRNRFKSF
ENCMRLCQDV RPVEPTPETR PTPPRNQTLP AVCPASSCDD LRCPYGVDEY ADEHGCKQCR
CSNPCYSHQC PAEQRCALEA YRAPNGDPKV RPVCRLTNKP GECPKPTDEP DDRRECVDRC
RDDADCRNSD KCCSNGCAMI CLPAAGVPQA PSTTEKAKPP PPDEYDVLEI VARAGTDVVL
DCGDSNYASK VSWSKDQQPI YFLGDYRVQL IENGSLLLKA VESDDIGTYA CTVEDSRGST
TTKFRKLIVQ APAQILPGPT QVLAPVNTDA FLQCNAIGFP EPRVTWSKSG SMLPTDSIRY
HQYKNYTLLV RRVGPDDGGI YTCQAHNGLG PAALLDVTLL IDYEQPEIRP YEPSSARLDE
RPPYEQSNYD LRRGNNENVR PLTPLTPTQP IEAVSVEAEI ASPEYKTGSS VQMNCIVRGY
PPPTVRWYLR GKAQPLSSDS RITIFPNNTL IIDKATPSDS GEYMCIATND YNEASASIPL
KVEDIYVPTE CIDSPNFANC ALVVKVQYCN NKHYARFCCR SCLLSGQLDR SSINEILS
//
