ID A0A158R1D8_NIPBR Unreviewed; 1540 AA.
AC A0A158R1D8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Papilin (inferred by orthology to a C. elegans protein) {ECO:0000313|WBParaSite:NBR_0001359201-mRNA-1};
GN ORFNames=NBR_LOCUS13593 {ECO:0000313|EMBL:VDL77182.1};
OS Nippostrongylus brasiliensis (Rat hookworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0001359201-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:NBR_0001359201-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL77182.1, ECO:0000313|Proteomes:UP000271162}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; UYSL01021089; VDL77182.1; -; Genomic_DNA.
DR STRING; 27835.A0A158R1D8; -.
DR WBParaSite; NBR_0001359201-mRNA-1; NBR_0001359201-mRNA-1; NBR_0001359201.
DR OMA; YGCPESC; -.
DR Proteomes; UP000038043; Unplaced.
DR Proteomes; UP000271162; 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; 4.
DR CDD; cd22635; Kunitz_papilin; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 6.
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; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
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; PF00014; Kunitz_BPTI; 6.
DR Pfam; PF19030; TSP1_ADAMTS; 5.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 6.
DR SMART; SM00209; TSP1; 7.
DR SUPFAM; SSF57362; BPTI-like; 6.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 6.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 5.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 6.
DR PROSITE; PS50092; TSP1; 6.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1540
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036006532"
FT DOMAIN 1073..1125
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1134..1186
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1254..1304
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1363..1413
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1430..1480
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1487..1537
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DISULFID 81..110
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 85..115
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 96..100
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1540 AA; 167962 MW; 8C1E5F9DB3906AF0 CRC64;
MRALLLSVAL FQALNAFSLF SSNEPTTPYL HPLSRPEISP AEARVKRQAY QVYVDGDSSV
SLDKTGQSET GPWGPWTPEQ CSRTCGGGVQ TEKRQCSGDC TGPSVRYVSC NLEPCAEGGD
FRAEQCAAHN DDPLDGQYHK WIPYKGKNKC ELLCRPENAK FYYKWDDKVV DGTKCDSKGD
DICVDGVCLP LGCDGKLGSD LKLDKCGVCD GDGSKCKTIA GRFDERNLSP GYHDVMRLPV
GSTAIRIEEA RPSSNNLAMK NTSDVFFLNG NSMIQVEKEV DINGVLFEYD DGKPERISAK
GPLKEEVVVS VLVRKGNRDV SIEFEFSVPI IEDVEYMYKP GEWSACSVTC GKGLITRTPY
CVDTKSQARV NDQLCDDANS TKPEYEKPCE TVDCEAEWFE GEWEPCSQTC GAKGEQYRVV
YCHKVFANGR RITVDDGNCT TERPIVRQEC NRFACPEWQA GPWSACSEKC GDAFQYRSVT
CRSEKEGEEG KLLPAEACDA DKNLESQRSC NLGPCTGLKF FTTDWKLCSK CNDTEETREV
TCKDSQGRAY PLEKCLTDDE KEIPADSRAC ATQQPCIYEW TASQWSKCST ECGHGHKTRR
VICAIHEEGG ITVVDEALCQ GEKPEAKTNC TNEEQCTGTW YSGPWTPCSA ECGGGTQERL
AVCLNYDKKP VPEWCDEAEM PTLTQECNTE ECPSCFDSEF GCCPDNVTIA TGDFNQGCSN
CSLSEFGCCA DNYTEASGKG GLGCEEYVLA PLNLEEAPEG SGEEKAGECQ VSSDNGETAT
VSCLTSNVTS AEGDDLFGNA TDTNATMHCS KSEFGCCPDW FTPAEGPGNA GCPVFVLGAC
NETEYGCCHD EVTLARGPNL EGCGEPTCAG SLYGCCKDRK TIAFGPHYAG CERSSFPCEL
STFGCCADGE TAALGANGTG CGENCLTTKY GCCPDGKGIA KGHHNEGCGC VYAQYGCCPD
GKTAAKGAGF YGCPDSCAQS QFGCCPDGKT PARGSHKEGC PCQYTRYGCC PDGETTALGP
RNDGCDDCRY AKYGCCPDGE SKALGPDYAG CPSTTLAPFL LGGTVAPSKI TSCVMPQDQG
TVCSSGYKLV WYYNTTEGRC SQFWYGGCDG NDNRFATKEQ CETICVEPPG IGRCYLPKVE
GPLRCDQPQA RYWYDYNTKQ CAAFWWRGCH GNANNFASWE ECSTFCKDVG PFELPATEAP
AFEPPHQPPY VHQPEPVDLD HEVVAHPITD DAPVPAPRLD ERQRPPLPTM EEVCRSTQDA
GPCQDYSDQY YYDAYKGTCQ TFIYGGCGGN LNRFRTEEEC MQRCGFLNPG VQQIVAPSGR
LEDQAQQQPL QPSYPEHALV RPPPQPIVPQ QPGGHSVKSR QACQLPLDVG KCHGSFPSWY
YEVATGSCVE FKYSGCSGNA NRFTSHEECE STCVRQPEPE SDSRSAASVC DEAKETGPCT
NFITKWYYNK ADGTCNRFHY GGCEGTGNRF DNEQSCKAAC AHHQDACSLP KVQGPCSGKH
EYYYFNAAAS SCEKFTYGGC LGNTNRFATL EECQARCQRK
//