ID F1KQ30_ASCSU Unreviewed; 1658 AA.
AC F1KQ30;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Papilin {ECO:0000313|EMBL:ADY39984.1};
OS Ascaris suum (Pig roundworm) (Ascaris lumbricoides).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Ascarididae; Ascaris.
OX NCBI_TaxID=6253 {ECO:0000313|EMBL:ADY39984.1};
RN [1] {ECO:0000313|EMBL:ADY39984.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21685128; DOI=10.1101/gr.121426.111;
RA Wang J., Czech B., Crunk A., Wallace A., Mitreva M., Hannon G.J.,
RA Davis R.E.;
RT "Deep small RNA sequencing from the nematode Ascaris reveals conservation,
RT functional diversification, and novel developmental profiles.";
RL Genome Res. 21:1462-1477(2011).
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DR EMBL; JI164046; ADY39984.1; -; mRNA.
DR MEROPS; I02.955; -.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00109; Kunitz-type; 5.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 8.
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 PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF217; WU:FB59D01; 1.
DR Pfam; PF00014; Kunitz_BPTI; 8.
DR Pfam; PF14625; Lustrin_cystein; 3.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 8.
DR SMART; SM00289; WR1; 3.
DR SUPFAM; SSF57362; BPTI-like; 8.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 4.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 8.
PE 2: Evidence at transcript level;
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 41..91
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 112..162
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 174..224
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 427..477
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 700..750
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 765..815
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1161..1211
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 1598..1655
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT REGION 338..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..941
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1474..1511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..365
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..590
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..941
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1332..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1501
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1658 AA; 180461 MW; F85326D08429191F CRC64;
METFTPNSPM QTTHPVEPLA PLISKQDIGT PAESLLPENR CIHARDPGDC NGQFVRWYWD
SNVKMCEVFT YTGCNGNGNN FASREECISV CHREDALPAA TKVEQPDLAN VCEHEVDAGE
CKGEFQRFAF DAKLGECRAF VYGGCGGNGN NFASITDCQR KCHSEGSTLS TNVCEHPIEV
GECSGVFARF AYDSVANECR QFTYGGCGGN GNNFATLADC RTLCVKVKCP PEPRCDLTRC
QLVNDAQGCP FCSCPPPHQP HPPTAEREQH PSPLCSLGAD NLFSCSGRPI ERPDCPPLDV
MLCIEPCIIF SNRRGCQECV CPVIPPNNVV EATNSIIGPV SPTGTLPTVQ TDRPPSPPSS
PAAPSSAAPP ASVSMPAQPP RQASVPILKS FDKGPLVSQQ QAEKPRQPYP LTPASRIPNI
ADLGEKCTQP LDAGPCKNFT PRWYFNVSST TCEQFDYGGC AGNRNHFFSK NECEIHCGRF
ARAFAVEGRQ PAPQQPIQAV PQRQEQPAGP LQQTHAETIT DSSLPGISQQ NFQPSNFPSP
LPLPLPAIRA AITSPQSPQI SSTTPSPSQS SPSTITLSIQ QPTSSITTTS ARQEVNANKN
TQKTIASNVA QSENVDKLHQ LEEIIESSTQ FALTESEEQE EEEPTEQEAK HPPKQFVSSS
NSDEVEIFGP PLRPPIVPHK EPPRIIGASP SPIEIDEETC VLPPEAGPCV DYVPRWFYNS
QTGNCEQFSY GSCGGNTNNF MDRQTCEAKC QSGSDSIKSQ VPDRCTHEKD EGYGGGYNVK
WYFNIRNLRC EQMVYQGEGG NDNQFSSLGD CQTSCVPVEG IGFSPKPVRI TQPTMSTLVA
EEEFTRESVP RSRLIMQKKI DHHHSASNRA FHGTVIAESV NEYGQIRESA PSLPIADKAH
KKIHAHTTAS ATKKTEVGST SAVDSHGPEL ASSRNELNTA ESISSKSEFE YNTELLNKKP
LAAINSQMPI LAPSPPMKIN YQNGVRINKA EDEWVDELVE VPPQKGLEQI LSGIEAPVHA
FGSAISEVQR IPVCPNGLKA IQSADGKPVM CLPGKNHCPG TSSCYFNGID FFCCPNEEDP
YDKHVFGGYN GDEERHGYKS LKSSLNIRSL ADEKIRRVRR AASPSAAFSL DLASHPARFD
AKAPRQYTRA SLRRPAKIDP CTESVDSGSC NEAHLRYFYD RRADTCRLFY YSGCSGNSNN
FATQYECEQR CKVGRLSSRT TPPGTCPGGR PPLGENAPVL CGNQTDSIGC PAGYYCRNGP
PDVCCPNDAL DFENVRKSNK KSKSKPRINA ALIHHGSRDS TENVVYGVGD AYSKESAAVS
RASPGRGSAK GTPSEAESSP MSTPPTMCPD GSDALLDESS GLPLKCGSGF DGQALCPVGF
YCSIDSERNG RLCCPLGVYG SNIPPPPVIA PYLGLRRPNP GEVIDRGSLL SDPKPPRLTT
PKAMATMAGH CLVGRMRVST YKCHILVHRA PYSHAEESME NTRERGEYTN ESDEGHASEL
TSSENEHGSA EAVEENVNVM APTPEGSLDG QKGEGPYGRM LLKPTDKQQL EVNKAYPGGE
MKSAREENDG VQIDIGEGED PFESDQLPAK KPLDRSACHL KPTEGRPCHE NETAPKTNLQ
YFYSRRDRKC KLYFYRGCGG NANRFEKKRD CETLCMGL
//