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Database: UniProt
Entry: A0A016U233_9BILA
LinkDB: A0A016U233_9BILA
Original site: A0A016U233_9BILA 
ID   A0A016U233_9BILA        Unreviewed;       550 AA.
AC   A0A016U233;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Kunitz/Bovine pancreatic trypsin inhibitor domain protein {ECO:0008006|Google:ProtNLM};
GN   Name=Acey_s0060.g3075 {ECO:0000313|EMBL:EYC09369.1};
GN   ORFNames=Y032_0060g3075 {ECO:0000313|EMBL:EYC09369.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC09369.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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:EYC09369.1}.
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DR   EMBL; JARK01001396; EYC09369.1; -; Genomic_DNA.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00054; EGF_CA; 2.
DR   CDD; cd00109; Kunitz-type; 1.
DR   Gene3D; 2.10.25.10; Laminin; 3.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 5.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR024731; EGF_dom.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR   PANTHER; PTHR10083:SF352; TISSUE FACTOR PATHWAY INHIBITOR 2; 1.
DR   Pfam; PF12947; EGF_3; 1.
DR   Pfam; PF07645; EGF_CA; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 5.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00181; EGF; 4.
DR   SMART; SM00179; EGF_CA; 2.
DR   SMART; SM00131; KU; 5.
DR   SUPFAM; SSF57362; BPTI-like; 5.
DR   SUPFAM; SSF57196; EGF/Laminin; 2.
DR   PROSITE; PS00010; ASX_HYDROXYL; 2.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 5.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 2.
DR   PROSITE; PS01187; EGF_CA; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW   ProRule:PRU00076}; Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..550
FT                   /note="Kunitz/Bovine pancreatic trypsin inhibitor domain
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001491852"
FT   DOMAIN          31..81
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          95..148
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          194..234
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          274..314
FT                   /note="EGF-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50026"
FT   DOMAIN          320..376
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          388..444
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          455..511
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
SQ   SEQUENCE   550 AA;  63732 MW;  6E8C1B92647219DC CRC64;
     MRLIVVVISL LSAKHGFSGE PVFVRNPEDR CKETVDPGPC QYYQVKWFWD EVDESCKEFH
     YGGCMGNKNR FNTKHECLKQ CRYKLFNPVA VPDLCLLEPD PGHCTDETKG QWWFFFNSDA
     GICEKFFFYG CGGNDNKFYS LHMCNKVCGE RLSPQIACEH CDLRTSFCKS HSKVNYTCEC
     RLGYEKNQYG ECIDIDECRG YTAACDRNAW CTNTIGSYSC ECMASYRGDG KHCTYVGLGR
     SSLDCKDCSS DATCENGICQ CKEGFEGDGF NCTDVNECLR APYICDKNAE CINRDGSFIC
     TCLSGYAGNG YNCTKTKNAC LDKFDRGYQE TCGGENWRQH FFLNHESKTC QPFWYDGCKG
     RSRNIFSDQE TCEQMCEATN ILTRAEVCWD KFDMNYRNQC LNGQWQQRFY FDHASLTCRQ
     FWYDGCRSDS RNMFEDMLTC QWLCETQPMY KSRACLQDFD QHYKDQCNGG RWRQQYYFDR
     YVKRCIAFWY DGCTGESENL FQDEQTCLLT CENPAKKDSL KPWHGGDKHK MKEKLESIYS
     XSDSGLGGRR
//
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