ID A0A016U5D1_9BILA Unreviewed; 379 AA.
AC A0A016U5D1;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=BPTI/Kunitz inhibitor domain-containing protein {ECO:0000259|PROSITE:PS50279};
GN Name=Acey_s0056.g2712 {ECO:0000313|EMBL:EYC10375.1};
GN ORFNames=Y032_0056g2712 {ECO:0000313|EMBL:EYC10375.1};
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:EYC10375.1, 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: 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:EYC10375.1}.
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DR EMBL; JARK01001392; EYC10375.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016U5D1; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR CDD; cd00109; Kunitz-type; 3.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 4.
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:SF217; PROTEIN CBG23496; 1.
DR Pfam; PF00014; Kunitz_BPTI; 4.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 4.
DR SUPFAM; SSF57362; BPTI-like; 4.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 4.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 4.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW 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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..379
FT /note="BPTI/Kunitz inhibitor domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001491995"
FT DOMAIN 23..73
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 105..155
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 162..227
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 321..371
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT COILED 246..316
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 379 AA; 41802 MW; 94808CC8644EA730 CRC64;
MKMMKAAVAV LLCLAGSAIG DRCSKPLIRG PCLSIRPRYG FDPKLGKCVR FFYGGCGGNG
NNFETKEECQ DVCESDDPGL MPPIDPGFFN EDTGGSFSGP TSNVCSLPVD RGNCRGRMTR
YAFDAERGRC VPFIWGGCGG NANRFETQLS CRVSFYAIPN PCELPLAKGP CSAFIPRTLT
KSALMMKWGF SSYGYDKAKG KCVQFAYGGC KGNKNNFLSI ENCQQECMGE GILDRVSSLS
KKYVEKKELT KEVKAAFDKA KTKEEKKQLK EAIQKNVAEA IKKTIVEEKI KRIVKDAAVK
NKVEKAVEKL KELKEKKSNP CMMPIVQGKC RALIKRYAFD AKKGKCVKFS YGGCGGNENN
FETMAECKKR CKANTPMPI
//
