ID A0A077ZJB7_TRITR Unreviewed; 727 AA.
AC A0A077ZJB7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Tissue factor pathway inhibitor 2 {ECO:0000313|EMBL:CDW60492.1};
DE Flags: Fragment;
GN ORFNames=TTRE_0000887301 {ECO:0000313|EMBL:CDW60492.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW60492.1};
RN [1] {ECO:0000313|EMBL:CDW60492.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW60492.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG807134; CDW60492.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077ZJB7; -.
DR STRING; 36087.A0A077ZJB7; -.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR CDD; cd00109; Kunitz-type; 2.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
DR Gene3D; 3.30.505.10; SH2 domain; 2.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF217; WU:FB59D01; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 2.
DR SUPFAM; SSF57362; BPTI-like; 3.
DR SUPFAM; SSF55550; SH2 domain; 2.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
DR PROSITE; PS50001; SH2; 1.
PE 4: Predicted;
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW SH2 domain {ECO:0000256|PROSITE-ProRule:PRU00191}.
FT DOMAIN 310..418
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT DOMAIN 585..635
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 646..696
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT NON_TER 727
FT /evidence="ECO:0000313|EMBL:CDW60492.1"
SQ SEQUENCE 727 AA; 83749 MW; A0F6EAA563498C0B CRC64;
MHDIVGPYAG VYKWLYKTAP FRQDLPSIPV DQLPYYHGRI RHELAAQRLC CNGDFLIYAE
GDEEPSLVLL VRDQFSKCVQ IDINYNQNHH FWIYPMDEEY GYSTVDALIR NHVNMSTTFK
LDECAFARLE HAVSSPEFLS SIRCEGKVDP VELRYFHEIA AQDAEEILCN SGDFILKRSD
KDAKAIDLMV RWEEEVKTMH GLGTLGNSVY PLFKTSTNLP DEHVYSLDDY LKSSVLCQHP
INGVLLKKPI FHATTNRSAI EDNAQPDEND GTLNTHELNE TAVQQAATSG GLMHTLLNYC
APRPISSLPY FHGYLSEEEA QTLLHNDGDF LLFIDKLDGQ LYVVLHKNRE MVADWHYREV
RTNFYNRAVF IRDKDKDLNY LTVDELIAYY QTYAVPIQEG AQWTTANEAN KEVLRYPVTS
CTCQKDIMLE VNTFRYNLSY YNMSLSDEKV SDLLVEEGDY LLRGRDYEED QLCVKWNRQI
HKLPVPKNGY DGNYTLPHKD PTLPEEHSIT LDGLLKTYVL CQIPYKGKRI FFRNVLSKRT
VKSKLTNTSS SVHMAKSQET LFFWTFCSLT KTLAQRAESR NEKSSEEVAD PGPCRGKFPR
YYYDWDSKQC TQFTYGGCEG NANNYDSIAE CEATCPGEEQ KPENPCELPS DSGPCMAYFT
KYYYNKESKK CETFVYGGCQ GNENRFDTLE ECEAKCAEEK PVKDPCKLPA DPGPCRGKFP
RYYYDWD
//