ID V9KIY9_CALMI Unreviewed; 234 AA.
AC V9KIY9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Tissue factor pathway inhibitor {ECO:0000256|PIRNR:PIRNR001620};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO98389.1};
RN [1] {ECO:0000313|EMBL:AFO98389.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Gills {ECO:0000313|EMBL:AFO98389.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|PIRNR:PIRNR001620}.
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; JW865872; AFO98389.1; -; mRNA.
DR AlphaFoldDB; V9KIY9; -.
DR MEROPS; I02.951; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-UniRule.
DR CDD; cd22617; Kunitz_TFPI2_2-like; 2.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 3.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR008296; TFPI-like.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR PANTHER; PTHR10083:SF352; TISSUE FACTOR PATHWAY INHIBITOR 2; 1.
DR Pfam; PF00014; Kunitz_BPTI; 3.
DR PIRSF; PIRSF001620; TFPI; 2.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 3.
DR SUPFAM; SSF57362; BPTI-like; 3.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 3.
PE 2: Evidence at transcript level;
KW Blood coagulation {ECO:0000256|ARBA:ARBA00023084,
KW ECO:0000256|PIRNR:PIRNR001620};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Hemostasis {ECO:0000256|ARBA:ARBA00022696, ECO:0000256|PIRNR:PIRNR001620};
KW Protease inhibitor {ECO:0000256|PIRNR:PIRNR001620};
KW Serine protease inhibitor {ECO:0000256|PIRNR:PIRNR001620};
KW Signal {ECO:0000256|PIRNR:PIRNR001620}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|PIRNR:PIRNR001620"
FT CHAIN 23..234
FT /note="Tissue factor pathway inhibitor"
FT /evidence="ECO:0000256|PIRNR:PIRNR001620"
FT /id="PRO_5011023987"
FT DOMAIN 29..79
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 89..139
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 149..199
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 234 AA; 26700 MW; 552BC43C74621C33 CRC64;
MAFNLFTAIC SIWILSAPCS LAKDNREICL QLPDRGPCRA MLTQYFYNRY TQKCEEFEYG
GCMGNDNLFE TMSHCNSACL RIKVVPKVCR LMAATGPGRA LFTRYHYNLT SDRCEEFTYG
GLFENGNIFR DKASCQRRCK PVNPMPSFCA AASDRGRCSA DVLRYYFNVK THTCETFSYS
GCGGNDNNFT SAKVCQQVCQ KRNKKKTSQK YPTASITRKV VKKNSRKKFL KNPY
//
