ID L5LMM7_MYODS Unreviewed; 300 AA.
AC L5LMM7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Tissue factor pathway inhibitor {ECO:0000256|PIRNR:PIRNR001620};
GN ORFNames=MDA_GLEAN10023616 {ECO:0000313|EMBL:ELK27699.1};
OS Myotis davidii (David's myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=225400 {ECO:0000313|EMBL:ELK27699.1, ECO:0000313|Proteomes:UP000010556};
RN [1] {ECO:0000313|Proteomes:UP000010556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|PIRNR:PIRNR001620}.
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DR EMBL; KB109900; ELK27699.1; -; Genomic_DNA.
DR AlphaFoldDB; L5LMM7; -.
DR eggNOG; KOG4295; Eukaryota.
DR Proteomes; UP000010556; Unassembled WGS sequence.
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; 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 InterPro; IPR008296; TFPI-like.
DR PANTHER; PTHR10083; KUNITZ-TYPE PROTEASE INHIBITOR-RELATED; 1.
DR Pfam; PF00014; Kunitz_BPTI; 4.
DR PIRSF; PIRSF001620; TFPI; 3.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00131; KU; 4.
DR SUPFAM; SSF57362; BPTI-like; 4.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 4.
PE 4: Predicted;
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 Reference proteome {ECO:0000313|Proteomes:UP000010556};
KW Serine protease inhibitor {ECO:0000256|PIRNR:PIRNR001620};
KW Signal {ECO:0000256|PIRNR:PIRNR001620}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|PIRNR:PIRNR001620"
FT CHAIN 25..300
FT /note="Tissue factor pathway inhibitor"
FT /evidence="ECO:0000256|PIRNR:PIRNR001620"
FT /id="PRO_5011023966"
FT DOMAIN 43..93
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 102..152
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 161..211
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 222..272
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
SQ SEQUENCE 300 AA; 33499 MW; 94B11B14F52636D8 CRC64;
MRKTTLLWAS VCLLLSGAFR PLDAAPERED EEDADGTGRP DFCLLDPKVG RCRAHFNRYF
YNHHSGRCEL FVYGGCWGNL NNFVTEAECQ RYCGHPGRPG FCLLEAEVGP CRANFIRYFY
NHLSGRCEVF GYGGCEGNPN NFETEAECQR YCGHPGRPGF CLLEAEVGPC LALLKRYFYN
HLSGRCEEFM YGGCQGNPNN FETEAECQRS CGHPDFNLPS WCLTGADRGQ CTANVTRFYY
DSDAATCHTF SYSGCGGNEN NFVSERACLK ACTKARGTGM CTEGLAHHGT RLSQPQVLLR
//
