ID   FETCA_GLOBR             Reviewed;         324 AA.
AC   Q5KQS3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Antihemorrhagic factor cHLP-A;
DE   AltName: Full=Chinese mamushi HSF-like protein A;
DE   Flags: Precursor;
OS   Gloydius brevicaudus (Korean slamosa snake) (Agkistrodon halys
OS   brevicaudus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=259325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Aoki N., Tsutsumi K., Deshimaru M., Terada S.;
RT   "A fetuin family antihemorrhagic factor and its homologous proteins in
RT   Chinese mamushi snake serum.";
RL   Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Potent inhibitor of hemorrhagic activity but also proteolytic
CC       activities. Inhibition occurs by formation of a non-covalent complex
CC       between this protein and the proteinases at their metalloproteinase
CC       domains (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC   -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00861}.
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DR   EMBL; AB200170; BAD88537.1; -; mRNA.
DR   AlphaFoldDB; Q5KQS3; -.
DR   SMR; Q5KQS3; -.
DR   MEROPS; I25.026; -.
DR   MEROPS; I25.042; -.
DR   PRIDE; Q5KQS3; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004869; F:cysteine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   CDD; cd00042; CY; 1.
DR   InterPro; IPR000010; Cystatin_dom.
DR   InterPro; IPR025760; Cystatin_Fetuin_A.
DR   InterPro; IPR046350; Cystatin_sf.
DR   InterPro; IPR001363; Prot_inh_fetuin_CS.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 2.
DR   SUPFAM; SSF54403; SSF54403; 2.
DR   PROSITE; PS51529; CYSTATIN_FETUIN_A; 2.
DR   PROSITE; PS01255; FETUIN_2; 1.
PE   2: Evidence at transcript level;
KW   Disulfide bond; Glycoprotein; Metalloenzyme inhibitor;
KW   Metalloprotease inhibitor; Protease inhibitor; Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..324
FT                   /note="Antihemorrhagic factor cHLP-A"
FT                   /id="PRO_5000052210"
FT   DOMAIN          21..130
FT                   /note="Cystatin fetuin-A-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DOMAIN          141..254
FT                   /note="Cystatin fetuin-A-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   SITE            140..141
FT                   /note="Cleavage; by trypsin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        204
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..315
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        85..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        110..129
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        143..146
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        205..217
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        230..253
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
SQ   SEQUENCE   324 AA;  36585 MW;  9A340BB7DA9FEB20 CRC64;
     MNSLVALVLL GQIIGSTLSF QLGPNMDCNT KGTKDWADIG VRYINEHKLD GYKNALNIIK
     IFRLLPSDGR SVIVHFKLNL LETKCHVLDP TPVENCAVRQ QHNHAVEMDC NVRIIHDIAT
     FEDEVFVKCK STPDSVENVR RNCPKCPILL PPNDPHVVDS VEYVLNKHNE KLSGHVYEVL
     EISRGQHKYE PEAFYVEFAI VEVNCTAQEA RDGHHQCHPY TAGEDHIAFC RATVFRSHAS
     LEKPKDENFE SDCVILDVKE GHAHSHLIQQ HIEKYSTSPG HNSTDEYVVE CPVAFVEKEV
     PTDMSDHDTP PVKGCPGRVL HFQL