ID   FETCB_GLOBR             Reviewed;         342 AA.
AC   Q5KQS2;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Antihemorrhagic factor cHLP-B;
DE   AltName: Full=Chinese mamushi HSF-like protein B;
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}.
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; AB200171; BAD88538.1; -; mRNA.
DR   AlphaFoldDB; Q5KQS2; -.
DR   SMR; Q5KQS2; -.
DR   MEROPS; I25.042; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; 2.
DR   InterPro; IPR000010; Cystatin_dom.
DR   InterPro; IPR025760; Cystatin_Fetuin_A.
DR   InterPro; IPR046350; Cystatin_sf.
DR   Pfam; PF00031; Cystatin; 1.
DR   SMART; SM00043; CY; 2.
DR   SUPFAM; SSF54403; SSF54403; 2.
DR   PROSITE; PS51529; CYSTATIN_FETUIN_A; 2.
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..342
FT                   /note="Antihemorrhagic factor cHLP-B"
FT                   /id="PRO_5000052211"
FT   DOMAIN          20..129
FT                   /note="Cystatin fetuin-A-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DOMAIN          140..253
FT                   /note="Cystatin fetuin-A-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   SITE            139..140
FT                   /note="Cleavage; by trypsin"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        95
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        281
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..333
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        85..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        110..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        142..145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        204..216
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
FT   DISULFID        229..252
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00861"
SQ   SEQUENCE   342 AA;  38504 MW;  8ECC8CF9FCAAE9E5 CRC64;
     MNSLVALVLL GQMIGSTLSH HLQSHVDCNG EDAEKWADMA VHYINEHNLH GYKQVFNVIN
     EIHVLPRRPR GKIIILELKL LETECHVLDP TPVENCTVRP PHYHAVEGDC DVKILHDEGV
     DKVIGAKCHS DPDSVEDVRR NCPKCPILLP LSDPHVVDSV EYVLNKHNEK LSGHVYEVLE
     ISRGQHKYEP EAFYVEFAIV EVNCTAQEAH DDHHHCHPNT AGENHIGFCR ATVFRSHASL
     EKPKDEQFES DCVIFDVKEG HAHSHLIEHH IGNYNTSPGH NNTVLNLAHS HNHTSASHES
     HSHEHVAEVP VAVAKREVPT NTPHDHTHPV KLCPGKVHHF KL