ID   FETJ_GLOBL              Reviewed;         324 AA.
AC   Q5KQS1;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Antihemorrhagic factor jMSF;
DE   AltName: Full=Japanese mamushi serum factor;
DE   Flags: Precursor;
OS   Gloydius blomhoffii (Mamushi) (Agkistrodon halys blomhoffi).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Gloydius.
OX   NCBI_TaxID=242054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-70; 189-231 AND 275-298,
RP   FUNCTION, GLYCOSYLATION AT ASN-204 AND ASN-282, AND MASS SPECTROMETRY.
RC   TISSUE=Liver, and Serum;
RX   PubMed=18037153; DOI=10.1016/j.toxicon.2007.09.007;
RA   Aoki N., Tsutsumi K., Deshimaru M., Terada S.;
RT   "Properties and cDNA cloning of antihemorrhagic factors in sera of Chinese
RT   and Japanese mamushi (Gloydius blomhoffi).";
RL   Toxicon 51:251-261(2008).
CC   -!- FUNCTION: Suppress hemorrhage induced by metalloproteinases from the
CC       same venom (brevilysin-H3, -H4, -H6) and from habu venom (weak
CC       inhibition of the metalloproteinases HR2A). The non-hemorrhagic
CC       brevilysin-H2 is strongly inhibited by jMSF, whereas the brevilysin-L6
CC       is not inhibited. Does not inhibit serine and cysteine proteases such
CC       as trypsin, chymotrypsin, thermolysin, and papain. The inhibition may
CC       occur by formation of a non-covalent complex between this protein and
CC       the proteinases at their metalloproteinase domains.
CC       {ECO:0000269|PubMed:18037153}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Expressed by the liver.
CC   -!- MASS SPECTROMETRY: Mass=40500; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:18037153};
CC   -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00861}.
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DR   EMBL; AB200172; BAD88539.1; -; mRNA.
DR   AlphaFoldDB; Q5KQS1; -.
DR   SMR; Q5KQS1; -.
DR   MEROPS; I25.042; -.
DR   iPTMnet; Q5KQS1; -.
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; 2.
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; PS01254; FETUIN_1; 1.
DR   PROSITE; PS01255; FETUIN_2; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein;
KW   Metalloenzyme inhibitor; Metalloprotease inhibitor; Protease inhibitor;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:18037153"
FT   CHAIN           20..324
FT                   /note="Antihemorrhagic factor jMSF"
FT                   /id="PRO_5000052212"
FT   DOMAIN          22..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   MOTIF           23..25
FT                   /note="Cell attachment site"
FT                   /evidence="ECO:0000255"
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:0000269|PubMed:18037153"
FT   CARBOHYD        282
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:18037153"
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"
FT   DISULFID        287..291
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   324 AA;  36663 MW;  B0912A254BECCB4D CRC64;
     MHFLVALVLL GQIIGSTLSS QVRGDLECDD REAKEWADQA VRYINEHKLH EYKQALNVIK
     NIVVVPWNGD LVAVFLKLNL LETECHVLDP TPVEKCTIRP QQNHAVEMDC DAKIMFDVET
     FKQDVFVKCH STPDSVEDVR RNCPKCPILL SPRDPHVVDS VEYVLNKHNE QLSGHVYEVL
     EISRGQHKYE PEAFYVEFAI VEVNCTAQEA HDDHHHCHPN TAGEDHIAFC KATVFRSHAS
     LEKPKHENFE SDCVILDVKE GHAHSHLIEH HIGKYSTSPG QNSTVECVAE CPVAFVNKEV
     PTDISDRHTT PVKGCPGKIL HFQL