FETAF_PROFL
ID FETAF_PROFL Reviewed; 342 AA.
AC P29695; Q98TC1;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Antihemorrhagic factor HSF;
DE AltName: Full=Habu serum factor;
DE AltName: Full=Metalloproteinase inhibitor;
DE Flags: Precursor;
OS Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC Serpentes; Colubroidea; Viperidae; Crotalinae; Protobothrops.
OX NCBI_TaxID=88087;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-67, FUNCTION, BINDING TO
RP BREVILYSIN H6, AND MASS SPECTROMETRY.
RC TISSUE=Liver, and Serum;
RX PubMed=16289179; DOI=10.1016/j.toxicon.2005.09.003;
RA Deshimaru M., Tanaka C., Fujino K., Aoki N., Terada S., Hattori S.,
RA Ohno M.;
RT "Properties and cDNA cloning of an antihemorrhagic factor (HSF) purified
RT from the serum of Trimeresurus flavoviridis.";
RL Toxicon 46:937-945(2005).
RN [2]
RP PROTEIN SEQUENCE OF 20-342, AND GLYCOSYLATION AT ASN-142; ASN-204 AND
RP ASN-282.
RC TISSUE=Serum;
RX PubMed=1478916; DOI=10.1093/oxfordjournals.jbchem.a123944;
RA Yamakawa Y., Omori-Satoh T.;
RT "Primary structure of the antihemorrhagic factor in serum of the Japanese
RT Habu: a snake venom metalloproteinase inhibitor with a double-headed
RT cystatin domain.";
RL J. Biochem. 112:583-589(1992).
RN [3]
RP PROTEIN SEQUENCE OF 20-54; 61-81; 123-142 AND 331-342, GLYCOSYLATION AT
RP ASN-142, DISULFIDE BOND, REGION, AND 3D-STRUCTURE MODELING.
RC TISSUE=Serum;
RX PubMed=17222882; DOI=10.1016/j.toxicon.2006.11.001;
RA Aoki N., Deshimaru M., Terada S.;
RT "Active fragments of the antihemorrhagic protein HSF from serum of habu
RT (Trimeresurus flavoviridis).";
RL Toxicon 49:653-662(2007).
CC -!- FUNCTION: Inhibits hemorrhagic and proteolytic activities of
CC metalloproteinases (HR1A, HR1B, HR2a, HR2b and H2 proteinase from
CC T.flavodidis and brevilysins H3, H4, H6 and L4 from A.halys
CC brevicaudus). Has no effect on brevilysins H2. Has no effect on papain
CC and cathepsin-B. {ECO:0000269|PubMed:16289179}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver.
CC -!- PTM: Cys-63 may exist in a mixed disulfide form with a thiol compound
CC such as glutathione.
CC -!- MASS SPECTROMETRY: Mass=47810; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:16289179};
CC -!- MISCELLANEOUS: Is highly stable to extreme pH and heating, stability
CC that may be conferred by the disulfide bond between Cys-28 and Cys-332.
CC -!- SIMILARITY: Belongs to the fetuin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00861}.
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DR EMBL; AB058635; BAB39858.1; -; mRNA.
DR PIR; JX0240; JX0240.
DR AlphaFoldDB; P29695; -.
DR SMR; P29695; -.
DR MEROPS; I25.026; -.
DR MEROPS; I25.042; -.
DR iPTMnet; P29695; -.
DR PRIDE; P29695; -.
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:1478916,
FT ECO:0000269|PubMed:16289179, ECO:0000269|PubMed:17222882"
FT CHAIN 20..342
FT /note="Antihemorrhagic factor HSF"
FT /id="PRO_0000138376"
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 REGION 24..108
FT /note="Indispensable for metalloproteinase inhibition"
FT MOTIF 23..25
FT /note="Cell attachment site"
FT SITE 140..141
FT /note="Cleavage; by trypsin"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1478916,
FT ECO:0000269|PubMed:17222882"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1478916"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1478916"
FT DISULFID 28..332
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00861,
FT ECO:0000269|PubMed:17222882"
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 CONFLICT 20
FT /note="S -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="S -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="K -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 38916 MW; F9B45B00B489A519 CRC64;
MNSLVALVLL GQIIGSTLSS QVRGDLECDD KEAKNWADDA VRYINEHKLH GHKQALNVIK
NICVVPWNGD LVAVFLELNL LETECHVLDP TPVEKCTVRQ QHNHAVEMDC DAKIMFNVET
FKRDVFVKCH STPDSVENVR RNCSKCPILL PPNNPHVVDS VEYVLNKHNE KLSGHIYEVL
EISRGQHKYE PEAYYLEFVI VEINCTAQEA HDDHHQCHPY TAGEDHIAFC RSTVFRSHAS
LEKPKDEKFE SNCVILDVKD GHAHSHLIQQ HIEKNSISPE HNITILNFVH PDDHTSTSHE
SHEHVAEVPV VFVKKELPTD ISDHHTTPVK GCPGKVHHFK LY
