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Proclotting enzyme (EC 3.4.21.86) [Cleaved into: Proclotting enzyme light chain; Proclotting enzyme heavy chain]

 PCE_TACTR               Reviewed;         375 AA.
P21902;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
23-MAY-2018, entry version 103.
RecName: Full=Proclotting enzyme;
EC=3.4.21.86 {ECO:0000269|PubMed:2266134, ECO:0000269|PubMed:977558};
Contains:
RecName: Full=Proclotting enzyme light chain {ECO:0000303|PubMed:2266134};
Contains:
RecName: Full=Proclotting enzyme heavy chain {ECO:0000303|PubMed:2266134};
Flags: Precursor;
Tachypleus tridentatus (Japanese horseshoe crab).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
Xiphosura; Limulidae; Tachypleus.
NCBI_TaxID=6853;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
DOMAIN, PROTEOLYTIC CLEAVAGE, DISULFIDE BONDS, GLYCOSYLATION AT
ASN-122; ASN-235 AND ASN-304, AND PYROGLUTAMATE FORMATION AT GLN-30.
TISSUE=Hemocyte;
PubMed=2266134;
Muta T., Hashimoto R., Miyata T., Nishimura H., Toh Y., Iwanaga S.;
"Proclotting enzyme from horseshoe crab hemocytes. cDNA cloning,
disulfide locations, and subcellular localization.";
J. Biol. Chem. 265:22426-22433(1990).
[2]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=977558;
Nakamura S., Takagi T., Iwanaga S., Niwa M., Takahashi K.;
"A clottable protein (coagulogen) of horseshoe crab hemocytes.
Structural change of its polypeptide chain during gel formation.";
J. Biochem. 80:649-652(1976).
[3]
CATALYTIC ACTIVITY, SUBUNIT, PROTEOLYTIC CLEAVAGE, DISULFIDE BOND, AND
GLYCOSYLATION.
PubMed=4030738;
Nakamura T., Morita T., Iwanaga S.;
"Intracellular proclotting enzyme in limulus (Tachypleus tridentatus)
hemocytes: its purification and properties.";
J. Biochem. 97:1561-1574(1985).
-!- FUNCTION: This enzyme is closely associated with an endotoxin-
sensitive hemolymph coagulation system in limulus
(PubMed:2266134). Its active form catalyzes the conversion of
coagulogen to insoluble coagulin gel (PubMed:977558).
{ECO:0000269|PubMed:977558, ECO:0000303|PubMed:2266134}.
-!- CATALYTIC ACTIVITY: Selective cleavage of 18-Arg-|- and 47-
Arg-|- bonds in coagulogen to form coagulin and fragments.
{ECO:0000269|PubMed:977558, ECO:0000305|PubMed:4030738}.
-!- SUBUNIT: In the active form, heterodimer of a light chain and a
heavy chain; disulfide-linked. {ECO:0000269|PubMed:2266134,
ECO:0000269|PubMed:4030738}.
-!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle
{ECO:0000269|PubMed:2266134}. Secreted
{ECO:0000269|PubMed:2266134}. Note=Secreted in hemolymph probably
upon bacterial lipopolysaccharide (LPS) stimulation.
{ECO:0000303|PubMed:2266134}.
-!- TISSUE SPECIFICITY: Expressed in hemocytes.
{ECO:0000269|PubMed:2266134}.
-!- DOMAIN: The CLIP domain consists of 37-55 residues which are
"knitted" together usually by 3 conserved disulfide bonds forming
a clip-like compact structure. {ECO:0000269|PubMed:2266134}.
-!- PTM: Proteolytically cleaved into its mature active form by serine
protease factor B. Cleavage produces a 25 kDa light chain
containing the CLIP domain and a catalytic 31 kDa heavy chain
which remain covalently associated through an interchain disulfide
bond. {ECO:0000269|PubMed:2266134, ECO:0000269|PubMed:4030738}.
-!- PTM: Contains six O-linked carbohydrate chains in the N-terminal
light chain. {ECO:0000269|PubMed:2266134,
ECO:0000269|PubMed:4030738}.
-!- SIMILARITY: Belongs to the peptidase S1 family. CLIP subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M58366; AAA30094.1; -; mRNA.
PIR; A23689; A23689.
ProteinModelPortal; P21902; -.
SMR; P21902; -.
MEROPS; S01.221; -.
PRIDE; P21902; -.
KEGG; ag:AAA30094; -.
KO; K20753; -.
PMAP-CutDB; P21902; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0042381; P:hemolymph coagulation; IEA:UniProtKB-KW.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.20.20.90; -; 1.
InterPro; IPR022700; CLIP.
InterPro; IPR038565; CLIP_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00680; CLIP; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Calcium; Cleavage on pair of basic residues; Cytoplasmic vesicle;
Direct protein sequencing; Disulfide bond; Glycoprotein;
Hemolymph clotting; Hydrolase; Metal-binding; Protease;
Pyrrolidone carboxylic acid; Secreted; Serine protease; Signal;
Zymogen.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 27 {ECO:0000305|PubMed:2266134}.
/FTId=PRO_0000028427.
CHAIN 30 127 Proclotting enzyme light chain.
{ECO:0000305|PubMed:2266134}.
/FTId=PRO_0000028428.
CHAIN 128 375 Proclotting enzyme heavy chain.
{ECO:0000305|PubMed:2266134}.
/FTId=PRO_0000028429.
DOMAIN 40 85 CLIP. {ECO:0000255}.
DOMAIN 128 375 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 172 172 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 228 228 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
ACT_SITE 326 326 Charge relay system.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
METAL 194 194 Calcium. {ECO:0000250|UniProtKB:O97366}.
METAL 196 196 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O97366}.
METAL 199 199 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:O97366}.
METAL 202 202 Calcium. {ECO:0000250|UniProtKB:O97366}.
SITE 127 128 Cleavage. {ECO:0000269|PubMed:2266134}.
MOD_RES 30 30 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:2266134}.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2266134}.
CARBOHYD 235 235 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2266134}.
CARBOHYD 304 304 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:2266134}.
DISULFID 40 83 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:2266134}.
DISULFID 50 73 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:2266134}.
DISULFID 56 84 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:2266134}.
DISULFID 118 248 Interchain (between light and heavy
chains). {ECO:0000269|PubMed:2266134,
ECO:0000269|PubMed:4030738}.
DISULFID 157 173 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:2266134}.
DISULFID 295 311 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:2266134}.
DISULFID 322 351 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:2266134}.
SEQUENCE 375 AA; 41592 MW; 94209E514DFCF8FB CRC64;
MLVNNVFSLL CFPLLMSVVR CSTLSRQRRQ FVFPDEEELC SNRFTEEGTC KNVLDCRILL
QKNDYNLLKE SICGFEGITP KVCCPKSSHV ISSTQAPPET TTTERPPKQI PPNLPEVCGI
HNTTTTRIIG GREAPIGAWP WMTAVYIKQG GIRSVQCGGA LVTNRHVITA SHCVVNSAGT
DVMPADVFSV RLGEHNLYST DDDSNPIDFA VTSVKHHEHF VLATYLNDIA ILTLNDTVTF
TDRIRPICLP YRKLRYDDLA MRKPFITGWG TTAFNGPSSA VLREVQLPIW EHEACRQAYE
KDLNITNVYM CAGFADGGKD ACQGDSGGPM MLPVKTGEFY LIGIVSFGKK CALPGFPGVY
TKVTEFLDWI AEHMV


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