PHYSA_PHYPO
ID PHYSA_PHYPO Reviewed; 575 AA.
AC Q8MZS4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Physarolisin;
DE EC=3.4.21.103;
DE AltName: Full=Physaropepsin;
DE Contains:
DE RecName: Full=Physarolisin heavy chain;
DE Contains:
DE RecName: Full=Physarolisin light chain;
DE Flags: Precursor;
OS Physarum polycephalum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Myxogastria;
OC Myxogastromycetidae; Physariida; Physaraceae; Physarum.
OX NCBI_TaxID=5791;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 222-224; 321-345; 390-396;
RP 442-457 AND 545-566, PH DEPENDENCE, ACTIVITY REGULATION, AND 3D-STRUCTURE
RP MODELING.
RC STRAIN=Ng-1;
RX PubMed=12589815; DOI=10.1016/s0006-291x(03)00083-4;
RA Nishii W., Ueki T., Miyashita R., Kojima M., Kim Y.-T., Sasaki N.,
RA Murakami-Murofushi K., Takahashi K.;
RT "Structural and enzymatic characterization of physarolisin (formerly
RT physaropepsin) proves that it is a unique serine-carboxyl proteinase.";
RL Biochem. Biophys. Res. Commun. 301:1023-1029(2003).
RN [2]
RP PROTEIN SEQUENCE OF 174-193 AND 390-394, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, GLYCOSYLATION, AND KINETIC PARAMETERS.
RX PubMed=2246266; DOI=10.1016/s0021-9258(17)45457-3;
RA Murakami-Murofushi K., Takahashi T., Minowa Y., Iino S., Takeuchi T.,
RA Kitagaki-Ogawa H., Murofushi H., Takahashi K.;
RT "Purification and characterization of a novel intracellular acid proteinase
RT from the plasmodia of a true slime mold, Physarum polycephalum.";
RL J. Biol. Chem. 265:19898-19903(1990).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Milk clotting activity. Preferential cleavage of 8-Gly-|-Ser-9
CC in B chain of insulin most rapidly, followed by 11-Leu-|-Val-12, 19-
CC Cys(SO(3)H)-|-Gly and 24-Phe-|-Phe-25. No action on Ac-Phe-Tyr(I)2.;
CC EC=3.4.21.103; Evidence={ECO:0000269|PubMed:2246266};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by diisopropylfluorophosphate (DFP) and
CC diazoacetyl-D,L-norleucine methyl ester (DAN).
CC {ECO:0000269|PubMed:12589815, ECO:0000269|PubMed:2246266}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=48.3 uM for Lys-Pro-Ile-Glu-Phe+Phe(NO(2))-Arg-Leu
CC {ECO:0000269|PubMed:2246266};
CC pH dependence:
CC Optimum pH is 1.7 with hemoglogin as substrate.
CC {ECO:0000269|PubMed:12589815};
CC -!- PTM: Autocatalytically processed.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:2246266}.
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DR EMBL; AF502290; AAM27198.1; -; mRNA.
DR AlphaFoldDB; Q8MZS4; -.
DR SMR; Q8MZS4; -.
DR MEROPS; S53.006; -.
DR KEGG; ag:AAM27198; -.
DR BRENDA; 3.4.21.103; 4800.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04056; Peptidases_S53; 1.
DR CDD; cd11377; Pro-peptidase_S53; 1.
DR Gene3D; 3.40.50.200; -; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015366; S53_propep.
DR InterPro; IPR030400; Sedolisin_dom.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF09286; Pro-kuma_activ; 1.
DR SMART; SM00944; Pro-kuma_activ; 1.
DR SUPFAM; SSF52743; SSF52743; 1.
DR PROSITE; PS51695; SEDOLISIN; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Glycoprotein; Hydrolase; Metal-binding;
KW Protease; Serine protease; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..173
FT /note="Removed in mature form"
FT /evidence="ECO:0000269|PubMed:2246266"
FT /id="PRO_0000298946"
FT CHAIN 174..575
FT /note="Physarolisin"
FT /id="PRO_0000298947"
FT CHAIN 174..389
FT /note="Physarolisin heavy chain"
FT /id="PRO_0000298948"
FT CHAIN 390..575
FT /note="Physarolisin light chain"
FT /id="PRO_0000298949"
FT DOMAIN 179..574
FT /note="Peptidase S53"
FT ACT_SITE 248
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 252
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 484
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 529
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 530
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 552
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 554
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 529
FT /note="DNA-binding"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 575 AA; 62709 MW; A538BDA91E473BC5 CRC64;
MRLLSLLFLL GLATLSFAVR SQWAQQGRAT HEALITIRFA LTQQNLDVLE RTLLDISDTT
SKNYGKWKTA EEVTELVAPA REISERVASF LERQGATKVE NFRDMVKVTA PVSWIEETLH
TNLFFFQHKT RTSKVIIRAD GGYKIPAEIA EHVDFVAGLF EFPSIKNART QVGAGVDGYI
VPYVIFDLYG IPTTFPVHPN SSICLVEFQD DQSYNKDDLK KFAKENEITE TVVSHTVGPY
SGSSADTEST LDVQYGGAIA LNTTVWFWTV EDWMYDFATD FLNTKNPPLV VSMSWGWPEP
EQCQVGNCTG DETSLEYVVR TNVEFQKIGA IGTTLLAASG DQGAPGDSDP ECNSKKKPLS
SIFPGASPWV LSVGATMLSN MTTEDADPSA EPPICKSWTC STSTTELVCT IPQALITTGG
GFSDYSLQPS YQNAAVAAYF KSGVPLPPQT DFNASNRGFP DVSALGHNYL IALSGDFEQV
DGTSASTPVF AAIIAHLNSY RLNNGKPPLA FAVPLIYQAF ASDPTIFNDI TTGDNKCTED
CCSKFGYEAT KGWDPVTGVG TPVFSKLLAF VQTLP
