CARP_RHIMI
ID CARP_RHIMI Reviewed; 430 AA.
AC P00799;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Mucorpepsin;
DE EC=3.4.23.23;
DE AltName: Full=Mucor rennin;
DE Flags: Precursor;
OS Rhizomucor miehei.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Rhizomucor.
OX NCBI_TaxID=4839;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3549462; DOI=10.1016/0378-1119(86)90350-1;
RA Gray G.L., Hayenga K., Cullen D., Wilson L.J., Norton S.;
RT "Primary structure of Mucor miehei aspartyl protease: evidence for a
RT zymogen intermediate.";
RL Gene 48:41-53(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3329734; DOI=10.1002/prot.340010409;
RA Boel E., Bech A.-M., Randrup K., Draeger B., Fiil N.P., Foltmann B.;
RT "Primary structure of a precursor to the aspartic proteinase from
RT Rhizomucor miehei shows that the enzyme is synthesized as a zymogen.";
RL Proteins 1:363-369(1986).
RN [3]
RP PROTEIN SEQUENCE OF 70-430.
RA Bech A.-M., Foltmann B.;
RT "Partial primary structure of Mucor miehei protease.";
RL Neth. Milk Dairy J. 35:275-280(1981).
RN [4]
RP SEQUENCE REVISION.
RA Foltmann B.;
RL Submitted (NOV-1982) to the PIR data bank.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=15299327; DOI=10.1107/s090744499401156x;
RA Jia Z., Vandonselaar M., Schneider P., Quail J.W.;
RT "Crystallization and preliminary X-ray structure solution of Rhizomucor
RT miehei aspartic proteinase.";
RL Acta Crystallogr. D 51:243-244(1995).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
RX PubMed=9159482; DOI=10.1006/jmbi.1997.0968;
RA Yang J., Teplyakov A., Quail J.W.;
RT "Crystal structure of the aspartic proteinase from Rhizomucor miehei at
RT 2.15-A resolution.";
RL J. Mol. Biol. 268:449-459(1997).
CC -!- FUNCTION: This enzyme, capable of clotting milk is frequently used for
CC cheese production.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins, favoring hydrophobic residues at P1
CC and P1'. Clots milk. Does not accept Lys at P1, and hence does not
CC activate trypsinogen.; EC=3.4.23.23;
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; M18411; AAA33423.1; -; mRNA.
DR EMBL; M15267; AAA33421.1; -; Genomic_DNA.
DR PIR; A29039; CMUMF.
DR PDB; 2ASI; X-ray; 2.15 A; A=70-430.
DR PDB; 2RMP; X-ray; 2.70 A; A=70-430.
DR PDBsum; 2ASI; -.
DR PDBsum; 2RMP; -.
DR AlphaFoldDB; P00799; -.
DR SMR; P00799; -.
DR Allergome; 3880; Rhi m AP.
DR MEROPS; A01.013; -.
DR iPTMnet; P00799; -.
DR EvolutionaryTrace; P00799; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; PTHR47966; 1.
DR Pfam; PF00026; Asp; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; SSF50630; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Hydrolase; Protease; Signal; Zymogen.
FT SIGNAL 1..22
FT PROPEP 23..69
FT /note="Activation peptide"
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000025893"
FT CHAIN 70..430
FT /note="Mucorpepsin"
FT /evidence="ECO:0000269|PubMed:3329734"
FT /id="PRO_0000025894"
FT DOMAIN 89..421
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3329734"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:3329734"
FT DISULFID 120..126
FT /evidence="ECO:0000269|PubMed:3329734"
FT DISULFID 341..385
FT /evidence="ECO:0000269|PubMed:3329734"
FT VARIANT 262
FT /note="G -> S"
FT CONFLICT 136
FT /note="A -> T (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 163..169
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 392
FT /note="D -> N (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="V -> Y (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="Missing (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:2ASI"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 89..95
FT /evidence="ECO:0007829|PDB:2ASI"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 141..149
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 156..169
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 171..183
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 223..229
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 232..241
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 244..254
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 292..306
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:2ASI"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 322..326
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:2RMP"
FT STRAND 334..336
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:2ASI"
FT TURN 341..345
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 350..357
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 364..371
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 375..392
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 401..404
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:2ASI"
FT TURN 413..416
FT /evidence="ECO:0007829|PDB:2ASI"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:2ASI"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:2ASI"
SQ SEQUENCE 430 AA; 46168 MW; 1431DB2435B71CEF CRC64;
MLFSQITSAI LLTAASLSLT TARPVSKQSE SKDKLLALPL TSVSRKFSQT KFGQQQLAEK
LAGLKPFSEA AADGSVDTPG YYDFDLEEYA IPVSIGTPGQ DFLLLFDTGS SDTWVPHKGC
TKSEGCVGSR FFDPSASSTF KATNYNLNIT YGTGGANGLY FEDSIAIGDI TVTKQILAYV
DNVRGPTAEQ SPNADIFLDG LFGAAYPDNT AMEAEYGSTY NTVHVNLYKQ GLISSPLFSV
YMNTNSGTGE VVFGGVNNTL LGGDIAYTDV MSRYGGYYFW DAPVTGITVD GSAAVRFSRP
QAFTIDTGTN FFIMPSSAAS KIVKAALPDA TETQQGWVVP CASYQNSKST ISIVMQKSGS
SSDTIEISVP VSKMLLPVDQ SNETCMFIIL PDGGNQYIVG NLFLRFFVNV YDFGNNRIGF
APLASAYENE
