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 04-NOV-2026, entry version 118. 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. 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. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 AlphaFoldDB; P00799; -. DR SMR; P00799; -. DR Allergome; 3880; Rhi m AP. DR MEROPS; A01.013; -. DR GlyCosmos; P00799; 2 sites, No reported glycans. DR iPTMnet; P00799; -. DR EvolutionaryTrace; P00799; -. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR CDD; cd05471; pepsin_like; 1. DR FunFam; 2.40.70.10:FF:000008; Cathepsin D; 1. DR Gene3D; 2.40.70.10; Acid Proteases; 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:SF1; ASPARTYL PROTEINASE; 1. DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1. DR Pfam; PF00026; Asp; 1. DR PRINTS; PR00792; PEPSIN. DR SUPFAM; SSF50630; Acid proteases; 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..83 FT /evidence="ECO:0007829|PDB:2ASI" FT TURN 84..87 FT /evidence="ECO:0007829|PDB:2ASI" FT STRAND 88..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..118 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 //