CARP_RHIPU
ID CARP_RHIPU Reviewed; 427 AA.
AC P09177;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Mucorpepsin;
DE EC=3.4.23.23;
DE AltName: Full=Mucor rennin;
DE Flags: Precursor;
OS Rhizomucor pusillus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Rhizomucor.
OX NCBI_TaxID=4840;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=IFO 4578(+);
RX PubMed=3534790; DOI=10.1093/nar/14.19.7557;
RA Tonouchi N., Shoun H., Uozumi T., Beppu T.;
RT "Cloning and sequencing of a gene for Mucor rennin, an aspartate protease
RT from Mucor pusillus.";
RL Nucleic Acids Res. 14:7557-7568(1986).
RN [2]
RP PROTEIN SEQUENCE OF 67-427.
RX PubMed=3042459; DOI=10.1016/0014-5793(88)81277-8;
RA Baudys M., Foundling S., Pavlik M., Blundell T.L., Kostka V.;
RT "Protein chemical characterization of Mucor pusillus aspartic proteinase.
RT Amino acid sequence homology with the other aspartic proteinases, disulfide
RT bond arrangement and site of carbohydrate attachment.";
RL FEBS Lett. 235:271-274(1988).
RN [3]
RP SEQUENCE REVISION TO 22, AND PROTEOLYTIC PROCESSING.
RX PubMed=2506185; DOI=10.1016/s0021-9258(19)84786-5;
RA Hiramatsu R., Aikawa J., Horinouchi S., Beppu T.;
RT "Secretion by yeast of the zymogen form of Mucor rennin, an aspartic
RT proteinase of Mucor pusillus, and its conversion to the mature form.";
RL J. Biol. Chem. 264:16862-16866(1989).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=8450540; DOI=10.1006/jmbi.1993.1141;
RA Newman M., Watson F., Roychowdhury P., Jones H., Badassi M., Cleasby A.,
RA Wood S.P., Tickle I.J., Blundell T.L.;
RT "X-ray analyses of aspartic proteinases. V. Structure and refinement at
RT 2.0-A resolution of the aspartic proteinase from Mucor pusillus.";
RL J. Mol. Biol. 230:260-283(1993).
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; X06219; CAA29568.1; ALT_SEQ; Genomic_DNA.
DR PIR; A25767; A25767.
DR PDB; 1MPP; X-ray; 2.00 A; A=67-426.
DR PDBsum; 1MPP; -.
DR AlphaFoldDB; P09177; -.
DR SMR; P09177; -.
DR MEROPS; A01.013; -.
DR KEGG; ag:CAA29568; -.
DR EvolutionaryTrace; P09177; -.
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..66
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:3042459"
FT /id="PRO_0000025895"
FT CHAIN 67..427
FT /note="Mucorpepsin"
FT /id="PRO_0000025896"
FT DOMAIN 86..418
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 104
FT ACT_SITE 303
FT CARBOHYD 254
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 117..123
FT DISULFID 338..382
FT CONFLICT 427
FT /note="N -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:1MPP"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:1MPP"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 111..114
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 138..147
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 152..164
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 167..182
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 229..238
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 242..252
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 273..286
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 289..303
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 313..323
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 333..337
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 338..341
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 347..353
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 361..367
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 368..371
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 381..392
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:1MPP"
FT HELIX 398..401
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:1MPP"
FT TURN 410..413
FT /evidence="ECO:0007829|PDB:1MPP"
FT STRAND 414..420
FT /evidence="ECO:0007829|PDB:1MPP"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:1MPP"
SQ SEQUENCE 427 AA; 45646 MW; DB560157A5D99BCF CRC64;
MLFSKISSAI LLTAASFALT SARPVSKQSD ADDKLLALPL TSVNRKYSQT KHGQQAAEKL
GGIKAFAEGD GSVDTPGLYD FDLEEYAIPV SIGTPGQDFY LLFDTGSSDT WVPHKGCDNS
EGCVGKRFFD PSSSSTFKET DYNLNITYGT GGANGIYFRD SITVGGATVK QQTLAYVDNV
SGPTAEQSPD SELFLDGMFG AAYPDNTAME AEYGDTYNTV HVNLYKQGLI SSPVFSVYMN
TNDGGGQVVF GGANNTLLGG DIQYTDVLKS RGGYFFWDAP VTGVKIDGAD AVSFDGAQAF
TIDTGTNFFI APSSFAEKVV KAALPDATES QQGYTVPCSK YQDSKTTFSL VLQKSGSSSD
TIDVSVPISK MLLPVDKSGE TCMFIVLPDG GNQFIVGNLF LRFFVNVYDF GKNRIGFAPL
ASGYENN
