CARP_RHICH
ID CARP_RHICH Reviewed; 393 AA.
AC P06026;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Rhizopuspepsin;
DE EC=3.4.23.21;
DE Flags: Precursor;
OS Rhizopus chinensis (Bread mold).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4843;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RA Gregoli P.A., Delaney R.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 42-393.
RX PubMed=3027093; DOI=10.1016/s0021-9258(19)75658-0;
RA Delaney R., Wong R.N.S., Meng G.-Z., Wu N.-H., Tang J.;
RT "Amino acid sequence of rhizopuspepsin isozyme pI 5.";
RL J. Biol. Chem. 262:1461-1467(1987).
RN [3]
RP PROTEIN SEQUENCE OF 69-393.
RX PubMed=3100534; DOI=10.1016/s0021-9258(19)75659-2;
RA Takahashi K.;
RT "The amino acid sequence of rhizopuspepsin, an aspartic proteinase from
RT Rhizopus chinensis.";
RL J. Biol. Chem. 262:1468-1478(1987).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-392.
RX PubMed=322132; DOI=10.1073/pnas.74.2.556;
RA Subramanian E., Swan I.D.A., Liu M., Davies D.R., Jenkins J.A.,
RA Tickle I.J., Blundell T.L.;
RT "Homology among acid proteases: comparison of crystal structures at 3-A
RT resolution of acid proteases from Rhizopus chinensis and Endothia
RT parasitica.";
RL Proc. Natl. Acad. Sci. U.S.A. 74:556-559(1977).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 69-392.
RX PubMed=3316666; DOI=10.1016/0022-2836(87)90411-6;
RA Suguna K., Bott R.R., Padlan E.A., Subramanian E., Sheriff S., Cohen G.H.,
RA Davies D.R.;
RT "Structure and refinement at 1.8-A resolution of the aspartic proteinase
RT from Rhizopus chinensis.";
RL J. Mol. Biol. 196:877-900(1987).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins with broad specificity similar to that
CC of pepsin A, preferring hydrophobic residues at P1 and P1'. Clots
CC milk and activates trypsinogen. Does not cleave 4-Gln-|-His-5, but
CC does cleave 10-His-|-Leu-11 and 12-Val-|-Glu-13 in B chain of
CC insulin.; EC=3.4.23.21;
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; L33859; AAB59306.1; -; Genomic_DNA.
DR EMBL; L33858; AAB59305.1; -; Genomic_DNA.
DR EMBL; J02651; AAA33879.1; -; mRNA.
DR PIR; A26681; A26681.
DR PIR; A41415; A41415.
DR PDB; 1UH7; X-ray; 2.10 A; A=69-392.
DR PDB; 1UH8; X-ray; 2.30 A; A=69-392.
DR PDB; 1UH9; X-ray; 2.00 A; A=69-392.
DR PDB; 2APR; X-ray; 1.80 A; A=69-392.
DR PDB; 3APR; X-ray; 1.80 A; E=69-392.
DR PDB; 4APR; X-ray; 2.50 A; E=69-392.
DR PDB; 5APR; X-ray; 2.10 A; E=69-392.
DR PDB; 6APR; X-ray; 2.50 A; E=69-392.
DR PDBsum; 1UH7; -.
DR PDBsum; 1UH8; -.
DR PDBsum; 1UH9; -.
DR PDBsum; 2APR; -.
DR PDBsum; 3APR; -.
DR PDBsum; 4APR; -.
DR PDBsum; 5APR; -.
DR PDBsum; 6APR; -.
DR AlphaFoldDB; P06026; -.
DR SMR; P06026; -.
DR BindingDB; P06026; -.
DR ChEMBL; CHEMBL4253; -.
DR MEROPS; A01.012; -.
DR EvolutionaryTrace; P06026; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06097; Aspergillopepsin_like; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034163; Aspergillopepsin-like_cat_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 Hydrolase; Protease; Signal; Zymogen.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT PROPEP 22..68
FT /note="Activation peptide"
FT /evidence="ECO:0000305|PubMed:3100534"
FT /id="PRO_0000025881"
FT CHAIN 69..393
FT /note="Rhizopuspepsin"
FT /id="PRO_0000025882"
FT DOMAIN 85..389
FT /note="Peptidase A1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01103"
FT ACT_SITE 103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT ACT_SITE 286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT DISULFID 116..119
FT DISULFID 320..353
FT VARIANT 83
FT /note="V -> I"
FT VARIANT 129
FT /note="K -> N"
FT VARIANT 184
FT /note="N -> S"
FT VARIANT 230
FT /note="S -> K"
FT VARIANT 298
FT /note="V -> I"
FT VARIANT 309
FT /note="S -> Y"
FT VARIANT 361
FT /note="N -> D"
FT VARIANT 393
FT /note="Q -> E"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:2APR"
FT TURN 80..83
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 84..91
FT /evidence="ECO:0007829|PDB:2APR"
FT TURN 92..95
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 110..113
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4APR"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 150..162
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 165..178
FT /evidence="ECO:0007829|PDB:2APR"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:2APR"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:2APR"
FT HELIX 207..213
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:2APR"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 235..239
FT /evidence="ECO:0007829|PDB:2APR"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 290..295
FT /evidence="ECO:0007829|PDB:2APR"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 312..314
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:2APR"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:2APR"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 345..349
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 352..367
FT /evidence="ECO:0007829|PDB:2APR"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 375..380
FT /evidence="ECO:0007829|PDB:2APR"
FT TURN 381..384
FT /evidence="ECO:0007829|PDB:2APR"
FT STRAND 385..391
FT /evidence="ECO:0007829|PDB:2APR"
SQ SEQUENCE 393 AA; 41327 MW; 479BBDB3D001D25C CRC64;
MKFTLISSCI AIAALAVAVD AAPGEKKISI PLAKNPNYKP SAKNAIQKAI AKYNKHKINT
STGGIVPDAG VGTVPMTDYG NDVEYYGQVT IGTPGKKFNL DFDTGSSDLW IASTLCTNCG
SRQTKYDPKQ SSTYQADGRT WSISYGDGSS ASGILAKDNV NLGGLLIKGQ TIELAKREAA
SFANGPNDGL LGLGFDTITT VRGVKTPMDN LISQGLISRP IFGVYLGKAS NGGGGEYIFG
GYDSTKFKGS LTTVPIDNSR GWWGITVDRA TVGTSTVASS FDGILDTGTT LLILPNNVAA
SVARAYGASD NGDGTYTISC DTSRFKPLVF SINGASFQVS PDSLVFEEYQ GQCIAGFGYG
NFDFAIIGDT FLKNNYVVFN QGVPEVQIAP VAQ
