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 04-NOV-2026, entry version 128. 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. 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. 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}. 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; 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=69-393. DR PDB; 1UH8; X-ray; 2.30 A; A=69-393. DR PDB; 1UH9; X-ray; 2.00 A; A=69-393. DR PDB; 2APR; X-ray; 1.80 A; A=69-393. DR PDB; 3APR; X-ray; 1.80 A; E=69-393. DR PDB; 4APR; X-ray; 2.50 A; E=69-393. DR PDB; 5APR; X-ray; 2.10 A; E=69-393. DR PDB; 6APR; X-ray; 2.50 A; E=69-393. DR PDB; 8FXQ; X-ray; 1.21 A; A/B=65-393. DR AlphaFoldDB; P06026; -. DR MDposit; P06026; -. DR MDRepo; P06026; -. DR SMR; P06026; -. DR BindingDB; P06026; -. DR ChEMBL; CHEMBL4253; -. DR MEROPS; A01.012; -. DR OMA; ADCWVWS; -. DR EvolutionaryTrace; P06026; -. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR GO; GO:0006508; P:proteolysis; IEA:InterPro. DR CDD; cd06097; Aspergillopepsin_like; 1. DR FunFam; 2.40.70.10:FF:000115; Lysosomal aspartic protease; 1. DR Gene3D; 2.40.70.10; Acid Proteases; 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: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 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 72..79 FT /evidence="ECO:0007829|PDB:8FXQ" FT TURN 80..83 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 84..91 FT /evidence="ECO:0007829|PDB:8FXQ" FT TURN 92..95 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 96..103 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 121..123 FT /evidence="ECO:0007829|PDB:4APR" FT HELIX 128..130 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 135..144 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 150..162 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 165..178 FT /evidence="ECO:0007829|PDB:8FXQ" FT HELIX 180..183 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 188..192 FT /evidence="ECO:0007829|PDB:8FXQ" FT HELIX 196..198 FT /evidence="ECO:0007829|PDB:8FXQ" FT HELIX 207..213 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 221..226 FT /evidence="ECO:0007829|PDB:8FXQ" FT HELIX 229..231 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 235..239 FT /evidence="ECO:0007829|PDB:8FXQ" FT HELIX 244..246 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 252..255 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 264..267 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 269..272 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 275..278 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 281..285 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 289..294 FT /evidence="ECO:0007829|PDB:8FXQ" FT HELIX 296..306 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 312..314 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 316..318 FT /evidence="ECO:0007829|PDB:8FXQ" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:2APR" FT STRAND 328..332 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 335..339 FT /evidence="ECO:0007829|PDB:8FXQ" FT HELIX 341..344 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 345..349 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 352..359 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 363..367 FT /evidence="ECO:0007829|PDB:8FXQ" FT HELIX 369..372 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 375..380 FT /evidence="ECO:0007829|PDB:8FXQ" FT TURN 381..384 FT /evidence="ECO:0007829|PDB:8FXQ" FT STRAND 385..391 FT /evidence="ECO:0007829|PDB:8FXQ" 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 //