PRTA_ASPNG
ID PRTA_ASPNG Reviewed; 282 AA.
AC P24665;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Aspergillopepsin-2;
DE EC=3.4.23.19;
DE AltName: Full=Acid protease A;
DE AltName: Full=Aspergillopepsin II;
DE AltName: Full=Proctase A;
DE Contains:
DE RecName: Full=Aspergillopepsin-2 light chain;
DE AltName: Full=Aspergillopepsin II light chain;
DE Contains:
DE RecName: Full=Aspergillopepsin-2 heavy chain;
DE AltName: Full=Aspergillopepsin II heavy chain;
DE Flags: Precursor;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Var. Macrosporus;
RX PubMed=1918060; DOI=10.1016/s0021-9258(18)55022-5;
RA Inoue H., Kimura T., Makabe O., Takahashi K.;
RT "The gene and deduced protein sequences of the zymogen of Aspergillus niger
RT acid proteinase A.";
RL J. Biol. Chem. 266:19484-19489(1991).
RN [2]
RP PROTEIN SEQUENCE OF 60-98 AND 110-282, AND PYROGLUTAMATE FORMATION AT
RP GLN-110.
RC STRAIN=Var. Macrosporus;
RX PubMed=1918059; DOI=10.1016/s0021-9258(18)55021-3;
RA Takahashi K., Inoue H., Sakai K., Kohama T., Kitahara S., Takishima K.,
RA Tanji M., Athauda S.B.P., Takahashi T., Akanuma H., Mamiya G., Yamasaki M.;
RT "The primary structure of Aspergillus niger acid proteinase A.";
RL J. Biol. Chem. 266:19480-19483(1991).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage in B chain of insulin: 3-Asn-|-Gln-4,
CC 13-Gly-|-Ala-14, and 26-Tyr-|-Thr-27.; EC=3.4.23.19;
CC -!- SUBUNIT: Heterodimer of two noncovalently bound light and heavy chains.
CC -!- SIMILARITY: Belongs to the peptidase G1 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; M68871; AAA32687.1; -; Genomic_DNA.
DR PIR; A41025; A41025.
DR PDB; 1Y43; X-ray; 1.40 A; A=60-98, B=110-282.
DR PDB; 3TRS; X-ray; 1.60 A; A/C=60-98, B/D=110-282.
DR PDBsum; 1Y43; -.
DR PDBsum; 3TRS; -.
DR AlphaFoldDB; P24665; -.
DR SMR; P24665; -.
DR STRING; 5061.CADANGAP00000047; -.
DR MEROPS; G01.002; -.
DR VEuPathDB; FungiDB:An01g00530; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1142023; -.
DR VEuPathDB; FungiDB:ATCC64974_23000; -.
DR VEuPathDB; FungiDB:M747DRAFT_296186; -.
DR eggNOG; ENOG502RJF6; Eukaryota.
DR EvolutionaryTrace; P24665; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.700; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000250; Peptidase_G1.
DR InterPro; IPR038656; Peptidase_G1_sf.
DR PANTHER; PTHR37536; PTHR37536; 1.
DR Pfam; PF01828; Peptidase_A4; 1.
DR PRINTS; PR00977; SCYTLDPTASE.
DR SUPFAM; SSF49899; SSF49899; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; Hydrolase; Protease;
KW Pyrrolidone carboxylic acid; Signal; Zymogen.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..59
FT /evidence="ECO:0000269|PubMed:1918059"
FT /id="PRO_0000028495"
FT CHAIN 60..98
FT /note="Aspergillopepsin-2 light chain"
FT /id="PRO_0000028496"
FT PROPEP 99..109
FT /evidence="ECO:0000269|PubMed:1918059"
FT /id="PRO_0000028497"
FT CHAIN 110..282
FT /note="Aspergillopepsin-2 heavy chain"
FT /id="PRO_0000028498"
FT REGION 27..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 110
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:1918059"
FT DISULFID 115..139
FT /evidence="ECO:0000269|PubMed:1918059"
FT DISULFID 127..210
FT /evidence="ECO:0000269|PubMed:1918059"
FT STRAND 61..72
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 76..84
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3TRS"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 144..154
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:1Y43"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 195..201
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 213..219
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 235..245
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1Y43"
FT HELIX 252..254
FT /evidence="ECO:0007829|PDB:3TRS"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 268..272
FT /evidence="ECO:0007829|PDB:1Y43"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:1Y43"
SQ SEQUENCE 282 AA; 29887 MW; 4EA727F9AE33F72A CRC64;
MKFSTILTGS LFATAALAAP LTEKRRARKE ARAAGKRHSN PPYIPGSDKE ILKLNGTTNE
EYSSNWAGAV LIGDGYTKVT GEFTVPSVSA GSSGSSGYGG GYGYWKNKRQ SEEYCASAWV
GIDGDTCETA ILQTGVDFCY EDGQTSYDAW YEWYPDYAYD FSDITISEGD SIKVTVEATS
KSSGSATVEN LTTGQSVTHT FSGNVEGDLC ETNAEWIVED FESGDSLVAF ADFGSVTFTN
AEATSGGSTV GPSDATVMDI EQDGSVLTET SVSGDSVTVT YV
