CARP_NEUCR
ID CARP_NEUCR Reviewed; 396 AA.
AC Q01294; Q7RVB0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Vacuolar protease A;
DE EC=3.4.23.-;
DE Flags: Precursor;
GN Name=pep-4; ORFNames=B13D24.090, NCU02273;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8702999; DOI=10.1074/jbc.271.36.21944;
RA Vazquez-Laslop N., Tenney K., Bowman B.J.;
RT "Characterization of a vacuolar protease in Neurospora crassa and the use
RT of gene RIPing to generate protease-deficient strains.";
RL J. Biol. Chem. 271:21944-21949(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase A1 family. {ECO:0000305}.
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DR EMBL; U36471; AAA79878.1; -; Genomic_DNA.
DR EMBL; BX908789; CAF05874.1; -; Genomic_DNA.
DR EMBL; CM002242; EAA30681.1; -; Genomic_DNA.
DR PIR; T47207; T47207.
DR RefSeq; XP_959917.1; XM_954824.3.
DR AlphaFoldDB; Q01294; -.
DR SMR; Q01294; -.
DR STRING; 5141.EFNCRP00000003251; -.
DR MEROPS; A01.018; -.
DR PRIDE; Q01294; -.
DR EnsemblFungi; EAA30681; EAA30681; NCU02273.
DR GeneID; 3876039; -.
DR KEGG; ncr:NCU02273; -.
DR VEuPathDB; FungiDB:NCU02273; -.
DR HOGENOM; CLU_013253_3_4_1; -.
DR InParanoid; Q01294; -.
DR OMA; DKSHYTG; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
DR GO; GO:0000324; C:fungal-type vacuole; IBA:GO_Central.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd05488; Proteinase_A_fungi; 1.
DR Gene3D; 2.40.70.10; -; 2.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR033819; Saccharopepsin.
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 3: Inferred from homology;
KW Aspartyl protease; Disulfide bond; Glycoprotein; Hydrolase; Protease;
KW Reference proteome; Signal; Vacuole; Zymogen.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT PROPEP 18..70
FT /note="Activation peptide"
FT /id="PRO_0000025875"
FT CHAIN 71..396
FT /note="Vacuolar protease A"
FT /id="PRO_0000025876"
FT DOMAIN 85..392
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 284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..121
FT /evidence="ECO:0000250"
FT DISULFID 318..351
FT /evidence="ECO:0000250"
FT CONFLICT 31..32
FT /note="EQ -> DE (in Ref. 1; AAA79878)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="I -> L (in Ref. 1; AAA79878)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="N -> P (in Ref. 1; AAA79878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 396 AA; 42933 MW; 3498032A1E703195 CRC64;
MKGALLTAAM LLGSAQAGVH TMKLKKVPLA EQLESVPIDV QVQHLGQKYT GLRTESHTQA
MFKATDAQVS GNHPVPITNF MNAQYFSEIT IGTPPQTFKV VLDTGSSNLW VPSSQCGSIA
CYLHNKYESS ESSTYKKNGT SFKIEYGSGS LSGFVSQDRM TIGDITINDQ LFAEATSEPG
LAFAFGRFDG ILGLGYDRIA VNGITPPFYK MVEQKLVDEP VFSFYLADQD GESEVVFGGV
NKDRYTGKIT TIPLRRKAYW EVDFDAIGYG KDFAELEGHG VILDTGTSLI ALPSQLAEML
NAQIGAKKSW NGQFTIDCGK KSSLEDVTFT LAGYNFTLGP EDYILEASGS CLSTFMGMDM
PAPVGPLAIL GDAFLRKYYS IYDLGADTVG IATAKR
