ID K8YUV3_NANGC Unreviewed; 427 AA.
AC K8YUV3;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 03-MAY-2023, entry version 48.
DE SubName: Full=Cathepsin D {ECO:0000313|EMBL:EKU22454.1};
DE EC=3.4.23.5 {ECO:0000313|EMBL:EKU22454.1};
GN Name=CTSD {ECO:0000313|EMBL:EKU22454.1};
GN ORFNames=NGA_0463300 {ECO:0000313|EMBL:EKU22454.1};
OS Nannochloropsis gaditana (strain CCMP526) (Green microalga)
OS (Microchloropsis gaditana).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX NCBI_TaxID=1093141 {ECO:0000313|EMBL:EKU22454.1, ECO:0000313|Proteomes:UP000009377};
RN [1] {ECO:0000313|Proteomes:UP000009377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP526 {ECO:0000313|Proteomes:UP000009377};
RX PubMed=22353717;
RA Radakovits R., Jinkerson R.E., Fuerstenberg S.I., Tae H., Settlage R.E.,
RA Boore J.L., Posewitz M.C.;
RT "Draft genome sequence and genetic transformation of the oleaginous alga
RT Nannochloropis gaditana.";
RL Nat. Commun. 3:686-686(2012).
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; JH471271; EKU22454.1; -; Genomic_DNA.
DR RefSeq; XP_005853900.1; XM_005853838.1.
DR AlphaFoldDB; K8YUV3; -.
DR MEROPS; A01.018; -.
DR EnsemblProtists; EKU22454; EKU22454; NGA_0463300.
DR GeneID; 17360676; -.
DR KEGG; ngd:NGA_0463300; -.
DR OMA; KYDHDAS; -.
DR OrthoDB; 615305at2759; -.
DR Proteomes; UP000009377; Unassembled WGS sequence.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; Acid Proteases; 3.
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 PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF51; NAPSIN-A; 1.
DR Pfam; PF00026; Asp; 2.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Hydrolase {ECO:0000256|RuleBase:RU000454, ECO:0000313|EMBL:EKU22454.1};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000009377};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..427
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003922856"
FT DOMAIN 66..424
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 84
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 318
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
SQ SEQUENCE 427 AA; 46076 MW; D213BA951CA75793 CRC64;
MRLSLCLLSL AVLESIKGQT LRIPLKRRPA AQVIDSILAH PQRPLQGTDE PGEGDIIISD
VSNAQYFGEI SVGSDRQAFQ VIFDTGSSNL WIPSEDCLAS CASKAKYDHD ASDTYVENGA
IFKIMYGSGP VQVESPTSLP PLPAFFGLPH ASFLSPPFTT FVIIAYFEAT VLNWCCPLLS
MFSFWQGYFS EDDVELGGLT ISQQAFAEVT DASGLGAAFA AGSFDGILGL GFDSISVGKV
TTPFHNLIKQ GLVAEPVFSF YLGDNAPGEL TLGGTDPAHY KGDIHYVPLK SATYWEVALE
DVQVQGLSLT NVDSAIIDSG TSLITGPKKE VAKLAKLVGA TRFILGEYLI DCNAQGPDID
FVIDGRTYSL SADDYKIRDG GLCLFAFMGL DIPRPSGPLW ILGDSFMRRY YTTFNYEKQS
VGLALAA
//