ID Q9FRW8_NEPAL Unreviewed; 514 AA.
AC Q9FRW8;
DT 01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2001, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE SubName: Full=Aspartic proteinase 2 {ECO:0000313|EMBL:BAB20970.1};
GN Name=NaAP2 {ECO:0000313|EMBL:BAB20970.1};
OS Nepenthes alata (Winged pitcher plant) (Nepenthes copelandii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Nepenthaceae; Nepenthes.
OX NCBI_TaxID=4376 {ECO:0000313|EMBL:BAB20970.1};
RN [1] {ECO:0000313|EMBL:BAB20970.1}
RP NUCLEOTIDE SEQUENCE.
RA An C., Fukusaki E., Kobayashi A.;
RT "Aspartic proteinases of carnivorous plant Nepenthes alata.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR EMBL; AB045892; BAB20970.1; -; mRNA.
DR AlphaFoldDB; Q9FRW8; -.
DR MEROPS; A01.A02; -.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06098; phytepsin; 1.
DR Gene3D; 2.40.70.10; Acid Proteases; 2.
DR Gene3D; 1.10.225.10; Saposin-like; 1.
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; IPR033869; Phytepsin.
DR InterPro; IPR007856; SapB_1.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF93; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 1.
DR Pfam; PF05184; SapB_1; 1.
DR Pfam; PF03489; SapB_2; 1.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF47862; Saposin; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 2.
DR PROSITE; PS51767; PEPTIDASE_A1; 1.
DR PROSITE; PS50015; SAP_B; 2.
PE 2: Evidence at transcript level;
KW Aspartyl protease {ECO:0000256|ARBA:ARBA00022750,
KW ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR601461-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..514
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004326113"
FT DOMAIN 90..511
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 320..360
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DOMAIN 384..425
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DISULFID 121..127
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 514 AA; 55390 MW; F46C39A8090B5F55 CRC64;
MGRTFETALT TLFLLLLLSP LVTSLSSDRL LRVGLKKRKL DQINRLSSHY GCKGKGSTSP
SIWKHGLGNG LGNSDDADII SLKNYMDAQY FGEIGIGSPP QKFTVIFDTG SSNLWVPSAK
CYFSIACYLH PKYKSFKSST YAKNGKSAAI HYGTGAISGF FSQDHVKMGD LVVENQDFIE
ATKEPSITFV AAKFDGILGL GFQEISVGDA VPAWYNMIDQ GLVNEPVFSF WLNRKSEEEE
GGEIVFGGVD PNHYKGEHTY VPVTRKGYWQ FDMDDVLVGG ETTGYCSGGC SAIADSGTSL
LAGPTTIIVQ INHAIGASGL VSQECKAVVS QYGKAILDAL VAEAQPQKIC SQIGLCTFDG
KRGVSMGIES VVEKNPGNSS DGLQDAMCTA CEMAVVWMQN QLRQNRTEEQ ILNYVNELCN
RLPSPMGESS VDCGSLSSMP NVSLTIGGKV FDLSPEKYVL KVGEGVAAQC ISGFIALDIA
PPRGPLWILG DIFMGQYHTV FDYGNLSVGF AEAA
//
