ID A0A0L9UN75_PHAAN Unreviewed; 499 AA.
AC A0A0L9UN75;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Aspartic proteinase {ECO:0000313|EMBL:KAG2371593.1};
GN ORFNames=HKW66_Vig0217670 {ECO:0000313|EMBL:KAG2371593.1},
GN LR48_Vigan05g161700 {ECO:0000313|EMBL:KOM44012.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM44012.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
RN [2] {ECO:0000313|EMBL:KOM44012.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Seedling {ECO:0000313|EMBL:KOM44012.1};
RA Chooi Y.-H.;
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KAG2371593.1, ECO:0000313|Proteomes:UP000743370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Leaf {ECO:0000313|EMBL:KAG2371593.1};
RA Xiang H.;
RT "Vigna angularis (adzuki bean) Var. LongXiaoDou No. 4 denovo assembly.";
RL Submitted (MAY-2020) 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; JABFOF010000011; KAG2371593.1; -; Genomic_DNA.
DR EMBL; CM003375; KOM44012.1; -; Genomic_DNA.
DR RefSeq; XP_017423838.1; XM_017568349.1.
DR RefSeq; XP_017423839.1; XM_017568350.1.
DR AlphaFoldDB; A0A0L9UN75; -.
DR STRING; 3914.A0A0L9UN75; -.
DR EnsemblPlants; KOM44012; KOM44012; LR48_Vigan05g161700.
DR GeneID; 108333032; -.
DR Gramene; KOM44012; KOM44012; LR48_Vigan05g161700.
DR KEGG; var:108333032; -.
DR OMA; KMPSIRD; -.
DR OrthoDB; 1120702at2759; -.
DR Proteomes; UP000053144; Chromosome 5.
DR Proteomes; UP000743370; Unassembled WGS sequence.
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:SF39; EUKARYOTIC ASPARTYL PROTEASE FAMILY 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 3: Inferred from homology;
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000454};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..499
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5036294347"
FT DOMAIN 75..496
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 305..345
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT DOMAIN 369..410
FT /note="Saposin B-type"
FT /evidence="ECO:0000259|PROSITE:PS50015"
FT ACT_SITE 93
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 280
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 106..112
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 271..275
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 499 AA; 54423 MW; 2026731EA1FA99AD CRC64;
MRSKYSLVAL FLLLLHPVVL SGPTNGIIRF GLKKNKFDES KILKGHIGEE GTTLRDENSD
DISNIRLKNY MNAQYFGQIG IGTPPQKFTV IFDTGSSNLW VPSSKCYFSV ACYLHSRYKS
SQSGTYKRNG SSAEIHYGTG QISGFFSQDH VKIGDLNVYG QDFIEATREP SLTFLAAKFD
GILGLGFQEI SVGNAAPIWY NMVHQKLVAE PVFSFWLNRN TDEEQGGEIV FGGVDSDHYK
GEHTYVPVTH KGYWQIQIED VLIDNLTTGF CSAKCSAIVD SGTSLLAGPT GVIAQINHAI
GAVGLVNQDC KAVVAQYGKT ILDKLINKAL SQQICSQIGL CAFDGTQGVS KGIQSVVDKN
IGKTSYSLND AGCTACEMTV VWMKNRLRLN ETEDQILAYA NSLCDMLPSP NGESTVECST
LSKMPNVSFT IGGKVFELSP EQYILKVGKG ATAQCISGFI ALDIAPPRGP LWILGDIFMG
RYHTVFDYGN MKVGFAESA
//