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Database: UniProt
Entry: A0A0L9UN75_PHAAN
LinkDB: A0A0L9UN75_PHAAN
Original site: A0A0L9UN75_PHAAN 
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
//
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