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Database: UniProt
Entry: A0A0D3BVN1_BRAOL
LinkDB: A0A0D3BVN1_BRAOL
Original site: A0A0D3BVN1_BRAOL 
ID   A0A0D3BVN1_BRAOL        Unreviewed;       509 AA.
AC   A0A0D3BVN1;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   Name=106337618 {ECO:0000313|EnsemblPlants:Bo4g092600.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo4g092600.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo4g092600.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo4g092600.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   RefSeq; XP_013632177.1; XM_013776723.1.
DR   RefSeq; XP_013632178.1; XM_013776724.1.
DR   RefSeq; XP_013632180.1; XM_013776726.1.
DR   AlphaFoldDB; A0A0D3BVN1; -.
DR   STRING; 109376.A0A0D3BVN1; -.
DR   MEROPS; A01.A02; -.
DR   EnsemblPlants; Bo4g092600.1; Bo4g092600.1; Bo4g092600.
DR   GeneID; 106337618; -.
DR   Gramene; Bo4g092600.1; Bo4g092600.1; Bo4g092600.
DR   KEGG; boe:106337618; -.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_1_1; -.
DR   OMA; CRVHQKF; -.
DR   OrthoDB; 1120702at2759; -.
DR   Proteomes; UP000032141; Chromosome C4.
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:SF35; ASPARTIC PROTEINASE A2; 1.
DR   PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR   Pfam; PF00026; Asp; 1.
DR   Pfam; PF05184; SapB_1; 1.
DR   Pfam; PF03489; SapB_2; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SMART; SM00741; SapB; 1.
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:UP000032141};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..509
FT                   /note="Peptidase A1 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002258193"
FT   DOMAIN          85..506
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          315..355
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   DOMAIN          379..420
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   DISULFID        116..122
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   509 AA;  55169 MW;  28DF0FFD9C276F33 CRC64;
     MGVHSVTSLV VSFLLFFSAS SESNDGTLRV GLKKLKLDPN NRLATRFGSK QEKAFRSSLK
     EFRSNDKNAG DADIVALKNY LDAQYYGEIA IGTPPQKFTV IFDTGSSNLW VPSGKCYFSL
     SCFFHSKYKS SRSSTYKESG KRAAIHYGSG SIAGFFSYDA VTVGDLVVKT QEFIEATSEP
     GLTFLVAKFD GLLGLGFQEI SVGNATPVWY NMLKQGLIKK PVFSFWLNRD TKSEEGGELV
     FGGVDPKHFK GEHTYVPVTR RGYWQFDMGE VLIAGKSTGY CENGCSAIAD SGTSLLAGPT
     AVIAMINKAI GASGVVSQQC KTVVDQYGQS ILDLLLAKAQ PKHICSQIGL CTFDGTHGVS
     MGIESVVDKE STKSSSGLRD AGCAPCEMAV VWIQSQLMQN MTQKRIVNYI NDICERMPSP
     NGESAVDCSQ LCKMPTVSFT IGGKVFDLAP EEYVLKIGEG PVAQCISGFT ALDLPPPRGP
     LWILGDVFMG RYHTVFHFGN EQVGFAEAA
//
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