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Database: UniProt
Entry: F6H7H1_VITVI
LinkDB: F6H7H1_VITVI
Original site: F6H7H1_VITVI 
ID   F6H7H1_VITVI            Unreviewed;       530 AA.
AC   F6H7H1;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=Aspartic proteinase A1 {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=VIT_10s0116g01210 {ECO:0000313|EMBL:CCB48187.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB48187.1, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   EMBL; FN595248; CCB48187.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6H7H1; -.
DR   STRING; 29760.F6H7H1; -.
DR   MEROPS; A01.020; -.
DR   PaxDb; 29760-VIT_10s0116g01210-t01; -.
DR   EnsemblPlants; Vitvi10g00064_t001; Vitvi10g00064_P001; Vitvi10g00064.
DR   Gramene; Vitvi10g00064_t001; Vitvi10g00064_P001; Vitvi10g00064.
DR   eggNOG; KOG1339; Eukaryota.
DR   HOGENOM; CLU_013253_3_1_1; -.
DR   InParanoid; F6H7H1; -.
DR   Proteomes; UP000009183; Chromosome 10.
DR   ExpressionAtlas; F6H7H1; baseline and differential.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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:SF54; ASPARTIC PROTEINASE A1-LIKE; 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   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:UP000009183};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          106..527
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   DOMAIN          336..376
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   DOMAIN          400..441
FT                   /note="Saposin B-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50015"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        311
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        137..143
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   530 AA;  57636 MW;  2989640188A3F16F CRC64;
     MKTKRENRQS VDRMVNMEAK LKAVLVSLFL SSLLFSLVSS ATTDGLFRIG LKKMKLDQND
     QLAARLESKE GESLRASIRK YFRHGNLGDS QDTDIVGLKN YMDAQYFGEI GIGTPPQTFT
     VIFDTGSSNL WVPSSKCYFS VPCYFHSKYK SSQSSTYRKN GKSADIHYGT GAISGFFSED
     NVKVGDLVVK NQEFIEATRE PSVTFLVAKF DGILGLGFQE ISVGNAVPVW YNMVKQGLVK
     EPVFSFWLNR KTDDDEGGEL VFGGVDPDHF KGEHTYVPVT QKGYWQFDMG EVLIDGETTG
     YCAGGCAAIA DSGTSLLAGP TAVVAMINHA IGATGVVSQE CKTVVAQYGE TIMDLLLSEA
     SPQKICSQIG LCTFDGTRGV GMGIESVVDE KNGDKSSGVH DAGCSACEMA VVWMQSQLRQ
     NQTKERILEY VNELCDRLPS PMGESAVDCL QLSSMPNVSL TIGGKVFDLS ANEYVLKVGE
     GAAAQCISGF IAMDVPPPRG PLWILGDVFM GRYHTVFDYG NMRVGFAEAA
//
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