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Database: UniProt
Entry: F6HKK3_VITVI
LinkDB: F6HKK3_VITVI
Original site: F6HKK3_VITVI 
ID   F6HKK3_VITVI            Unreviewed;       203 AA.
AC   F6HKK3;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Germin-like protein {ECO:0000256|RuleBase:RU366015};
GN   OrderedLocusNames=VIT_08s0007g03430 {ECO:0000313|EMBL:CCB55425.1};
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:CCB55425.1, 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   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000256|ARBA:ARBA00004271, ECO:0000256|RuleBase:RU366015}.
CC   -!- SIMILARITY: Belongs to the germin family.
CC       {ECO:0000256|ARBA:ARBA00007456, ECO:0000256|RuleBase:RU366015}.
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DR   EMBL; FN595991; CCB55425.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6HKK3; -.
DR   PaxDb; 29760-VIT_08s0007g03430-t01; -.
DR   EnsemblPlants; Vitvi08g01471_t001; Vitvi08g01471_P001; Vitvi08g01471.
DR   Gramene; Vitvi08g01471_t001; Vitvi08g01471_P001; Vitvi08g01471.
DR   eggNOG; ENOG502RDTK; Eukaryota.
DR   HOGENOM; CLU_015790_0_3_1; -.
DR   InParanoid; F6HKK3; -.
DR   Proteomes; UP000009183; Chromosome 8.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd02241; cupin_OxOx; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR001929; Germin.
DR   InterPro; IPR019780; Germin_Mn-BS.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR31238:SF8; GERMIN-LIKE PROTEIN SUBFAMILY 3 MEMBER 2; 1.
DR   PANTHER; PTHR31238; GERMIN-LIKE PROTEIN SUBFAMILY 3 MEMBER 3; 1.
DR   Pfam; PF00190; Cupin_1; 1.
DR   PRINTS; PR00325; GERMIN.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; RmlC-like cupins; 1.
DR   PROSITE; PS00725; GERMIN; 1.
PE   3: Inferred from homology;
KW   Apoplast {ECO:0000256|ARBA:ARBA00022523, ECO:0000256|RuleBase:RU366015};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601929-3};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|PIRSR:PIRSR601929-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601929-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009183};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525, ECO:0000256|RuleBase:RU366015}.
FT   DOMAIN          47..193
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   BINDING         92
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         95
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         97
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         97
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         102
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         102
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         141
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   DISULFID        14..33
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-3"
SQ   SEQUENCE   203 AA;  22189 MW;  8C28347E5AF236BD CRC64;
     MAMASDPDPL QDFCIPNTKW GYGRAARLDT VPCKNSSEAT TDDFVFSGLK KPAEEFSNMG
     IAAVSVTPQM FPGLNTLGMS FVRADIQVGG INAPHFHPRA TEITYVLQGK VYSGFVDSTN
     RVFATVLEQG EVMVFPRGLV HFQMNVGESP ATVFGCFNSQ NPGVQKIPSA LFGSEIKDEL
     LEKAFGMTPK QIDKMRRKFV PKG
//
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