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Database: UniProt
Entry: F6HZ02_VITVI
LinkDB: F6HZ02_VITVI
Original site: F6HZ02_VITVI 
ID   F6HZ02_VITVI            Unreviewed;       206 AA.
AC   F6HZ02;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=Germin-like protein {ECO:0000256|RuleBase:RU366015};
GN   OrderedLocusNames=VIT_14s0128g00640 {ECO:0000313|EMBL:CCB59916.1};
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:CCB59916.1, 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   -!- SUBUNIT: Oligomer (believed to be a pentamer but probably hexamer).
CC       {ECO:0000256|ARBA:ARBA00011268}.
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; FN596501; CCB59916.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6HZ02; -.
DR   PaxDb; 29760-VIT_14s0128g00640-t01; -.
DR   HOGENOM; CLU_015790_0_0_1; -.
DR   InParanoid; F6HZ02; -.
DR   Proteomes; UP000009183; Chromosome 14.
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:SF300; GERMIN-LIKE PROTEIN SUBFAMILY 1 MEMBER 13-RELATED; 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};
KW   Signal {ECO:0000256|RuleBase:RU366015}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|RuleBase:RU366015"
FT   CHAIN           24..206
FT                   /note="Germin-like protein"
FT                   /evidence="ECO:0000256|RuleBase:RU366015"
FT                   /id="PRO_5019620385"
FT   DOMAIN          64..199
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000259|SMART:SM00835"
FT   BINDING         109
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         112
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         114
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         114
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         119
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   BINDING         119
FT                   /ligand="oxalate"
FT                   /ligand_id="ChEBI:CHEBI:30623"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-1"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-2"
FT   DISULFID        33..50
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601929-3"
SQ   SEQUENCE   206 AA;  21912 MW;  275CBC6D838F10B3 CRC64;
     MKKGVSSLVT VALMALASSL ASAFDPRPLQ DTCVAIDEPE NAVFVNGKFC KNPNLTVADD
     FLYQGLNIPG NTTNLVGSNV TIINVDVLPG QNTLGISLVR IDYAPYGQNP SHIHPRASEI
     LTVLEGTLLV GFVTSNPQNR FISKVLNKGD VFVFPIGLIH FQFNIGHTNA VAIAGLNSQN
     PGVITIANAV FGSNPPINPD FLARAF
//
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