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
//