ID   GL24_ORYSJ              Reviewed;         229 AA.
AC   Q6ESF0; A0A0P0VK03;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Germin-like protein 2-4;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os02g0532500, LOC_Os02g32980; ORFNames=P0605D08.24;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: May play a role in plant defense. Probably has no oxalate
CC       oxidase activity even if the active site is conserved.
CC   -!- SUBUNIT: Oligomer (believed to be a pentamer but probably hexamer).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; AP005110; BAD28420.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08939.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79042.1; -; Genomic_DNA.
DR   EMBL; AK059817; BAG87146.1; -; mRNA.
DR   RefSeq; XP_015622959.1; XM_015767473.1.
DR   AlphaFoldDB; Q6ESF0; -.
DR   SMR; Q6ESF0; -.
DR   STRING; 4530.OS02T0532500-01; -.
DR   PaxDb; Q6ESF0; -.
DR   PRIDE; Q6ESF0; -.
DR   EnsemblPlants; Os02t0532500-01; Os02t0532500-01; Os02g0532500.
DR   GeneID; 4329551; -.
DR   Gramene; Os02t0532500-01; Os02t0532500-01; Os02g0532500.
DR   KEGG; osa:4329551; -.
DR   eggNOG; ENOG502RDTK; Eukaryota.
DR   HOGENOM; CLU_015790_0_3_1; -.
DR   InParanoid; Q6ESF0; -.
DR   OMA; AINPPHF; -.
DR   OrthoDB; 1164277at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6ESF0; OS.
DR   GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0030145; F:manganese ion binding; IEA:InterPro.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR001929; Germin.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 1.
DR   PRINTS; PR00325; GERMIN.
DR   SMART; SM00835; Cupin_1; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   2: Evidence at transcript level;
KW   Apoplast; Disulfide bond; Glycoprotein; Manganese; Metal-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..229
FT                   /note="Germin-like protein 2-4"
FT                   /id="PRO_0000365501"
FT   DOMAIN          66..213
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         115
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         117
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        57
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..52
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   229 AA;  24318 MW;  0FB9F1546EE3F6C0 CRC64;
     MAHRRRCLLL LLAVLLPAMA ARGDPDAVQD FCVPDAGRGR PVELAMLPAY PCRSPANLTA
     GDFAFSGVRA AGNFSPETGF AGVSVTPAQF PGLHTLGMSF ARADLSAAGG VNPPHYHPRA
     TETALVLAGR VYAGFVDSGG RLFAKVLEQG EVMVFPRAMV HFQLNVGDTP ATVYGAFNSE
     NPGIVRIPAT VFGSGIREAV LERAFGLTPA ELRRLEKRFG PPKKAEMED