ID   GL21_ORYSJ              Reviewed;         216 AA.
AC   Q6K5Q0; A0A0P0VJ67;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Putative germin-like protein 2-1;
DE   Flags: Precursor;
GN   OrderedLocusNames=Os02g0491600, LOC_Os02g29000;
GN   ORFNames=OSJNBa0048K16.34, P0579G08.10;
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).
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; AP004864; BAD21898.1; -; Genomic_DNA.
DR   EMBL; AP005317; BAD22075.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF08788.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS78742.1; -; Genomic_DNA.
DR   RefSeq; XP_015624078.1; XM_015768592.1.
DR   AlphaFoldDB; Q6K5Q0; -.
DR   SMR; Q6K5Q0; -.
DR   STRING; 4530.OS02T0491600-00; -.
DR   PaxDb; Q6K5Q0; -.
DR   PRIDE; Q6K5Q0; -.
DR   EnsemblPlants; Os02t0491600-00; Os02t0491600-00; Os02g0491600.
DR   GeneID; 4329389; -.
DR   Gramene; Os02t0491600-00; Os02t0491600-00; Os02g0491600.
DR   KEGG; osa:4329389; -.
DR   eggNOG; ENOG502QQ4A; Eukaryota.
DR   HOGENOM; CLU_015790_0_0_1; -.
DR   InParanoid; Q6K5Q0; -.
DR   OMA; INGFACK; -.
DR   OrthoDB; 1164277at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6K5Q0; 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; IPR019780; Germin_Mn-BS.
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.
DR   PROSITE; PS00725; GERMIN; 1.
PE   3: Inferred from homology;
KW   Apoplast; Disulfide bond; Glycoprotein; Manganese; Metal-binding;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..216
FT                   /note="Putative germin-like protein 2-1"
FT                   /id="PRO_0000365498"
FT   DOMAIN          60..210
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         108
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         156
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..46
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   216 AA;  23264 MW;  5B3D5B54CE985091 CRC64;
     MASTWFFLLA LLAVSISNAF ASDPSQLQDF CVADKMSQVL VNGFACKDPA AITVEDFFFS
     GLHMAGNTSN RQGSAVTGVN VAQISGLNTL GISLARVDYA PYGLNPPHIH PRATEILTIL
     EGSLYVGFVT SNPENKLFTK VLNKGDVFVF PQGLIHFQFN YGTKDVIALA ALSSQNPGVI
     TIANAVFGSK PFISDDILAK AFQVEKKIVD RIQAQF