ID   GL110_ARATH             Reviewed;         223 AA.
AC   Q9FMA9;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Germin-like protein subfamily 1 member 10;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g38930; ORFNames=K15E6.16, K15E6_110;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
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; AB009048; BAB08649.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94376.1; -; Genomic_DNA.
DR   RefSeq; NP_198709.1; NM_123255.2.
DR   AlphaFoldDB; Q9FMA9; -.
DR   SMR; Q9FMA9; -.
DR   STRING; 3702.AT5G38930.1; -.
DR   PaxDb; Q9FMA9; -.
DR   ProteomicsDB; 228794; -.
DR   EnsemblPlants; AT5G38930.1; AT5G38930.1; AT5G38930.
DR   GeneID; 833885; -.
DR   Gramene; AT5G38930.1; AT5G38930.1; AT5G38930.
DR   KEGG; ath:AT5G38930; -.
DR   Araport; AT5G38930; -.
DR   TAIR; locus:2152257; AT5G38930.
DR   eggNOG; ENOG502QQ4A; Eukaryota.
DR   HOGENOM; CLU_015790_0_0_1; -.
DR   InParanoid; Q9FMA9; -.
DR   OMA; FAGLHNA; -.
DR   OrthoDB; 1164277at2759; -.
DR   PhylomeDB; Q9FMA9; -.
DR   PRO; PR:Q9FMA9; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FMA9; baseline and differential.
DR   Genevisible; Q9FMA9; AT.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..223
FT                   /note="Germin-like protein subfamily 1 member 10"
FT                   /id="PRO_0000010810"
FT   DOMAIN          65..215
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         113
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         120
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        38
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        34..51
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   223 AA;  23631 MW;  C24E679455B0BB8B CRC64;
     MAMKSLSFLA ALSLLALTLP LTIASDPSQL QDFCVSANSS ANGVFVNGKF CKDPKLVTAD
     DFFFPGLQTA RPITSPVGST VTAVNVNNLL GLNTLGISLV RIDYAVDGQN PPHTHPRATE
     ILVVELGTLL VGFVTSNPDN RLFTKVLNEG DVFVFPEGLI HFQANIGKAP AVAFAALSSQ
     NPGVITIAPT VFGANPAINP NILAKAFQVD PRVVMDLQTK FKK