ID   GL114_ARATH             Reviewed;         222 AA.
AC   Q9FID0;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 130.
DE   RecName: Full=Germin-like protein subfamily 1 member 14;
DE   Flags: Precursor;
GN   OrderedLocusNames=At5g39110; ORFNames=MXF12.14, MXF12_120;
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=10048488; DOI=10.1093/dnares/5.6.379;
RA   Asamizu E., Sato S., Kaneko T., Nakamura Y., Kotani H., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VIII. Sequence
RT   features of the regions of 1,081,958 bp covered by seventeen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:379-391(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; AB016892; BAB10832.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED94395.1; -; Genomic_DNA.
DR   RefSeq; NP_198727.1; NM_123273.2.
DR   AlphaFoldDB; Q9FID0; -.
DR   SMR; Q9FID0; -.
DR   STRING; 3702.AT5G39110.1; -.
DR   PaxDb; Q9FID0; -.
DR   PRIDE; Q9FID0; -.
DR   ProteomicsDB; 230456; -.
DR   EnsemblPlants; AT5G39110.1; AT5G39110.1; AT5G39110.
DR   GeneID; 833904; -.
DR   Gramene; AT5G39110.1; AT5G39110.1; AT5G39110.
DR   KEGG; ath:AT5G39110; -.
DR   Araport; AT5G39110; -.
DR   TAIR; locus:2177147; AT5G39110.
DR   eggNOG; ENOG502QQ4A; Eukaryota.
DR   HOGENOM; CLU_015790_0_0_1; -.
DR   InParanoid; Q9FID0; -.
DR   OMA; IHFTVIA; -.
DR   OrthoDB; 1164277at2759; -.
DR   PhylomeDB; Q9FID0; -.
DR   PRO; PR:Q9FID0; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FID0; baseline and differential.
DR   Genevisible; Q9FID0; 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..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..222
FT                   /note="Germin-like protein subfamily 1 member 14"
FT                   /id="PRO_0000010814"
FT   DOMAIN          63..214
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         111
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         113
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         160
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        78
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..49
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   222 AA;  23913 MW;  C5DC6322D9F9762A CRC64;
     MRFSKSLILI TLSALVISFA EANDPSPLQD FCVAIGDLKN GVFVNGKFCK DPKQAKAEDF
     FYSGLNQAGT TNNKVKSNVT TVNVDQIPGL NTLGISLVRI DYAPYGQNPP HTHPRATEIL
     VLVEGTLYVG FVSSNQDNNR LFAKVLNPGD VFVFPIGMIH FQVNIGKTPA VAFAGLSSQN
     AGVITIADTV FGSTPPINPD ILAQAFQLDV NVVKDLEAKF KN