GL111_ARATH
ID GL111_ARATH Reviewed; 223 AA.
AC Q9FMA8; Q52K86;
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 11;
DE Flags: Precursor;
GN OrderedLocusNames=At5g38940; ORFNames=K15E6.18, K15E6_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=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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Kim C.J., Chen H., Cheuk R.F., Shinn P., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB009048; BAB08650.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94377.1; -; Genomic_DNA.
DR EMBL; BT021982; AAY17419.1; -; mRNA.
DR EMBL; BT023474; AAY57313.1; -; mRNA.
DR RefSeq; NP_198710.2; NM_123256.4.
DR AlphaFoldDB; Q9FMA8; -.
DR SMR; Q9FMA8; -.
DR STRING; 3702.AT5G38940.1; -.
DR PaxDb; Q9FMA8; -.
DR ProteomicsDB; 228795; -.
DR EnsemblPlants; AT5G38940.1; AT5G38940.1; AT5G38940.
DR GeneID; 833886; -.
DR Gramene; AT5G38940.1; AT5G38940.1; AT5G38940.
DR KEGG; ath:AT5G38940; -.
DR Araport; AT5G38940; -.
DR TAIR; locus:2152267; AT5G38940.
DR eggNOG; ENOG502QQ4A; Eukaryota.
DR HOGENOM; CLU_015790_0_0_1; -.
DR InParanoid; Q9FMA8; -.
DR PhylomeDB; Q9FMA8; -.
DR PRO; PR:Q9FMA8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FMA8; baseline and differential.
DR Genevisible; Q9FMA8; 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 2: Evidence at transcript level;
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 11"
FT /id="PRO_0000010811"
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; 23650 MW; 9F78B07DB89923AB CRC64;
MAMKSLSFLA VLSLLALTLP LAIASDPSQL QDFCVSANTS ANGVFVNGKF CKDPKLVTAD
DFFFSGLQTA RPITSPVGST VTAVNVNNLL GLNTLGISLV RIDYAVNGQN PPHTHPRATE
ILVVEQGTLL VGFVTSNPDN RLFSKVLNEG DVFVFPEGLI HFQANIGKAP AVAFAALSSQ
NPGVITIANT VFGANPAINP TILAKAFQLN PRVVMDLQTK FKK
