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GL113_ARATH
ID   GL113_ARATH             Reviewed;         222 AA.
AC   P92997; F4KD10;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Germin-like protein subfamily 1 member 13;
DE   Flags: Precursor;
GN   Name=GLP6; OrderedLocusNames=At5g39100; ORFNames=MXF12.13;
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 [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9869400; DOI=10.1023/a:1006038117130;
RA   Carter C., Graham R.A., Thornburg R.W.;
RT   "Arabidopsis thaliana contains a large family of germin-like proteins:
RT   characterization of cDNA and genomic sequences encoding 12 unique family
RT   members.";
RL   Plant Mol. Biol. 38:929-943(1998).
RN   [2]
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   [3]
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; U75194; AAB51572.1; -; mRNA.
DR   EMBL; AB016892; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED94394.2; -; Genomic_DNA.
DR   RefSeq; NP_001318702.1; NM_001344284.1.
DR   AlphaFoldDB; P92997; -.
DR   SMR; P92997; -.
DR   PRIDE; P92997; -.
DR   GeneID; 833903; -.
DR   KEGG; ath:AT5G39100; -.
DR   Araport; AT5G39100; -.
DR   InParanoid; P92997; -.
DR   OrthoDB; 1164277at2759; -.
DR   PRO; PR:P92997; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P92997; baseline and differential.
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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..222
FT                   /note="Germin-like protein subfamily 1 member 13"
FT                   /id="PRO_0000010813"
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"
FT   CONFLICT        214
FT                   /note="E -> K (in Ref. 1; AAB51572)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   222 AA;  24095 MW;  967705F8096E4115 CRC64;
     MRVSKSLILI TLSALVISFA EAYDPSPLQD FCVAIDDLKN GVFVNGKFCK DPKQAKAEDF
     FFSGLNQAGS TNNKVRSNVT TVNVDQIPGL NTMGISLVRI DYAPYGQNPP HTHPRATEIL
     VLIEGTLYVG FVSSNQDNNR LFAKVLYPGD VFVFPIGMIH FQVNIGKTPA VAFAGLSSQN
     AGVITIADTV FGSTPPINPD ILAQAFQLDV NIVEDLEAKF RN
 
 
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