GL31_ARATH
ID GL31_ARATH Reviewed; 208 AA.
AC P94040; O04751; Q96265;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Germin-like protein subfamily 3 member 1;
DE Short=At-GERM1;
DE Short=AtGER1;
DE Short=AtGLP1;
DE Flags: Precursor;
GN Name=GLP1; Synonyms=GER1, GLP3; OrderedLocusNames=At1g72610;
GN ORFNames=F28P22.20;
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; TISSUE=Seedling;
RX PubMed=9349269; DOI=10.1023/a:1005833028582;
RA Membre N., Berna A., Neutelings G., David A., David H., Staiger D.,
RA Saez Vasquez J., Raynal M., Delseny M., Bernier F.;
RT "cDNA sequence, genomic organization and differential expression of three
RT Arabidopsis genes for germin/oxalate oxidase-like proteins.";
RL Plant Mol. Biol. 35:459-469(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Sage-Ono K., Ono M., Oguchi T., Hasebe M., Xu Z.-J., Ueda K., Inoue M.,
RA Kamada H.;
RT "Molecular identification of two genes of germin-like protein in
RT Arabidopsis.";
RL Plant Biotechnol. 15:103-108(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Landsberg erecta;
RA Carter C., Thornburg R.W.;
RT "Cloning and characterization of the Arabidopsis thaliana germin-like
RT protein (GLP1) gene.";
RL (er) Plant Gene Register PGR98-183(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP CHARACTERIZATION.
RX PubMed=10987552; DOI=10.1007/s004250000277;
RA Membre N., Bernier F., Staiger D., Berna A.;
RT "Arabidopsis thaliana germin-like proteins: common and specific features
RT point to a variety of functions.";
RL Planta 211:345-354(2000).
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: May not form oligomer.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed during germination, and also in green
CC shoots, etiolated seedlings and whole seedlings.
CC -!- MISCELLANEOUS: Is the most highly expressed of the GLP genes.
CC -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR EMBL; X91921; CAA63014.1; -; mRNA.
DR EMBL; D89055; BAA77207.1; -; Genomic_DNA.
DR EMBL; AF090733; AAD05223.1; -; Genomic_DNA.
DR EMBL; U75189; AAB51567.1; -; mRNA.
DR EMBL; U75190; AAB51568.1; -; mRNA.
DR EMBL; U75196; AAB51574.1; -; mRNA.
DR EMBL; U75197; AAB51575.1; -; mRNA.
DR EMBL; U75201; AAB51579.1; -; mRNA.
DR EMBL; U75206; AAB51584.1; -; mRNA.
DR EMBL; U95034; AAB51750.1; -; mRNA.
DR EMBL; U95035; AAB51751.1; -; mRNA.
DR EMBL; AC010926; AAG51848.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35348.1; -; Genomic_DNA.
DR EMBL; AY085951; AAM63161.1; -; mRNA.
DR PIR; F96750; F96750.
DR RefSeq; NP_177405.1; NM_105920.2.
DR AlphaFoldDB; P94040; -.
DR SMR; P94040; -.
DR STRING; 3702.AT1G72610.1; -.
DR PaxDb; P94040; -.
DR PRIDE; P94040; -.
DR ProteomicsDB; 248573; -.
DR EnsemblPlants; AT1G72610.1; AT1G72610.1; AT1G72610.
DR GeneID; 843593; -.
DR Gramene; AT1G72610.1; AT1G72610.1; AT1G72610.
DR KEGG; ath:AT1G72610; -.
DR Araport; AT1G72610; -.
DR TAIR; locus:2030205; AT1G72610.
DR eggNOG; ENOG502QT7C; Eukaryota.
DR HOGENOM; CLU_015790_0_2_1; -.
DR OMA; VSFNSPN; -.
DR OrthoDB; 1164277at2759; -.
DR PhylomeDB; P94040; -.
DR PRO; PR:P94040; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P94040; baseline and differential.
DR Genevisible; P94040; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
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 1: Evidence at protein 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..208
FT /note="Germin-like protein subfamily 3 member 1"
FT /id="PRO_0000010826"
FT DOMAIN 52..198
FT /note="Cupin type-1"
FT /evidence="ECO:0000255"
FT BINDING 100
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 107
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 146
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 23..38
FT /evidence="ECO:0000250"
FT CONFLICT 13
FT /note="A -> G (in Ref. 1; CAA63014)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="G -> A (in Ref. 1; CAA63014)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="P -> R (in Ref. 1; CAA63014)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 208 AA; 21559 MW; E496DF08E5015844 CRC64;
MLRTIFLLSL LFALSNASVQ DFCVANLKRA ETPAGYPCIR PIHVKATDFV FSGLGTPGNT
TNIINAAVTP AFAAQFPGLN GLGLSTARLD LAPKGVIPMH THPGASEVLF VLTGSITAGF
VSSANAVYVQ TLKPGQVMVF PQGLLHFQIN AGKSSASAVV TFNSANPGLQ ILDFALFANS
LPTELVVGTT FLDATTVKKL KGVLGGTG
