GL32_ARATH
ID GL32_ARATH Reviewed; 227 AA.
AC Q9SR72;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Germin-like protein subfamily 3 member 2;
DE Flags: Precursor;
GN OrderedLocusNames=At3g10080; ORFNames=T22K18.9;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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].
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.
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; AC010927; AAF04416.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74857.1; -; Genomic_DNA.
DR EMBL; AY085880; AAM63093.1; -; mRNA.
DR RefSeq; NP_187619.1; NM_111843.5.
DR AlphaFoldDB; Q9SR72; -.
DR SMR; Q9SR72; -.
DR STRING; 3702.AT3G10080.1; -.
DR PaxDb; Q9SR72; -.
DR PRIDE; Q9SR72; -.
DR ProteomicsDB; 247393; -.
DR EnsemblPlants; AT3G10080.1; AT3G10080.1; AT3G10080.
DR GeneID; 820169; -.
DR Gramene; AT3G10080.1; AT3G10080.1; AT3G10080.
DR KEGG; ath:AT3G10080; -.
DR Araport; AT3G10080; -.
DR TAIR; locus:2100133; AT3G10080.
DR eggNOG; ENOG502RDTK; Eukaryota.
DR HOGENOM; CLU_015790_0_3_1; -.
DR InParanoid; Q9SR72; -.
DR PhylomeDB; Q9SR72; -.
DR PRO; PR:Q9SR72; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9SR72; baseline and differential.
DR Genevisible; Q9SR72; 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; 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.
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..227
FT /note="Germin-like protein subfamily 3 member 2"
FT /id="PRO_0000010827"
FT DOMAIN 68..213
FT /note="Cupin type-1"
FT /evidence="ECO:0000255"
FT BINDING 115
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 122
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 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..54
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 24779 MW; 527F80029D2302E5 CRC64;
MEANTLFLLK ALCLLCFNVC FTLASDPDPI QDFCIPKPVT SPYHDHHFST NLPCKNSSEV
TTEDFVFSGL KTAGNFTETG FATVPVGPEN FPGLNTLGIS FVRADLKPGS INPPHYHPRA
TEVAHLVKGR VYSGFVDSNN KVYAKVMEEG EMMVYPKGLV HFQMNVGDVT ATIVGGLNSQ
NPGIQKIPSV VFGSGINEEL LMKAFGLSLK QIGTLKKRFD PVMSNEH
