GL120_ARATH
ID GL120_ARATH Reviewed; 222 AA.
AC P92996; Q39106;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Germin-like protein subfamily 1 member 20;
DE AltName: Full=GLP2a copy 2;
DE AltName: Full=GLP2b;
DE AltName: Full=Germin type 2;
DE Short=At-GERM2;
DE Short=AtGER2;
DE Flags: Precursor;
GN Name=GLP5A; Synonyms=GER2, GERM2, GLP2A, GLP2B;
GN OrderedLocusNames=At5g39190; ORFNames=K3K3.6;
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=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 [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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
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: Oligomer (believed to be a pentamer but probably hexamer).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, apoplast
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P92996-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in stems and developing embryos.
CC -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR EMBL; X91957; CAA63023.1; -; mRNA.
DR EMBL; U75192; AAB51570.1; -; mRNA.
DR EMBL; AB010694; BAB09373.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94405.1; -; Genomic_DNA.
DR EMBL; BT003986; AAO42026.1; -; mRNA.
DR EMBL; BT005069; AAO50602.1; -; mRNA.
DR PIR; S71254; S71254.
DR RefSeq; NP_198735.1; NM_123281.4. [P92996-1]
DR AlphaFoldDB; P92996; -.
DR SMR; P92996; -.
DR BioGRID; 19165; 1.
DR STRING; 3702.AT5G39190.1; -.
DR PaxDb; P92996; -.
DR PRIDE; P92996; -.
DR EnsemblPlants; AT5G39190.1; AT5G39190.1; AT5G39190. [P92996-1]
DR GeneID; 833914; -.
DR Gramene; AT5G39190.1; AT5G39190.1; AT5G39190. [P92996-1]
DR KEGG; ath:AT5G39190; -.
DR Araport; AT5G39190; -.
DR TAIR; locus:2157230; AT5G39190.
DR eggNOG; ENOG502QQ4A; Eukaryota.
DR HOGENOM; CLU_015790_0_0_1; -.
DR InParanoid; P92996; -.
DR OMA; SKLWWAN; -.
DR OrthoDB; 1164277at2759; -.
DR PhylomeDB; P92996; -.
DR PRO; PR:P92996; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P92996; baseline and differential.
DR Genevisible; P92996; AT.
DR GO; GO:0048046; C:apoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0031012; C:extracellular matrix; IDA: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 Alternative splicing; Apoplast; Disulfide bond; Glycoprotein; Manganese;
KW Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..222
FT /note="Germin-like protein subfamily 1 member 20"
FT /id="PRO_0000010820"
FT DOMAIN 62..213
FT /note="Cupin type-1"
FT /evidence="ECO:0000255"
FT BINDING 110
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 112
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 159
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..48
FT /evidence="ECO:0000250"
FT CONFLICT 63
FT /note="G -> A (in Ref. 1; CAA63023)"
FT /evidence="ECO:0000305"
FT CONFLICT 98..99
FT /note="RI -> LV (in Ref. 1; CAA63023)"
FT /evidence="ECO:0000305"
FT CONFLICT 107
FT /note="N -> D (in Ref. 1; CAA63023)"
FT /evidence="ECO:0000305"
FT CONFLICT 135
FT /note="Q -> L (in Ref. 1; CAA63023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 222 AA; 23925 MW; E2BD7EDA9D47948C CRC64;
MRVSQSLVPF AIIALVLSFV NAYDPSPLQD FCVAIDDLKG VFVNGRFCKD PKRVDAKDFF
FSGLNVPGNT NNQVGSNVTT VNVDQIPGLN TMGISLVRID YAPHGQNPPH THPRGSEILV
LVEGTLYVGF VSSNQDNNRL FAKVLHPGDV FVFPIGMIHF QVNVGKIPAV AFAGLSSQNA
GVITIANTVF GSNPPIYPEL LARAFQLDAS VVKELQAKFG SI
