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GL33_ARATH
ID   GL33_ARATH              Reviewed;         211 AA.
AC   P94072; P94028;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Germin-like protein subfamily 3 member 3;
DE            Short=AtGER3;
DE            Short=AtGLP2;
DE   Flags: Precursor;
GN   Name=GER3; Synonyms=GLP2A, GLP2B, GLP3, GLP3A, GLP3B;
GN   OrderedLocusNames=At5g20630; ORFNames=T1M15.30;
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].
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 [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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10487221; DOI=10.1023/a:1006278030024;
RA   Staiger D.J., Apel K., Trepp G.B.;
RT   "The Atger3 promoter confers circadian clock-regulated transcription with
RT   peak expression at the beginning of the night.";
RL   Plant Mol. Biol. 40:873-882(1999).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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].
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   [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).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22092075; DOI=10.1021/pr200917t;
RA   Aryal U.K., Krochko J.E., Ross A.R.;
RT   "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT   polyethylene glycol fractionation, immobilized metal-ion affinity
RT   chromatography, two-dimensional gel electrophoresis and mass
RT   spectrometry.";
RL   J. Proteome Res. 11:425-437(2012).
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   -!- TISSUE SPECIFICITY: Expressed in leaves and flowers.
CC   -!- INDUCTION: Expressed with a circadian rhythm, with peak expression at
CC       the beginning of the night.
CC   -!- SIMILARITY: Belongs to the germin family. {ECO:0000305}.
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DR   EMBL; Y12673; CAA73213.1; -; mRNA.
DR   EMBL; D89374; BAA77208.1; -; Genomic_DNA.
DR   EMBL; U75188; AAB51566.1; -; mRNA.
DR   EMBL; U75193; AAB51571.1; -; mRNA.
DR   EMBL; U75195; AAB51573.1; -; mRNA.
DR   EMBL; U75203; AAB51581.1; -; mRNA.
DR   EMBL; U75205; AAB51583.1; -; mRNA.
DR   EMBL; AJ132237; CAB54516.1; -; Genomic_DNA.
DR   EMBL; AF296832; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CP002688; AED92868.1; -; Genomic_DNA.
DR   EMBL; AY039516; AAK62573.1; -; mRNA.
DR   EMBL; AY055786; AAL06953.1; -; mRNA.
DR   RefSeq; NP_197563.1; NM_122070.3.
DR   AlphaFoldDB; P94072; -.
DR   SMR; P94072; -.
DR   BioGRID; 17460; 3.
DR   STRING; 3702.AT5G20630.1; -.
DR   Allergome; 779; Ara t GLP.
DR   iPTMnet; P94072; -.
DR   PaxDb; P94072; -.
DR   PRIDE; P94072; -.
DR   ProteomicsDB; 230488; -.
DR   EnsemblPlants; AT5G20630.1; AT5G20630.1; AT5G20630.
DR   GeneID; 832185; -.
DR   Gramene; AT5G20630.1; AT5G20630.1; AT5G20630.
DR   KEGG; ath:AT5G20630; -.
DR   Araport; AT5G20630; -.
DR   TAIR; locus:2180444; AT5G20630.
DR   eggNOG; ENOG502QT7C; Eukaryota.
DR   HOGENOM; CLU_015790_0_2_1; -.
DR   InParanoid; P94072; -.
DR   OMA; KMIIQIF; -.
DR   OrthoDB; 1164277at2759; -.
DR   PhylomeDB; P94072; -.
DR   PRO; PR:P94072; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; P94072; baseline and differential.
DR   Genevisible; P94072; AT.
DR   GO; GO:0048046; C:apoplast; HDA:TAIR.
DR   GO; GO:0031012; C:extracellular matrix; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; HDA:TAIR.
DR   GO; GO:0009536; C:plastid; HDA:TAIR.
DR   GO; GO:0099503; C:secretory vesicle; 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   Phosphoprotein; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..20
FT   CHAIN           21..211
FT                   /note="Germin-like protein subfamily 3 member 3"
FT                   /id="PRO_0000010828"
FT   DOMAIN          55..201
FT                   /note="Cupin type-1"
FT                   /evidence="ECO:0000255"
FT   BINDING         103
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         110
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         140
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22092075"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..41
FT                   /evidence="ECO:0000250"
FT   CONFLICT        59
FT                   /note="T -> K (in Ref. 3; AAB51581/AAB51566)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   211 AA;  21836 MW;  BA0591DC005BFA24 CRC64;
     MKMIIQIFFI ISLISTISFA SVQDFCVADP KGPQSPSGYS CKNPDQVTEN DFAFTGLGTA
     GNTSNIIKAA VTPAFAPAYA GINGLGVSLA RLDLAGGGVI PLHTHPGASE VLVVIQGTIC
     AGFISSANKV YLKTLNRGDS MVFPQGLLHF QLNSGKGPAL AFVAFGSSSP GLQILPFALF
     ANDLPSELVE ATTFLSDAEV KKLKGVLGGT N
 
 
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