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GAE2_ARATH
ID   GAE2_ARATH              Reviewed;         434 AA.
AC   Q9LPC1; Q0WRB6; Q8LFM5;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=UDP-glucuronate 4-epimerase 2;
DE            EC=5.1.3.6;
DE   AltName: Full=UDP-glucuronic acid epimerase 2;
GN   Name=GAE2; OrderedLocusNames=At1g02000; ORFNames=F22M8.13;
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 [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   [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].
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 143-434.
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION, AND NOMENCLATURE.
RX   PubMed=11554483; DOI=10.1023/a:1010671129803;
RA   Reiter W.-D., Vanzin G.F.;
RT   "Molecular genetics of nucleotide sugar interconversion pathways in
RT   plants.";
RL   Plant Mol. Biol. 47:95-113(2001).
RN   [7]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   PubMed=15247385; DOI=10.1104/pp.104.043745;
RA   Moelhoej M., Verma R., Reiter W.-D.;
RT   "The biosynthesis of D-galacturonate in plants. Functional cloning and
RT   characterization of a membrane-anchored UDP-D-glucuronate 4-epimerase from
RT   Arabidopsis.";
RL   Plant Physiol. 135:1221-1230(2004).
RN   [8]
RP   TISSUE SPECIFICITY.
RX   PubMed=15225656; DOI=10.1016/j.febslet.2004.06.005;
RA   Usadel B., Schlueter U., Moelhoej M., Gipmans M., Verma R., Kossmann J.,
RA   Reiter W.-D., Pauly M.;
RT   "Identification and characterization of a UDP-D-glucuronate 4-epimerase in
RT   Arabidopsis.";
RL   FEBS Lett. 569:327-331(2004).
CC   -!- FUNCTION: Involved in the synthesis of the negatively charged
CC       monosaccharide that forms the backbone of pectic cell wall components.
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP-alpha-D-glucuronate = UDP-alpha-D-galacturonate;
CC         Xref=Rhea:RHEA:11404, ChEBI:CHEBI:57635, ChEBI:CHEBI:58052;
CC         EC=5.1.3.6;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: In roots, leaves, siliques, flowers, pollen and
CC       stems. {ECO:0000269|PubMed:15225656, ECO:0000269|PubMed:15247385}.
CC   -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM61323.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC020622; AAF76478.1; -; Genomic_DNA.
DR   EMBL; CP002684; AEE27364.1; -; Genomic_DNA.
DR   EMBL; AF334734; AAG50112.1; -; mRNA.
DR   EMBL; AY084754; AAM61323.1; ALT_INIT; mRNA.
DR   EMBL; AK228396; BAF00333.1; -; mRNA.
DR   PIR; A86152; A86152.
DR   RefSeq; NP_171702.1; NM_100080.4.
DR   AlphaFoldDB; Q9LPC1; -.
DR   SMR; Q9LPC1; -.
DR   STRING; 3702.AT1G02000.1; -.
DR   iPTMnet; Q9LPC1; -.
DR   PaxDb; Q9LPC1; -.
DR   PRIDE; Q9LPC1; -.
DR   ProteomicsDB; 247384; -.
DR   EnsemblPlants; AT1G02000.1; AT1G02000.1; AT1G02000.
DR   GeneID; 839289; -.
DR   Gramene; AT1G02000.1; AT1G02000.1; AT1G02000.
DR   KEGG; ath:AT1G02000; -.
DR   Araport; AT1G02000; -.
DR   TAIR; locus:2025472; AT1G02000.
DR   eggNOG; KOG1371; Eukaryota.
DR   HOGENOM; CLU_007383_1_2_1; -.
DR   InParanoid; Q9LPC1; -.
DR   OMA; MHIDNIP; -.
DR   OrthoDB; 662484at2759; -.
DR   PhylomeDB; Q9LPC1; -.
DR   BRENDA; 5.1.3.6; 399.
DR   PRO; PR:Q9LPC1; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LPC1; baseline and differential.
DR   Genevisible; Q9LPC1; AT.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050378; F:UDP-glucuronate 4-epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR001509; Epimerase_deHydtase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF01370; Epimerase; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Golgi apparatus; Isomerase; Membrane; NAD;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..434
FT                   /note="UDP-glucuronate 4-epimerase 2"
FT                   /id="PRO_0000292597"
FT   TRANSMEM        32..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        243
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         93..124
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   434 AA;  48133 MW;  2B67F704D617FD6E CRC64;
     MSHLDDIPST PGKFKMMDKS PFFLHRTRWQ SSVAKLAFWS LVFFGLLFIF FYRSPISNPD
     SSRRSLRTYS WGGPAWEKRV RSSARVRTRN GVSVLVTGAA GFVGTHVSAA LKRRGDGVLG
     LDNFNDYYDT SLKRSRQALL ERSGVFIVEG DINDLSLLKK LFEVVPFTHV MHLAAQAGVR
     YAMENPGSYV HSNIAGFVNL LEVCKSANPQ PAIVWASSSS VYGLNTKVPF SEKDRTDQPA
     SLYAATKKAG EEIAHTYNHI YGLSLTGLRF FTVYGPWGRP DMAYFFFTRD ILKGKAISIF
     EGANHGTVAR DFTYIDDIVK GCLGALDTAE KSTGSGGKKR GAAQLRVFNL GNTSPVPVTD
     LVSILERLLK VKAKRNMMKL PRNGDVPFTH ANISSAQREF GYKPSTDLQT GLKKFVRWYL
     GYYKQGGKKV AAAA
 
 
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