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AT74_ARATH
ID   AT74_ARATH              Reviewed;         316 AA.
AC   Q9MAA2; Q0WMW9;
DT   29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Phosphoglycerate mutase-like protein AT74 {ECO:0000305};
DE            Short=At-74 {ECO:0000303|PubMed:15737980};
GN   OrderedLocusNames=At3g05170 {ECO:0000312|Araport:AT3G05170};
GN   ORFNames=T12H1.14 {ECO:0000312|EMBL:AAF27023.1};
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] OF 1-284.
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   [4]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY SUCROSE.
RX   PubMed=15737980; DOI=10.1093/jxb/eri105;
RA   Bourgis F., Botha F.C., Mani S., Hiten F.N., Rigden D.J., Verbruggen N.;
RT   "Characterization and functional investigation of an Arabidopsis cDNA
RT   encoding a homologue to the d-PGMase superfamily.";
RL   J. Exp. Bot. 56:1129-1142(2005).
CC   -!- FUNCTION: Phosphoglycerate mutase-like protein lacking PGM activity.
CC       May play a role in carbohydrates metabolism.
CC       {ECO:0000269|PubMed:15737980}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, flowers and
CC       siliques. {ECO:0000269|PubMed:15737980}.
CC   -!- INDUCTION: By sucrose. {ECO:0000269|PubMed:15737980}.
CC   -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC       {ECO:0000305}.
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DR   EMBL; AC009177; AAF27023.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE74200.1; -; Genomic_DNA.
DR   EMBL; AK229691; BAF01531.1; -; mRNA.
DR   RefSeq; NP_187168.1; NM_111390.2.
DR   AlphaFoldDB; Q9MAA2; -.
DR   SMR; Q9MAA2; -.
DR   STRING; 3702.AT3G05170.1; -.
DR   PaxDb; Q9MAA2; -.
DR   PRIDE; Q9MAA2; -.
DR   ProteomicsDB; 246825; -.
DR   EnsemblPlants; AT3G05170.1; AT3G05170.1; AT3G05170.
DR   GeneID; 819681; -.
DR   Gramene; AT3G05170.1; AT3G05170.1; AT3G05170.
DR   KEGG; ath:AT3G05170; -.
DR   Araport; AT3G05170; -.
DR   TAIR; locus:2096249; AT3G05170.
DR   eggNOG; ENOG502QTHF; Eukaryota.
DR   HOGENOM; CLU_033323_3_2_1; -.
DR   InParanoid; Q9MAA2; -.
DR   OMA; HMADSDQ; -.
DR   OrthoDB; 800109at2759; -.
DR   PhylomeDB; Q9MAA2; -.
DR   PRO; PR:Q9MAA2; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9MAA2; baseline and differential.
DR   Genevisible; Q9MAA2; AT.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0005975; P:carbohydrate metabolic process; TAS:UniProtKB.
DR   CDD; cd07067; HP_PGM_like; 1.
DR   Gene3D; 3.40.50.1240; -; 1.
DR   InterPro; IPR013078; His_Pase_superF_clade-1.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR001345; PG/BPGM_mutase_AS.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; SSF53254; 1.
DR   PROSITE; PS00175; PG_MUTASE; 1.
PE   2: Evidence at transcript level;
KW   Reference proteome.
FT   CHAIN           1..316
FT                   /note="Phosphoglycerate mutase-like protein AT74"
FT                   /id="PRO_0000430635"
FT   REGION          275..316
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        17
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
FT   ACT_SITE        106
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P62707"
SQ   SEQUENCE   316 AA;  36880 MW;  84929674BE351F08 CRC64;
     MSPDNKLLPK RIILVRHGES EGNLDTAAYT TTPDHKIQLT DSGLLQAQEA GARLHALISS
     NPSSPEWRVY FYVSPYDRTR STLREIGRSF SRRRVIGVRE ECRIREQDFG NFQVKERMRA
     TKKVRERFGR FFYRFPEGES AADVFDRVSS FLESLWRDID MNRLHINPSH ELNFVIVSHG
     LTSRVFLMKW FKWSVEQFEG LNNPGNSEIR VMELGQGGDY SLAIHHTEEE LATWGLSPEM
     IADQKWRANA HKGEWKEDCK WYFGDFFDHM ADSDKECETE ATEDREEEEE EEGKRVNLLT
     SSEYSNEPEL YNGQCC
 
 
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