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PME61_ARATH
ID   PME61_ARATH             Reviewed;         587 AA.
AC   Q9FK05;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Probable pectinesterase/pectinesterase inhibitor 61;
DE   Includes:
DE     RecName: Full=Pectinesterase inhibitor 61;
DE     AltName: Full=Pectin methylesterase inhibitor 61;
DE   Includes:
DE     RecName: Full=Pectinesterase 61;
DE              Short=PE 61;
DE              EC=3.1.1.11;
DE     AltName: Full=AtPMEpcrF;
DE     AltName: Full=Pectin methylesterase 61;
DE              Short=AtPME61;
GN   Name=PME61; Synonyms=ARATH61; OrderedLocusNames=At5g53370;
GN   ORFNames=K19E1.17;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
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   TISSUE SPECIFICITY.
RX   PubMed=9767082; DOI=10.1016/s0378-1119(98)00431-4;
RA   Micheli F., Holliger C., Goldberg R., Richard L.;
RT   "Characterization of the pectin methylesterase-like gene AtPME3: a new
RT   member of a gene family comprising at least 12 genes in Arabidopsis
RT   thaliana.";
RL   Gene 220:13-20(1998).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=15337457; DOI=10.1016/j.carres.2004.06.023;
RA   Markovic O., Janecek S.;
RT   "Pectin methylesterases: sequence-structural features and phylogenetic
RT   relationships.";
RL   Carbohydr. Res. 339:2281-2295(2004).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=16622707; DOI=10.1007/s00425-006-0261-9;
RA   Louvet R., Cavel E., Gutierrez L., Guenin S., Roger D., Gillet F.,
RA   Guerineau F., Pelloux J.;
RT   "Comprehensive expression profiling of the pectin methylesterase gene
RT   family during silique development in Arabidopsis thaliana.";
RL   Planta 224:782-791(2006).
CC   -!- FUNCTION: Acts in the modification of cell walls via
CC       demethylesterification of cell wall pectin. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[(1->4)-alpha-D-galacturonosyl methyl ester](n) + n H2O =
CC         [(1->4)-alpha-D-galacturonosyl](n) + n H(+) + n methanol;
CC         Xref=Rhea:RHEA:22380, Rhea:RHEA-COMP:14570, Rhea:RHEA-COMP:14573,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC         ChEBI:CHEBI:140522, ChEBI:CHEBI:140523; EC=3.1.1.11;
CC   -!- PATHWAY: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-
CC       gluconate from pectin: step 1/5.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in siliques, floral stems and rosettes
CC       leaves. {ECO:0000269|PubMed:16622707, ECO:0000269|PubMed:9767082}.
CC   -!- DEVELOPMENTAL STAGE: Expressed throughout silique development.
CC       {ECO:0000269|PubMed:16622707}.
CC   -!- MISCELLANEOUS: The PMEI region may act as an autoinhibitory domain and
CC       prevent untimely PME activity during transport.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the PMEI family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the pectinesterase
CC       family. {ECO:0000305}.
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DR   EMBL; AB013388; BAB09799.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96345.1; -; Genomic_DNA.
DR   EMBL; AF360340; AAK28637.1; -; mRNA.
DR   EMBL; AY051077; AAK93754.1; -; mRNA.
DR   RefSeq; NP_200149.1; NM_124716.3.
DR   AlphaFoldDB; Q9FK05; -.
DR   SMR; Q9FK05; -.
DR   STRING; 3702.AT5G53370.1; -.
DR   iPTMnet; Q9FK05; -.
DR   PaxDb; Q9FK05; -.
DR   PRIDE; Q9FK05; -.
DR   ProteomicsDB; 226183; -.
DR   EnsemblPlants; AT5G53370.1; AT5G53370.1; AT5G53370.
DR   GeneID; 835418; -.
DR   Gramene; AT5G53370.1; AT5G53370.1; AT5G53370.
DR   KEGG; ath:AT5G53370; -.
DR   Araport; AT5G53370; -.
DR   TAIR; locus:2154277; AT5G53370.
DR   eggNOG; ENOG502QRD0; Eukaryota.
DR   HOGENOM; CLU_012243_9_1_1; -.
DR   InParanoid; Q9FK05; -.
DR   OMA; ENWAGPT; -.
DR   PhylomeDB; Q9FK05; -.
DR   UniPathway; UPA00545; UER00823.
DR   PRO; PR:Q9FK05; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FK05; baseline and differential.
DR   Genevisible; Q9FK05; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030599; F:pectinesterase activity; ISS:TAIR.
DR   GO; GO:0046910; F:pectinesterase inhibitor activity; IBA:GO_Central.
DR   GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR   GO; GO:0045490; P:pectin catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.20.140.40; -; 1.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR035513; Invertase/methylesterase_inhib.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR033131; Pectinesterase_Asp_AS.
DR   InterPro; IPR000070; Pectinesterase_cat.
DR   InterPro; IPR006501; Pectinesterase_inhib_dom.
DR   Pfam; PF01095; Pectinesterase; 1.
DR   Pfam; PF04043; PMEI; 1.
DR   SMART; SM00856; PMEI; 1.
DR   SUPFAM; SSF101148; SSF101148; 1.
DR   SUPFAM; SSF51126; SSF51126; 1.
DR   TIGRFAMs; TIGR01614; PME_inhib; 1.
DR   PROSITE; PS00503; PECTINESTERASE_2; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl esterase; Cell wall biogenesis/degradation; Disulfide bond;
KW   Hydrolase; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..587
FT                   /note="Probable pectinesterase/pectinesterase inhibitor 61"
FT                   /id="PRO_0000371707"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..223
FT                   /note="Pectinesterase inhibitor 61"
FT   REGION          273..571
FT                   /note="Pectinesterase 61"
FT   COMPBIAS        9..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        402
FT                   /note="Proton donor; for pectinesterase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   ACT_SITE        423
FT                   /note="Nucleophile; for pectinesterase activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10040"
FT   BINDING         349
FT                   /ligand="substrate"
FT                   /ligand_note="for pectinesterase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         379
FT                   /ligand="substrate"
FT                   /ligand_note="for pectinesterase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         491
FT                   /ligand="substrate"
FT                   /ligand_note="for pectinesterase activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         493
FT                   /ligand="substrate"
FT                   /ligand_note="for pectinesterase activity"
FT                   /evidence="ECO:0000250"
FT   SITE            401
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   DISULFID        416..436
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   587 AA;  64241 MW;  A60B9271DE489DBD CRC64;
     MGYDRLGPSG PSNPNQKDPA TSLPELQKKT KTKLILFTLA VLVVGVVCFG IFAGIRAVDS
     GKTEPKLTRK PTQAISRTCS KSLYPNLCID TLLDFPGSLT ADENELIHIS FNATLQKFSK
     ALYTSSTITY TQMPPRVRSA YDSCLELLDD SVDALTRALS SVVVVSGDES HSDVMTWLSS
     AMTNHDTCTD GFDEIEGQGG EVKDQVIGAV KDLSEMVSNC LAIFAGKVKD LSGVPVVNNR
     KLLGTEETEE LPNWLKREDR ELLGTPTSAI QADITVSKDG SGTFKTIAEA IKKAPEHSSR
     RFVIYVKAGR YEEENLKVGR KKTNLMFIGD GKGKTVITGG KSIADDLTTF HTATFAATGA
     GFIVRDMTFE NYAGPAKHQA VALRVGGDHA VVYRCNIIGY QDALYVHSNR QFFRECEIYG
     TVDFIFGNAA VILQSCNIYA RKPMAQQKIT ITAQNRKDPN QNTGISIHAC KLLATPDLEA
     SKGSYPTYLG RPWKLYSRVV YMMSDMGDHI DPRGWLEWNG PFALDSLYYG EYMNKGLGSG
     IGQRVKWPGY HVITSTVEAS KFTVAQFISG SSWLPSTGVS FFSGLSQ
 
 
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