Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Serine/threonine-protein phosphatase PP2A-5 catalytic subunit (EC 3.1.3.16) (Protein phosphatase 2A isoform 5)

 PP2A5_ARATH             Reviewed;         307 AA.
O04951; Q1EC63; Q42544;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
20-JUN-2018, entry version 139.
RecName: Full=Serine/threonine-protein phosphatase PP2A-5 catalytic subunit;
EC=3.1.3.16;
AltName: Full=Protein phosphatase 2A isoform 5;
Name=PP2A5 {ECO:0000303|PubMed:17368080}; OrderedLocusNames=At1g69960;
ORFNames=F20P5.30, T17F3.1;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
Stamey R.T., Rundle S.J.;
"Characterization of a novel isoform of a type 2A serine/threonine
protein phosphatase from Arabidopsis thaliana.";
(er) Plant Gene Register PGR95-116(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Quinitio C., Chen H., Kim C.J., Shinn P., Ecker J.R.;
"Arabidopsis ORF clones.";
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
Hayashizaki Y., Shinozaki K.;
"Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
[6]
INTERACTION WITH PP2AA1.
PubMed=10091592; DOI=10.1046/j.1432-1327.1999.00154.x;
Haynes J.G., Hartung A.J., Hendershot J.D. III, Passingham R.S.,
Rundle S.J.;
"Molecular characterization of the B' regulatory subunit gene family
of Arabidopsis protein phosphatase 2A.";
Eur. J. Biochem. 260:127-136(1999).
[7]
INTERACTION WITH CHIP.
PubMed=16640601; DOI=10.1111/j.1365-313X.2006.02730.x;
Luo J., Shen G., Yan J., He C., Zhang H.;
"AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A
subunits and alters plant response to abscisic acid treatment.";
Plant J. 46:649-657(2006).
[8]
GENE FAMILY, AND NOMENCLATURE.
PubMed=17368080; DOI=10.1016/j.tplants.2007.03.003;
Farkas I., Dombradi V., Miskei M., Szabados L., Koncz C.;
"Arabidopsis PPP family of serine/threonine phosphatases.";
Trends Plant Sci. 12:169-176(2007).
[9]
INTERACTION WITH TAF12B.
STRAIN=cv. Wassilewskija;
PubMed=17526916; DOI=10.1093/jxb/erm080;
Robles L.M., Wampole J.S., Christians M.J., Larsen P.B.;
"Arabidopsis enhanced ethylene response 4 encodes an EIN3-interacting
TFIID transcription factor required for proper ethylene response,
including ERF1 induction.";
J. Exp. Bot. 58:2627-2639(2007).
[10]
FUNCTION, INTERACTION WITH B'THETA, AND SUBCELLULAR LOCATION.
PubMed=25489022; DOI=10.1104/pp.114.254409;
Kataya A.R., Heidari B., Hagen L., Kommedal R., Slupphaug G.,
Lillo C.;
"Protein phosphatase 2A holoenzyme is targeted to peroxisomes by
piggybacking and positively affects peroxisomal beta-oxidation.";
Plant Physiol. 167:493-506(2015).
[11]
FUNCTION, INTERACTION WITH CLC-A; CLC-B; CLC-C AND CLC-G, INDUCTION BY
SALT STRESS, AND DISRUPTION PHENOTYPE.
PubMed=27676158; DOI=10.1111/pce.12837;
Hu R., Zhu Y., Wei J., Chen J., Shi H., Shen G., Zhang H.;
"Overexpression of PP2A-C5 that encodes the catalytic subunit 5 of
protein phosphatase 2A in Arabidopsis confers better root and shoot
development under salt conditions.";
Plant Cell Environ. 40:150-164(2017).
[12]
METHYLATION AT LEU-307.
PubMed=28741704; DOI=10.1111/pce.13038;
Creighton M.T., Kolton A., Kataya A.R.A., Maple-Groedem J.,
Averkina I.O., Heidari B., Lillo C.;
"Methylation of protein phosphatase 2A-influence of regulators and
environmental stress factors.";
Plant Cell Environ. 40:2347-2358(2017).
-!- FUNCTION: Associates with the serine/threonine-protein phosphatase
PP2A regulatory subunits A and B' to positively regulates beta-
oxidation of fatty acids and protoauxins in peroxisomes by
dephosphorylating peroxisomal beta-oxidation-related proteins
(PubMed:25489022). Involved in the positive regulation of salt
stress responses. May function by increasing chloride channel
activities on vacuolar membranes (PubMed:27676158).
{ECO:0000269|PubMed:25489022, ECO:0000269|PubMed:27676158}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit. {ECO:0000250};
-!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
constant regulatory subunit (subunit A), that associates with a
variety of regulatory subunits such as subunits B (the
R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families).
Also interacts with CHIP and TAF12B. Interacts with B'THETA
(PubMed:25489022). Interacts with CLC-A, CLC-B, CLC-C and CLC-G
(PubMed:27676158). {ECO:0000250|UniProtKB:P62714,
ECO:0000269|PubMed:10091592, ECO:0000269|PubMed:16640601,
ECO:0000269|PubMed:17526916, ECO:0000269|PubMed:25489022,
ECO:0000269|PubMed:27676158}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:25489022}. Peroxisome
{ECO:0000269|PubMed:25489022}. Note=Interacts with B'THETA in the
cytosol and peroxisomal import occurs by a piggybacking transport.
{ECO:0000269|PubMed:25489022}.
-!- INDUCTION: Induced by salt stress. {ECO:0000269|PubMed:27676158}.
-!- PTM: Reversibly methyl esterified on Leu-307 by leucine carboxyl
methyltransferase 1 (LCMT1) and pectin methylesterase 1 (PME1).
Carboxyl methylation influences the affinity of the catalytic
subunit for the different regulatory subunits, thereby modulating
the PP2A holoenzyme's substrate specificity, enzyme activity and
cellular localization. {ECO:0000305|PubMed:28741704}.
-!- PTM: Phosphorylation of either threonine (by autophosphorylation-
activated protein kinase) or tyrosine results in inactivation of
the phosphatase. Auto-dephosphorylation has been suggested as a
mechanism for reactivation. {ECO:0000250|UniProtKB:P67774}.
-!- PTM: Ubiquitinated. CHIP-mediated ubiquitination enhances
phosphatase activity after an abiotic stress such as low
temperature or darkness (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
conditions, but mutant plants are hypersensitive to salt stress.
{ECO:0000269|PubMed:27676158}.
-!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U39568; AAC49668.1; -; mRNA.
EMBL; AC002062; AAB61116.1; -; Genomic_DNA.
EMBL; AC010675; AAG52565.1; -; Genomic_DNA.
EMBL; CP002684; AEE35002.1; -; Genomic_DNA.
EMBL; BT025871; ABF85773.1; -; mRNA.
EMBL; AK227054; BAE99114.1; -; mRNA.
PIR; B96722; B96722.
RefSeq; NP_177154.1; NM_105665.3.
UniGene; At.20106; -.
ProteinModelPortal; O04951; -.
SMR; O04951; -.
BioGrid; 28554; 4.
STRING; 3702.AT1G69960.1; -.
PaxDb; O04951; -.
PRIDE; O04951; -.
EnsemblPlants; AT1G69960.1; AT1G69960.1; AT1G69960.
GeneID; 843333; -.
Gramene; AT1G69960.1; AT1G69960.1; AT1G69960.
KEGG; ath:AT1G69960; -.
Araport; AT1G69960; -.
TAIR; locus:2020598; AT1G69960.
eggNOG; KOG0371; Eukaryota.
eggNOG; COG0639; LUCA.
HOGENOM; HOG000172696; -.
KO; K04382; -.
OMA; EIRTIDH; -.
OrthoDB; EOG09360EXD; -.
PhylomeDB; O04951; -.
PRO; PR:O04951; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; O04951; baseline and differential.
Genevisible; O04951; AT.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; ISS:TAIR.
GO; GO:2000012; P:regulation of auxin polar transport; IMP:TAIR.
Gene3D; 3.60.21.10; -; 1.
InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
InterPro; IPR029052; Metallo-depent_PP-like.
InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
Pfam; PF00149; Metallophos; 1.
PRINTS; PR00114; STPHPHTASE.
SMART; SM00156; PP2Ac; 1.
PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Hydrolase; Manganese; Metal-binding;
Methylation; Peroxisome; Phosphoprotein; Protein phosphatase;
Reference proteome; Stress response; Ubl conjugation.
CHAIN 1 307 Serine/threonine-protein phosphatase
PP2A-5 catalytic subunit.
/FTId=PRO_0000058856.
ACT_SITE 116 116 Proton donor. {ECO:0000250}.
METAL 55 55 Manganese 1.
{ECO:0000250|UniProtKB:P67775}.
METAL 57 57 Manganese 1.
{ECO:0000250|UniProtKB:P67775}.
METAL 83 83 Manganese 1.
{ECO:0000250|UniProtKB:P67775}.
METAL 83 83 Manganese 2.
{ECO:0000250|UniProtKB:P67775}.
METAL 115 115 Manganese 2.
{ECO:0000250|UniProtKB:P67775}.
METAL 165 165 Manganese 2.
{ECO:0000250|UniProtKB:P67775}.
METAL 239 239 Manganese 2.
{ECO:0000250|UniProtKB:P67775}.
MOD_RES 307 307 Leucine methyl ester.
{ECO:0000305|PubMed:28741704}.
SEQUENCE 307 AA; 35042 MW; D00149EA0E20C82F CRC64;
MPPATGDIDR QIEQLMECKA LSETEVKMLC EHAKTILVEE YNVQPVKCPV TVCGDIHGQF
YDLIELFRIG GSSPDTNYLF MGDYVDRGYY SVETVSLLVA LKVRYRDRLT ILRGNHESRQ
ITQVYGFYDE CLRKYGNANV WKHFTDLFDY LPLTALIESQ VFCLHGGLSP SLDTLDNIRS
LDRIQEVPHE GPMCDLLWSD PDDRCGWGIS PRGAGYTFGQ DIATQFNHTN GLSLISRAHQ
LVMEGFNWCQ EKNVVTVFSA PNYCYRCGNM AAILEIGENM DQNFLQFDPA PRQVEPETTR
KTPDYFL


Related products :

Catalog number Product name Quantity
E1206r Rat ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit alpha isoform 96T
PP2AB_PIG Pig ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit beta isoform 96T
E1235m Human ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit beta isoform 96T
H0449 Serine threonine-protein phosphatase 2B catalytic subunit beta isoform (PPP3CB), Rat, ELISA Kit 96T
SYPL2_MOUSE Bovine ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit alpha isoform 96T
H0444 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Pig, ELISA Kit 96T
E0026h Bovine ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit alpha isoform 96T
E0375m Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit alpha isoform 96T
NXP20_MOUSE Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit alpha isoform 96T
GFRA2_MOUSE Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit alpha isoform 96T
CA055_HUMAN Bovine ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit alpha isoform 96T
E1778m Mouse ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit beta isoform 96T
H0446 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Rat, ELISA Kit 96T
H0443 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Mouse, ELISA Kit 96T
H0448 Serine threonine-protein phosphatase 2B catalytic subunit beta isoform (PPP3CB), Mouse, ELISA Kit 96T
H0447 Serine threonine-protein phosphatase 2B catalytic subunit beta isoform (PPP3CB), Human, ELISA Kit 96T
H0441 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Chicken, ELISA Kit 96T
H0450 Serine threonine-protein phosphatase 2B catalytic subunit gamma isoform (PPP3CC), Human, ELISA Kit 96T
H0440 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Bovine, ELISA Kit 96T
H0451 Serine threonine-protein phosphatase 2B catalytic subunit gamma isoform (PPP3CC), Mouse, ELISA Kit 96T
H0442 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Human, ELISA Kit 96T
H0445 Serine threonine-protein phosphatase 2A catalytic subunit alpha isoform (PPP2CA), Rabbit, ELISA Kit 96T
PP2BA_RAT ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit alpha isoform; organism: Rat; gene name: Ppp3ca 96T
PP2AB_RAT ELISA Kit FOR Serine per threonine-protein phosphatase 2A catalytic subunit beta isoform; organism: Rat; gene name: Ppp2cb 96T
PP2BB_RAT ELISA Kit FOR Serine per threonine-protein phosphatase 2B catalytic subunit beta isoform; organism: Rat; gene name: Ppp3cb 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur