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Protein

Serine/threonine-protein phosphatase PP2A-1 catalytic subunit

Gene
N/A
Organism
Acetabularia peniculus (Green alga) (Polyphysa peniculus)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Cofactori

Mn2+By similarityNote: Binds 2 manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi54 – 541Manganese 1By similarity
Metal bindingi56 – 561Manganese 1By similarity
Metal bindingi82 – 821Manganese 1By similarity
Metal bindingi82 – 821Manganese 2By similarity
Metal bindingi114 – 1141Manganese 2By similarity
Active sitei115 – 1151Proton donorBy similarity
Metal bindingi164 – 1641Manganese 2By similarity
Metal bindingi238 – 2381Manganese 2By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase PP2A-1 catalytic subunit (EC:3.1.3.16)
OrganismiAcetabularia peniculus (Green alga) (Polyphysa peniculus)
Taxonomic identifieri35862 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeChlorophytaUlvophyceaeDasycladalesPolyphysaceaeAcetabularia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 307307Serine/threonine-protein phosphatase PP2A-1 catalytic subunitPRO_0000058851Add
BLAST

Proteomic databases

PRIDEiP48577.

Structurei

3D structure databases

ProteinModelPortaliP48577.
SMRiP48577. Positions 2-307.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the PPP phosphatase family. PP-2A subfamily.Curated

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48577-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVVYKQLDEW IEHLMQCKPL PEENVKELVA KAREVFSNEK NVQPVKMPVT
60 70 80 90 100
VCGDIHGQFH DMVELFKIGG TCPDTNYLFM GDYVDRGYNS VETVTLLVSL
110 120 130 140 150
KVRYPERITI LRGNHESRQI TQVYGFYDEC LRKYGNANVW QLFTDLFDFL
160 170 180 190 200
PLTGLIENEV FCLHGGLSPA LDTLDQIREL DRIQEVPHEG PMCDLLWSDP
210 220 230 240 250
DERLGWGISP RGAGYTFGQD ISEQFNVRNS LKLVARAHQL VMEGYNWSHE
260 270 280 290 300
KNVVTIFSAP NYCYRCGNMA AIMEVAEGMD KGFQQFEPAP RRGAEGEVNR

RTPDYFL
Length:307
Mass (Da):35,246
Last modified:February 1, 1996 - v1
Checksum:iAA021D16540EDA98
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26654 mRNA. Translation: CAA81395.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z26654 mRNA. Translation: CAA81395.1.

3D structure databases

ProteinModelPortaliP48577.
SMRiP48577. Positions 2-307.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP48577.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR029052. Metallo-depent_PP-like.
IPR006186. Ser/Thr-sp_prot-phosphatase.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
PRINTSiPR00114. STPHPHTASE.
SMARTiSM00156. PP2Ac. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
PROSITEiPS00125. SER_THR_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Protein phosphatase 2A, a potential regulator of actin dynamics and actin-based organelle motility in the green alga Acetabularia."
    Menzel D., Vugrek O., Frank S., Elsner-Menzel C.
    Eur. J. Cell Biol. 67:179-187(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiPP2A_ACEPE
AccessioniPrimary (citable) accession number: P48577
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.