SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P83379

- PPH2_SOLLC

UniProt

P83379 - PPH2_SOLLC

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Purple acid phosphatase isozyme LeSAP2
Gene
N/A
Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.1 Publication

GO - Molecular functioni

  1. acid phosphatase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15162.
SABIO-RKP83379.

Names & Taxonomyi

Protein namesi
Recommended name:
Purple acid phosphatase isozyme LeSAP2 (EC:3.1.3.2)
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
ProteomesiUP000004994: Unplaced

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›7›7Purple acid phosphatase isozyme LeSAP2
PRO_0000114476

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Interactioni

Subunit structurei

Monomer.1 Publication

Family & Domainsi

Sequence similaritiesi

Sequencei

Sequence statusi: Fragment.

Length:7
Mass (Da):810
Last modified:October 1, 2002 - v1
Checksum:i672AA862C9C729A0
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei7 – 71

Cross-referencesi

3D structure databases

ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-15162.
SABIO-RK P83379.

Family and domain databases

ProtoNeti Search...

Publicationsi

  1. "Purification and characterization of two secreted purple acid phosphatase isozymes from phosphate-starved tomato (Lycopersicon esculentum) cell cultures."
    Bozzo G.G., Raghothama K.G., Plaxton W.C.
    Eur. J. Biochem. 269:6278-6286(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION.
    Strain: cv. Moneymaker.
    Tissue: Seed.

Entry informationi

Entry nameiPPH2_SOLLC
AccessioniPrimary (citable) accession number: P83379
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 2002
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

In L.esculentum there are at least two isozymes of purple acid phosphatase.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3