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Q9D358 (PPAC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low molecular weight phosphotyrosine protein phosphatase

Short name=LMW-PTP
Short name=LMW-PTPase
EC=3.1.3.48
Alternative name(s):
Low molecular weight cytosolic acid phosphatase
EC=3.1.3.2
Gene names
Name:Acp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates By similarity. UniProtKB P11064

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate. UniProtKB P11064

A phosphate monoester + H2O = an alcohol + phosphate.

Subunit structure

Interacts with the SH3 domain of SPTAN1. Interacts with EPHA2; dephosphorylates EPHA2. Interacts with EPHB1 By similarity.

Subcellular location

Cytoplasm By similarity UniProtKB P41498.

Tissue specificity

Widely expressed with highest levels in brain and liver and lowest levels in muscle. Ref.1

Sequence similarities

Belongs to the low molecular weight phosphotyrosine protein phosphatase family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 (identifier: Q9D358-1)

Also known as: m-IF1;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.1 (identifier: Q9D358-2)

Also known as: m-IF2;

The sequence of this isoform differs from the canonical sequence as follows:
     41-74: RIDSAATSTYEVGNPPDYRGQNCMRKHGIHMQHI → AIDSSAVSDWNVGRPPDPRAVSCLRNRGISTAHK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity UniProtKB P41498
Chain2 – 158157Low molecular weight phosphotyrosine protein phosphatase
PRO_0000046559

Sites

Active site131Nucleophile By similarity UniProtKB P11064
Active site191 By similarity UniProtKB P11064
Active site1301Proton donor By similarity UniProtKB P11064

Amino acid modifications

Modified residue21N-acetylalanine By similarity UniProtKB P41498
Modified residue1321Phosphotyrosine By similarity UniProtKB P24666
Modified residue1331Phosphotyrosine By similarity

Natural variations

Alternative sequence41 – 7434RIDSA…HMQHI → AIDSSAVSDWNVGRPPDPRA VSCLRNRGISTAHK in isoform 2. Ref.1
VSP_050726
Natural variant141L → P. Ref.1
Natural variant1571T → P. Ref.1
Isoform 2:
Natural variant671R → H.

Secondary structure

.................... 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (m-IF1) [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A374BE5C183226AE

FASTA15818,192
        10         20         30         40         50         60 
MAEVGSKSVL FVCLGNICRS PIAEAVFRKL VTDEKVSDNW RIDSAATSTY EVGNPPDYRG 

        70         80         90        100        110        120 
QNCMRKHGIH MQHIARQITK EDFATFDYIL CMDESNLRDL NRKSNQVKNC KAKIELLGSY 

       130        140        150 
DPQKQLIIED PYYGNDSDFE VVYQQCLRCC KAFLEKTY 

« Hide

Isoform 2 (m-IF2) [UniParc].

Checksum: A2A1AF4BF774889E
Show »

FASTA15817,941

References

« Hide 'large scale' references
[1]"Cloning of murine low molecular weight phosphotyrosine protein phosphatase cDNA: identification of a new isoform."
Magherini F., Giannoni E., Raugei G., Cirri P., Paoli P., Modesti A., Camici G., Ramponi G.
FEBS Lett. 437:263-266(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, VARIANTS PRO-14 AND PRO-157.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Cerebellum, Embryo, Skin and Spinal cord.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: FVB/N.
[4]"Structural genomics of protein phosphatases."
Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P., Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S., Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y., Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R. expand/collapse author list , Sali A., Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.
J. Struct. Funct. Genomics 8:121-140(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-158.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y17343 mRNA. Translation: CAA76753.1.
Y17344 mRNA. Translation: CAA76754.1.
Y17345 mRNA. Translation: CAA76755.1.
AK014603 mRNA. Translation: BAB29458.1.
AK018329 mRNA. Translation: BAB31164.1.
AK019186 mRNA. Translation: BAB31593.1.
AK082955 mRNA. Translation: BAC38707.1.
BC039744 mRNA. Translation: AAH39744.1.
RefSeqNP_001103709.1. NM_001110239.1.
NP_067305.2. NM_021330.4.
XP_006542863.1. XM_006542800.1.
UniGeneMm.359831.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2P4UX-ray1.90A/B/C/D2-158[»]
ProteinModelPortalQ9D358.
SMRQ9D358. Positions 6-158.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197927. 1 interaction.
IntActQ9D358. 2 interactions.
MINTMINT-1855654.

PTM databases

PhosphoSiteQ9D358.

2D gel databases

REPRODUCTION-2DPAGEQ9D358.

Proteomic databases

PaxDbQ9D358.
PRIDEQ9D358.

Protocols and materials databases

DNASU11431.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000062740; ENSMUSP00000106509; ENSMUSG00000044573. [Q9D358-1]
GeneID102642088.
11431.
KEGGmmu:11431.
mmu:631286.
UCSCuc007ngw.2. mouse. [Q9D358-1]

Organism-specific databases

CTD52.
MGIMGI:87881. Acp1.

Phylogenomic databases

eggNOGCOG0394.
GeneTreeENSGT00500000044891.
HOGENOMHOG000273094.
HOVERGENHBG007540.
InParanoidQ9D358.
KOK14394.
OrthoDBEOG7QZGCG.
PhylomeDBQ9D358.
TreeFamTF353727.

Gene expression databases

ArrayExpressQ9D358.
BgeeQ9D358.
CleanExMM_ACP1.
GenevestigatorQ9D358.

Family and domain databases

InterProIPR023485. Ptyr_pPase_SF.
IPR002115. Tyr_Pase_low_mol_wt_mml.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERPTHR11717. PTHR11717. 1 hit.
PfamPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSPR00719. LMWPTPASE.
PR00720. MAMMALPTPASE.
SMARTSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMSSF52788. SSF52788. 1 hit.
ProtoNetSearch...

Other

NextBio278712.
PROQ9D358.
SOURCESearch...

Entry information

Entry namePPAC_MOUSE
AccessionPrimary (citable) accession number: Q9D358
Secondary accession number(s): O88739, O88740, Q9QWF5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot