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Reviewed, UniProtKB/Swiss-Prot Q9D826 (SOX_MOUSE)

Last modified June 16, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Peroxisomal sarcosine oxidase
      Short name=PSO
    EC=1.5.3.1
    EC=1.5.3.7
Alternative name(s):
    L-pipecolate oxidase
    L-pipecolic acid oxidase
Gene names
Name: Pipox
Synonyms: Pso
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Metabolizes sarcosine, L-pipecolic acid and L-proline By similarity.

Catalytic activity

Sarcosine + H2O + O2 = glycine + formaldehyde + H2O2.

L-pipecolate + O2 = 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2.

Cofactor

Binds 1 FAD per subunit.

Subunit structure

Monomer By similarity.

Subcellular location

Peroxisome By similarity.

Tissue specificity

Kidney and liver.

Sequence similarities

Belongs to the MSOX/MTOX family.

Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

tetrahydrofolate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentperoxisome

Inferred from direct assay. Source: HGNC

   Molecular functionL-pipecolate oxidase activity

Inferred from electronic annotation. Source: EC

sarcosine oxidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 390390Peroxisomal sarcosine oxidase
PRO_0000213774

Regions

Nucleotide binding9 – 3931FAD Potential
Motif388 – 3903Microbody targeting signal Potential

Amino acid modifications

Modified residue3191S-8alpha-FAD cysteine Probable

Experimental info

Sequence conflict1641Q → H in AAC39948. Ref.1
Sequence conflict3331C → W in AAC39948. Ref.1
Sequence conflict3521K → T in AAC39948. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D826-1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 0C33A96A24731EE0

FASTA39043,847
        10         20         30         40         50         60 
MAAQTDFWDA IVIGAGIQGC FTAYHLAKHS KSVLLLEQFF LPHSRGSSHG QSRIIRKAYP 

        70         80         90        100        110        120 
EDFYTMMMKE CYQTWAQLER EAGTQLHRQT ELLLLGTKEN PGLKTIQATL SRQGIDHEYL 

       130        140        150        160        170        180 
SSVDLKQRFP NIRFTRGEVG LLDKTGGVLY ADKALRALQH IICQLGGTVC DGEKVVEIRP 

       190        200        210        220        230        240 
GLPVTVKTTL KSYQANSLVI TAGPWTNRLL HPLGIELPLQ TLRINVCYWR EKVPGSYGVS 

       250        260        270        280        290        300 
QAFPCILGLD LAPHHIYGLP ASEYPGLMKI CYHHGDNVDP EERDCPKTFS DIQDVQILCH 

       310        320        330        340        350        360 
FVRDHLPGLR AEPDIMERCM YTNTPDEHFI LDCHPKYDNI VIGAGFSGHG FKLAPVVGKI 

       370        380        390 
LYELSMKLPP SYDLAPFRMS RFSTLSKAHL 

« Hide

References

« Hide 'large scale' references
[1]"A mammalian homolog of the bacterial monomeric sarcosine oxidases maps to mouse chromosome 11, close to Cryba1."
Herbst R., Barton J.L., Nicklin M.J.H.
Genomics 46:480-482(1997) [PubMed: 9441754] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryo.
[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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Small intestine.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

U94700 mRNA. Translation: AAC39948.1.
AK008555 mRNA. Translation: BAB25741.1.
BC013525 mRNA. Translation: AAH13525.1.
IPIIPI00110719.
RefSeqNP_032978.2.
UniGeneMm.8543

3D structure databases

HSSPHSSP built from PDB template 1EL5 based on UniProtKB P40859.
ModBaseSearch...

Proteomic databases

PRIDEQ9D826.

Genome annotation databases

EnsemblENSMUSG00000017453. Mus musculus. [Contig view]
GeneID19193.
KEGGmmu:19193.

Organism-specific databases

MGIMGI:1197006. Pipox.

Phylogenomic databases

HOGENOMQ9D826.
HOVERGENQ9D826.
OMAQ9D826. ERDCPEA.

Enzyme and pathway databases

BRENDA1.5.3.1. 244.
1.5.3.7. 244.

Gene expression databases

ArrayExpressQ9D826.
BgeeQ9D826.
CleanExMM_PIPOX.
GermOnlineENSMUSG00000017453. Mus musculus.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR006281. SoxA_mon.
[Graphical view]
PfamPF01266. DAO. 1 hit.
[Graphical view]
TIGRFAMsTIGR01377. soxA_mon. 1 hit.
ProtoNetSearch...

Other Resources

NextBio295904.
SOURCESearch...

Entry information

Entry nameSOX_MOUSE
AccessionPrimary (citable) accession number: Q9D826
Secondary accession number(s): O55223
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: June 16, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents