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Reviewed, UniProtKB/Swiss-Prot Q9P0Z9 (SOX_HUMAN)

Last modified June 16, 2009. Version 66. 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: LPIPOX, PSO
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

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.

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 Ref.2

Traceable author statement. Source: ProtInc

   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_0000213773

Regions

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

Amino acid modifications

Modified residue3191S-8alpha-FAD cysteine By similarity

Experimental info

Sequence conflict376 – 39015PFRIS…GKAHL → AFSNQPFPKPGQSPPLTSGQ KPPFCAQEPVSQMEKMSQMK GVSLRYHPFLLPRLNPP Ref.3
Sequence conflict3861G → A in AAF37331. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9P0Z9-1 [UniParc].

Last modified October 11, 2004. Version 2.
Checksum: 581ADDA6F5D19C0F

FASTA39044,066
        10         20         30         40         50         60 
MAAQKDLWDA IVIGAGIQGC FTAYHLAKHR KRILLLEQFF LPHSRGSSHG QSRIIRKAYL 

        70         80         90        100        110        120 
EDFYTRMMHE CYQIWAQLEH EAGTQLHRQT GLLLLGMKEN QELKTIQANL SRQRVEHQCL 

       130        140        150        160        170        180 
SSEELKQRFP NIRLPRGEVG LLDNSGGVIY AYKALRALQD AIRQLGGIVR DGEKVVEINP 

       190        200        210        220        230        240 
GLLVTVKTTS RSYQAKSLVI TAGPWTNQLL RPLGIEMPLQ TLRINVCYWR EMVPGSYGVS 

       250        260        270        280        290        300 
QAFPCFLWLG LCPHHIYGLP TGEYPGLMKV SYHHGNHADP EERDCPTART DIGDVQILSS 

       310        320        330        340        350        360 
FVRDHLPDLK PEPAVIESCM YTNTPDEQFI LDRHPKYDNI VIGAGFSGHG FKLAPVVGKI 

       370        380        390 
LYELSMKLTP SYDLAPFRIS RFPSLGKAHL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of human L-pipecolate oxidase."
Ijlst L., de Kromme I., Oostheim W., Wanders R.J.A.
Biochem. Biophys. Res. Commun. 270:1101-1105(2000) [PubMed: 10772957] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"L-pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases."
Dodt G., Kim D.G., Reimann S.A., Reuber B.E., McCabe K., Gould S.J., Mihalik S.J.
Biochem. J. 345:487-494(2000) [PubMed: 10642506] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Adrenal gland.
[4]"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: Muscle.

Cross-references

Sequence databases

AF134593 mRNA. Translation: AAF37331.1.
AF136970 mRNA. Translation: AAG49431.1.
BC008960 mRNA. Translation: AAH08960.1.
IPIIPI00554660.
PIRJC7256.
RefSeqNP_057602.2.
UniGeneHs.462585

3D structure databases

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

Protein-protein interaction databases

IntActQ9P0Z9. 1 interaction.

Proteomic databases

PRIDEQ9P0Z9.

Genome annotation databases

EnsemblENSG00000179761. Homo sapiens. [Contig view]
GeneID51268.
KEGGhsa:51268.

Organism-specific databases

GeneCardsGC17P024394.
H-InvDBHIX0019115.
HGNCHGNC:17804. PIPOX.
HPAHPA015567.
PharmGKBPA33332.
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ9P0Z9.
HOVERGENQ9P0Z9.
OMAQ9P0Z9. KTPSFDL.

Enzyme and pathway databases

BRENDA1.5.3.1. 247.
1.5.3.7. 247.

Gene expression databases

ArrayExpressQ9P0Z9.
BgeeQ9P0Z9.
CleanExHS_PIPOX.
GermOnlineENSG00000179761. Homo sapiens.

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

DrugBankDB00145. Glycine.
NextBio54463.

Entry information

Entry nameSOX_HUMAN
AccessionPrimary (citable) accession number: Q9P0Z9
Secondary accession number(s): Q96H28, Q9C070
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 11, 2004
Last modified: June 16, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

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