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Q9P0Z9 (SOX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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.
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 = (S)-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
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processtetrahydrofolate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 [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]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF134593 mRNA. Translation: AAF37331.1.
AF136970 mRNA. Translation: AAG49431.1.
AK027498 mRNA. Translation: BAG51332.1.
CH471159 Genomic DNA. Translation: EAW51169.1.
BC008960 mRNA. Translation: AAH08960.1.
IPIIPI00554660.
PIRJC7256.
RefSeqNP_057602.2. NM_016518.2.
UniGeneHs.462585.

3D structure databases

ProteinModelPortalQ9P0Z9.
SMRQ9P0Z9. Positions 6-384.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9P0Z9. 1 interaction.
STRINGQ9P0Z9.

Polymorphism databases

DMDM54042061.

Proteomic databases

PRIDEQ9P0Z9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000323372; ENSP00000317721; ENSG00000179761.
GeneID51268.
KEGGhsa:51268.
UCSCuc002hdr.1. human.

Organism-specific databases

CTD51268.
GeneCardsGC17P027369.
H-InvDBHIX0019115.
HGNCHGNC:17804. PIPOX.
HPAHPA015567.
neXtProtNX_Q9P0Z9.
PharmGKBPA33332.
GenAtlasSearch...

Phylogenomic databases

GeneTreeENSGT00390000011000.
HOGENOMHBG589227.
HOVERGENHBG023161.
InParanoidQ9P0Z9.
OMAKTPSFDL.
OrthoDBEOG4GQQ50.
PhylomeDBQ9P0Z9.

Gene expression databases

ArrayExpressQ9P0Z9.
BgeeQ9P0Z9.
CleanExHS_PIPOX.
GenevestigatorQ9P0Z9.
GermOnlineENSG00000179761. Homo sapiens.

Family and domain databases

InterProIPR006076. FAD-dep_OxRdtase.
IPR006281. SoxA_mon.
[Graphical view]
KOK00306.
PfamPF01266. DAO. 1 hit.
[Graphical view]
TIGRFAMsTIGR01377. SoxA_mon. 1 hit.
ProtoNetSearch...

Other

DrugBankDB00145. Glycine.
NextBio54463.

Entry information

Entry nameSOX_HUMAN
AccessionPrimary (citable) accession number: Q9P0Z9
Secondary accession number(s): B3KNH0, Q96H28, Q9C070
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 11, 2004
Last modified: January 25, 2012
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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Index of protein domains and families