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Protein

Peroxisomal sarcosine oxidase

Gene

PIPOX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Sarcosine + H2O + O2 = glycine + formaldehyde + H2O2.
L-pipecolate + O2 = (S)-2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2.

Cofactori

FADNote: Binds 1 FAD per subunit.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi9 – 3931FADSequence analysisAdd
BLAST

GO - Molecular functioni

  • L-pipecolate oxidase activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • sarcosine oxidase activity Source: UniProtKB

GO - Biological processi

  • L-lysine catabolic process to acetyl-CoA via L-pipecolate Source: UniProtKB
  • lysine catabolic process Source: Reactome
  • oxidation-reduction process Source: UniProtKB
  • tetrahydrofolate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-HSA-71064. Lysine catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Peroxisomal sarcosine oxidase (EC:1.5.3.1, EC:1.5.3.7)
Short name:
PSO
Alternative name(s):
L-pipecolate oxidase
L-pipecolic acid oxidase
Gene namesi
Name:PIPOX
Synonyms:LPIPOX, PSO
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:17804. PIPOX.

Subcellular locationi

GO - Cellular componenti

  • peroxisomal matrix Source: Reactome
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33332.

Chemistry

ChEMBLiCHEMBL2254.
DrugBankiDB00145. Glycine.

Polymorphism and mutation databases

BioMutaiPIPOX.
DMDMi54042061.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 390390Peroxisomal sarcosine oxidasePRO_0000213773Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei126 – 1261N6-acetyllysineBy similarity
Modified residuei319 – 3191S-8alpha-FAD cysteineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9P0Z9.
PaxDbiQ9P0Z9.
PRIDEiQ9P0Z9.

PTM databases

iPTMnetiQ9P0Z9.
PhosphoSiteiQ9P0Z9.

Expressioni

Gene expression databases

BgeeiQ9P0Z9.
CleanExiHS_PIPOX.
ExpressionAtlasiQ9P0Z9. baseline and differential.
GenevisibleiQ9P0Z9. HS.

Organism-specific databases

HPAiHPA015567.

Interactioni

Subunit structurei

Monomer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
POT1Q9NUX52EBI-725582,EBI-752420

GO - Molecular functioni

  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi119422. 8 interactions.
IntActiQ9P0Z9. 2 interactions.
STRINGi9606.ENSP00000317721.

Chemistry

BindingDBiQ9P0Z9.

Structurei

3D structure databases

ProteinModelPortaliQ9P0Z9.
SMRiQ9P0Z9. Positions 6-385.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi388 – 3903Microbody targeting signalSequence analysis

Sequence similaritiesi

Belongs to the MSOX/MTOX family.Curated

Phylogenomic databases

eggNOGiKOG2820. Eukaryota.
COG0665. LUCA.
GeneTreeiENSGT00390000011000.
HOGENOMiHOG000236097.
HOVERGENiHBG023161.
InParanoidiQ9P0Z9.
KOiK00306.
OMAiIYAYKAL.
OrthoDBiEOG71RXJP.
PhylomeDBiQ9P0Z9.
TreeFamiTF313837.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR006281. SoxA_mon.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR01377. soxA_mon. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9P0Z9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQKDLWDA IVIGAGIQGC FTAYHLAKHR KRILLLEQFF LPHSRGSSHG
60 70 80 90 100
QSRIIRKAYL EDFYTRMMHE CYQIWAQLEH EAGTQLHRQT GLLLLGMKEN
110 120 130 140 150
QELKTIQANL SRQRVEHQCL SSEELKQRFP NIRLPRGEVG LLDNSGGVIY
160 170 180 190 200
AYKALRALQD AIRQLGGIVR DGEKVVEINP GLLVTVKTTS RSYQAKSLVI
210 220 230 240 250
TAGPWTNQLL RPLGIEMPLQ TLRINVCYWR EMVPGSYGVS QAFPCFLWLG
260 270 280 290 300
LCPHHIYGLP TGEYPGLMKV SYHHGNHADP EERDCPTART DIGDVQILSS
310 320 330 340 350
FVRDHLPDLK PEPAVIESCM YTNTPDEQFI LDRHPKYDNI VIGAGFSGHG
360 370 380 390
FKLAPVVGKI LYELSMKLTP SYDLAPFRIS RFPSLGKAHL
Length:390
Mass (Da):44,066
Last modified:October 11, 2004 - v2
Checksum:i581ADDA6F5D19C0F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti376 – 39015PFRIS…GKAHL → AFSNQPFPKPGQSPPLTSGQ KPPFCAQEPVSQMEKMSQMK GVSLRYHPFLLPRLNPP (PubMed:10931946).CuratedAdd
BLAST
Sequence conflicti386 – 3861G → A in AAF37331 (PubMed:10642506).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11248.1.
PIRiJC7256.
RefSeqiNP_057602.2. NM_016518.2.
UniGeneiHs.462585.

Genome annotation databases

EnsembliENST00000323372; ENSP00000317721; ENSG00000179761.
GeneIDi51268.
KEGGihsa:51268.
UCSCiuc002hdr.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11248.1.
PIRiJC7256.
RefSeqiNP_057602.2. NM_016518.2.
UniGeneiHs.462585.

3D structure databases

ProteinModelPortaliQ9P0Z9.
SMRiQ9P0Z9. Positions 6-385.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119422. 8 interactions.
IntActiQ9P0Z9. 2 interactions.
STRINGi9606.ENSP00000317721.

Chemistry

BindingDBiQ9P0Z9.
ChEMBLiCHEMBL2254.
DrugBankiDB00145. Glycine.

PTM databases

iPTMnetiQ9P0Z9.
PhosphoSiteiQ9P0Z9.

Polymorphism and mutation databases

BioMutaiPIPOX.
DMDMi54042061.

Proteomic databases

MaxQBiQ9P0Z9.
PaxDbiQ9P0Z9.
PRIDEiQ9P0Z9.

Protocols and materials databases

DNASUi51268.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000323372; ENSP00000317721; ENSG00000179761.
GeneIDi51268.
KEGGihsa:51268.
UCSCiuc002hdr.2. human.

Organism-specific databases

CTDi51268.
GeneCardsiPIPOX.
HGNCiHGNC:17804. PIPOX.
HPAiHPA015567.
MIMi616713. gene.
neXtProtiNX_Q9P0Z9.
PharmGKBiPA33332.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2820. Eukaryota.
COG0665. LUCA.
GeneTreeiENSGT00390000011000.
HOGENOMiHOG000236097.
HOVERGENiHBG023161.
InParanoidiQ9P0Z9.
KOiK00306.
OMAiIYAYKAL.
OrthoDBiEOG71RXJP.
PhylomeDBiQ9P0Z9.
TreeFamiTF313837.

Enzyme and pathway databases

ReactomeiR-HSA-71064. Lysine catabolism.

Miscellaneous databases

ChiTaRSiPIPOX. human.
GenomeRNAii51268.
PROiQ9P0Z9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9P0Z9.
CleanExiHS_PIPOX.
ExpressionAtlasiQ9P0Z9. baseline and differential.
GenevisibleiQ9P0Z9. HS.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR006076. FAD-dep_OxRdtase.
IPR023753. FAD/NAD-binding_dom.
IPR006281. SoxA_mon.
[Graphical view]
PfamiPF01266. DAO. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 2 hits.
TIGRFAMsiTIGR01377. soxA_mon. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. 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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiSOX_HUMAN
AccessioniPrimary (citable) accession number: Q9P0Z9
Secondary accession number(s): B3KNH0, Q96H28, Q9C070
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 11, 2004
Last modified: June 8, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.