SOX_HUMAN
ID SOX_HUMAN Reviewed; 390 AA.
AC Q9P0Z9; B3KNH0; Q96H28; Q9C070;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Peroxisomal sarcosine oxidase;
DE Short=PSO;
DE EC=1.5.3.1 {ECO:0000269|PubMed:10642506};
DE EC=1.5.3.7 {ECO:0000269|PubMed:10642506};
DE AltName: Full=L-pipecolate oxidase;
DE AltName: Full=L-pipecolic acid oxidase;
GN Name=PIPOX; Synonyms=LPIPOX, PSO;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10772957; DOI=10.1006/bbrc.2000.2575;
RA Ijlst L., de Kromme I., Oostheim W., Wanders R.J.A.;
RT "Molecular cloning and expression of human L-pipecolate oxidase.";
RL Biochem. Biophys. Res. Commun. 270:1101-1105(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=10642506; DOI=10.1042/bj3450487;
RA Dodt G., Kim D.G., Reimann S.A., Reuber B.E., McCabe K., Gould S.J.,
RA Mihalik S.J.;
RT "L-pipecolic acid oxidase, a human enzyme essential for the degradation of
RT L-pipecolic acid, is most similar to the monomeric sarcosine oxidases.";
RL Biochem. J. 345:487-494(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Muscle;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Metabolizes sarcosine and L-pipecolic acid.
CC {ECO:0000269|PubMed:10642506}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O2 + sarcosine = formaldehyde + glycine + H2O2;
CC Xref=Rhea:RHEA:13313, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16240, ChEBI:CHEBI:16842, ChEBI:CHEBI:57305,
CC ChEBI:CHEBI:57433; EC=1.5.3.1;
CC Evidence={ECO:0000269|PubMed:10642506};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-pipecolate + O2 = H(+) + H2O2 + L-1-piperideine-6-
CC carboxylate; Xref=Rhea:RHEA:11992, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:58769,
CC ChEBI:CHEBI:61185; EC=1.5.3.7;
CC Evidence={ECO:0000269|PubMed:10642506};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9P0Z9; Q9NUX5: POT1; NbExp=2; IntAct=EBI-725582, EBI-752420;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:10642506}.
CC -!- TISSUE SPECIFICITY: Expressed in the liver and kidney.
CC {ECO:0000269|PubMed:10642506}.
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. {ECO:0000305}.
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DR EMBL; AF134593; AAF37331.1; -; mRNA.
DR EMBL; AF136970; AAG49431.1; -; mRNA.
DR EMBL; AK027498; BAG51332.1; -; mRNA.
DR EMBL; CH471159; EAW51169.1; -; Genomic_DNA.
DR EMBL; BC008960; AAH08960.1; -; mRNA.
DR CCDS; CCDS11248.1; -.
DR PIR; JC7256; JC7256.
DR RefSeq; NP_057602.2; NM_016518.2.
DR AlphaFoldDB; Q9P0Z9; -.
DR SMR; Q9P0Z9; -.
DR BioGRID; 119422; 14.
DR IntAct; Q9P0Z9; 8.
DR STRING; 9606.ENSP00000317721; -.
DR BindingDB; Q9P0Z9; -.
DR ChEMBL; CHEMBL2254; -.
DR DrugBank; DB00145; Glycine.
DR iPTMnet; Q9P0Z9; -.
DR PhosphoSitePlus; Q9P0Z9; -.
DR BioMuta; PIPOX; -.
DR DMDM; 54042061; -.
DR EPD; Q9P0Z9; -.
DR jPOST; Q9P0Z9; -.
DR MassIVE; Q9P0Z9; -.
DR MaxQB; Q9P0Z9; -.
DR PaxDb; Q9P0Z9; -.
DR PeptideAtlas; Q9P0Z9; -.
DR PRIDE; Q9P0Z9; -.
DR ProteomicsDB; 83626; -.
DR Antibodypedia; 2669; 117 antibodies from 24 providers.
DR DNASU; 51268; -.
DR Ensembl; ENST00000323372.9; ENSP00000317721.4; ENSG00000179761.12.
DR GeneID; 51268; -.
DR KEGG; hsa:51268; -.
DR MANE-Select; ENST00000323372.9; ENSP00000317721.4; NM_016518.3; NP_057602.2.
DR UCSC; uc002hdr.2; human.
DR CTD; 51268; -.
DR DisGeNET; 51268; -.
DR GeneCards; PIPOX; -.
DR HGNC; HGNC:17804; PIPOX.
DR HPA; ENSG00000179761; Group enriched (kidney, liver).
DR MIM; 616713; gene.
DR neXtProt; NX_Q9P0Z9; -.
DR OpenTargets; ENSG00000179761; -.
DR PharmGKB; PA33332; -.
DR VEuPathDB; HostDB:ENSG00000179761; -.
DR eggNOG; KOG2820; Eukaryota.
DR GeneTree; ENSGT00390000011000; -.
DR HOGENOM; CLU_007884_2_2_1; -.
DR InParanoid; Q9P0Z9; -.
DR OMA; EMYSDPV; -.
DR OrthoDB; 752680at2759; -.
DR PhylomeDB; Q9P0Z9; -.
DR TreeFam; TF313837; -.
DR BRENDA; 1.5.3.7; 2681.
DR PathwayCommons; Q9P0Z9; -.
DR Reactome; R-HSA-71064; Lysine catabolism.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR SignaLink; Q9P0Z9; -.
DR BioGRID-ORCS; 51268; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; PIPOX; human.
DR GenomeRNAi; 51268; -.
DR Pharos; Q9P0Z9; Tbio.
DR PRO; PR:Q9P0Z9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9P0Z9; protein.
DR Bgee; ENSG00000179761; Expressed in right lobe of liver and 146 other tissues.
DR ExpressionAtlas; Q9P0Z9; baseline and differential.
DR Genevisible; Q9P0Z9; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005782; C:peroxisomal matrix; TAS:Reactome.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050031; F:L-pipecolate oxidase activity; IDA:UniProtKB.
DR GO; GO:0008115; F:sarcosine oxidase activity; IDA:UniProtKB.
DR GO; GO:0033514; P:L-lysine catabolic process to acetyl-CoA via L-pipecolate; IDA:UniProtKB.
DR GO; GO:0006554; P:lysine catabolic process; TAS:Reactome.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR045170; MTOX.
DR InterPro; IPR006281; SoxA_mon.
DR PANTHER; PTHR10961; PTHR10961; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01377; soxA_mon; 1.
PE 1: Evidence at protein level;
KW Acetylation; FAD; Flavoprotein; Oxidoreductase; Peroxisome;
KW Reference proteome.
FT CHAIN 1..390
FT /note="Peroxisomal sarcosine oxidase"
FT /id="PRO_0000213773"
FT MOTIF 388..390
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT BINDING 9..39
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255"
FT MOD_RES 126
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9D826"
FT MOD_RES 319
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 376..390
FT /note="PFRISRFPSLGKAHL -> AFSNQPFPKPGQSPPLTSGQKPPFCAQEPVSQM
FT EKMSQMKGVSLRYHPFLLPRLNPP (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="G -> A (in Ref. 2; AAF37331)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 44066 MW; 581ADDA6F5D19C0F CRC64;
MAAQKDLWDA IVIGAGIQGC FTAYHLAKHR KRILLLEQFF LPHSRGSSHG QSRIIRKAYL
EDFYTRMMHE CYQIWAQLEH EAGTQLHRQT GLLLLGMKEN QELKTIQANL SRQRVEHQCL
SSEELKQRFP NIRLPRGEVG LLDNSGGVIY AYKALRALQD AIRQLGGIVR DGEKVVEINP
GLLVTVKTTS RSYQAKSLVI TAGPWTNQLL RPLGIEMPLQ TLRINVCYWR EMVPGSYGVS
QAFPCFLWLG LCPHHIYGLP TGEYPGLMKV SYHHGNHADP EERDCPTART DIGDVQILSS
FVRDHLPDLK PEPAVIESCM YTNTPDEQFI LDRHPKYDNI VIGAGFSGHG FKLAPVVGKI
LYELSMKLTP SYDLAPFRIS RFPSLGKAHL
