SOX_MOUSE
ID SOX_MOUSE Reviewed; 390 AA.
AC Q9D826; O55223;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Peroxisomal sarcosine oxidase;
DE Short=PSO;
DE EC=1.5.3.1;
DE EC=1.5.3.7;
DE AltName: Full=L-pipecolate oxidase;
DE AltName: Full=L-pipecolic acid oxidase;
GN Name=Pipox; Synonyms=Pso;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=9441754; DOI=10.1006/geno.1997.5050;
RA Herbst R., Barton J.L., Nicklin M.J.H.;
RT "A mammalian homolog of the bacterial monomeric sarcosine oxidases maps to
RT mouse chromosome 11, close to Cryba1.";
RL Genomics 46:480-482(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-126 AND LYS-287, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
CC -!- FUNCTION: Metabolizes sarcosine, L-pipecolic acid and L-proline.
CC {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Note=Binds 1 FAD per subunit.;
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Kidney and liver.
CC -!- SIMILARITY: Belongs to the MSOX/MTOX family. {ECO:0000305}.
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DR EMBL; U94700; AAC39948.1; -; mRNA.
DR EMBL; AK008555; BAB25741.1; -; mRNA.
DR EMBL; BC013525; AAH13525.1; -; mRNA.
DR CCDS; CCDS25086.1; -.
DR RefSeq; NP_032978.2; NM_008952.2.
DR AlphaFoldDB; Q9D826; -.
DR SMR; Q9D826; -.
DR STRING; 10090.ENSMUSP00000017597; -.
DR iPTMnet; Q9D826; -.
DR PhosphoSitePlus; Q9D826; -.
DR SwissPalm; Q9D826; -.
DR jPOST; Q9D826; -.
DR MaxQB; Q9D826; -.
DR PaxDb; Q9D826; -.
DR PRIDE; Q9D826; -.
DR ProteomicsDB; 257380; -.
DR Antibodypedia; 2669; 117 antibodies from 24 providers.
DR DNASU; 19193; -.
DR Ensembl; ENSMUST00000017597; ENSMUSP00000017597; ENSMUSG00000017453.
DR GeneID; 19193; -.
DR KEGG; mmu:19193; -.
DR UCSC; uc007khm.2; mouse.
DR CTD; 51268; -.
DR MGI; MGI:1197006; Pipox.
DR VEuPathDB; HostDB:ENSMUSG00000017453; -.
DR eggNOG; KOG2820; Eukaryota.
DR GeneTree; ENSGT00390000011000; -.
DR HOGENOM; CLU_007884_2_2_1; -.
DR InParanoid; Q9D826; -.
DR OMA; QEQPAHF; -.
DR OrthoDB; 752680at2759; -.
DR PhylomeDB; Q9D826; -.
DR TreeFam; TF313837; -.
DR Reactome; R-MMU-71064; Lysine catabolism.
DR Reactome; R-MMU-9033241; Peroxisomal protein import.
DR BioGRID-ORCS; 19193; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q9D826; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D826; protein.
DR Bgee; ENSMUSG00000017453; Expressed in right kidney and 104 other tissues.
DR ExpressionAtlas; Q9D826; baseline and differential.
DR Genevisible; Q9D826; MM.
DR GO; GO:0005777; C:peroxisome; IDA:HGNC-UCL.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0050031; F:L-pipecolate oxidase activity; ISS:UniProtKB.
DR GO; GO:0008115; F:sarcosine oxidase activity; ISS:UniProtKB.
DR GO; GO:0033514; P:L-lysine catabolic process to acetyl-CoA via L-pipecolate; ISS:UniProtKB.
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_0000213774"
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:0007744|PubMed:23576753"
FT MOD_RES 287
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 319
FT /note="S-8alpha-FAD cysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="Q -> H (in Ref. 1; AAC39948)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="C -> W (in Ref. 1; AAC39948)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="K -> T (in Ref. 1; AAC39948)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 390 AA; 43847 MW; 0C33A96A24731EE0 CRC64;
MAAQTDFWDA IVIGAGIQGC FTAYHLAKHS KSVLLLEQFF LPHSRGSSHG QSRIIRKAYP
EDFYTMMMKE CYQTWAQLER EAGTQLHRQT ELLLLGTKEN PGLKTIQATL SRQGIDHEYL
SSVDLKQRFP NIRFTRGEVG LLDKTGGVLY ADKALRALQH IICQLGGTVC DGEKVVEIRP
GLPVTVKTTL KSYQANSLVI TAGPWTNRLL HPLGIELPLQ TLRINVCYWR EKVPGSYGVS
QAFPCILGLD LAPHHIYGLP ASEYPGLMKI CYHHGDNVDP EERDCPKTFS DIQDVQILCH
FVRDHLPGLR AEPDIMERCM YTNTPDEHFI LDCHPKYDNI VIGAGFSGHG FKLAPVVGKI
LYELSMKLPP SYDLAPFRMS RFSTLSKAHL
