SCLY_MOUSE
ID SCLY_MOUSE Reviewed; 432 AA.
AC Q9JLI6; Q8CB57; Q8CB94;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=Selenocysteine lyase {ECO:0000303|PubMed:10692412};
DE Short=mSCL {ECO:0000303|PubMed:10692412};
DE EC=4.4.1.16 {ECO:0000269|PubMed:10692412};
GN Name=Scly; Synonyms=Scl;
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] (ISOFORM 1), PROTEIN SEQUENCE OF 1-10, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=10692412; DOI=10.1074/jbc.275.9.6195;
RA Mihara H., Kurihara T., Watanabe T., Yoshimura T., Esaki N.;
RT "cDNA cloning, purification, and characterization of mouse liver
RT selenocysteine lyase. Candidate for selenium delivery protein in
RT selenoprotein synthesis.";
RL J. Biol. Chem. 275:6195-6200(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone;
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] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
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).
CC -!- FUNCTION: Catalyzes the decomposition of L-selenocysteine to L-alanine
CC and elemental selenium. {ECO:0000269|PubMed:10692412}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + L-selenocysteine = A + H(+) + hydrogenselenide + L-
CC alanine; Xref=Rhea:RHEA:11632, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29317, ChEBI:CHEBI:57843,
CC ChEBI:CHEBI:57972; EC=4.4.1.16;
CC Evidence={ECO:0000269|PubMed:10692412};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:10692412};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.9 mM for L-selenocysteine {ECO:0000269|PubMed:10692412};
CC KM=8.6 mM for L-cysteine sulfinate {ECO:0000269|PubMed:10692412};
CC KM=5.2 mM for L-cysteine {ECO:0000269|PubMed:10692412};
CC Vmax=58 umol/min/mg enzyme with L-selenocysteine as substrate
CC {ECO:0000269|PubMed:10692412};
CC Vmax=0.45 umol/min/mg enzyme with L-cysteine sulfinate as substrate
CC {ECO:0000269|PubMed:10692412};
CC Vmax=0.0074 umol/min/mg enzyme with L-cysteine as substrate
CC {ECO:0000269|PubMed:10692412};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10692412}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10692412}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9JLI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9JLI6-2; Sequence=VSP_030855;
CC -!- TISSUE SPECIFICITY: Widely expressed. Present in liver, kidney, testis
CC (at protein level). {ECO:0000269|PubMed:10692412}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AF175407; AAF36812.1; -; mRNA.
DR EMBL; AK036533; BAC29465.1; -; mRNA.
DR EMBL; AK036750; BAC29563.1; -; mRNA.
DR EMBL; BC019879; AAH19879.1; -; mRNA.
DR EMBL; BC021389; AAH21389.1; -; mRNA.
DR CCDS; CCDS15159.1; -. [Q9JLI6-1]
DR RefSeq; NP_057926.2; NM_016717.3.
DR AlphaFoldDB; Q9JLI6; -.
DR SMR; Q9JLI6; -.
DR BioGRID; 206142; 10.
DR IntAct; Q9JLI6; 1.
DR STRING; 10090.ENSMUSP00000027532; -.
DR iPTMnet; Q9JLI6; -.
DR PhosphoSitePlus; Q9JLI6; -.
DR EPD; Q9JLI6; -.
DR jPOST; Q9JLI6; -.
DR MaxQB; Q9JLI6; -.
DR PaxDb; Q9JLI6; -.
DR PeptideAtlas; Q9JLI6; -.
DR PRIDE; Q9JLI6; -.
DR ProteomicsDB; 255359; -. [Q9JLI6-1]
DR ProteomicsDB; 255360; -. [Q9JLI6-2]
DR DNASU; 50880; -.
DR GeneID; 50880; -.
DR KEGG; mmu:50880; -.
DR UCSC; uc007cae.1; mouse. [Q9JLI6-1]
DR CTD; 51540; -.
DR MGI; MGI:1355310; Scly.
DR eggNOG; KOG1549; Eukaryota.
DR InParanoid; Q9JLI6; -.
DR OrthoDB; 697150at2759; -.
DR PhylomeDB; Q9JLI6; -.
DR TreeFam; TF313550; -.
DR BRENDA; 4.4.1.16; 3474.
DR Reactome; R-MMU-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
DR SABIO-RK; Q9JLI6; -.
DR BioGRID-ORCS; 50880; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Scly; mouse.
DR PRO; PR:Q9JLI6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9JLI6; protein.
DR GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016597; F:amino acid binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0009000; F:selenocysteine lyase activity; ISO:MGI.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0070279; F:vitamin B6 binding; ISO:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:1900408; P:negative regulation of cellular response to oxidative stress; IMP:MGI.
DR GO; GO:0032868; P:response to insulin; IMP:MGI.
DR GO; GO:0001887; P:selenium compound metabolic process; IMP:MGI.
DR GO; GO:0016261; P:selenocysteine catabolic process; ISO:MGI.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR000192; Aminotrans_V_dom.
DR InterPro; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00266; Aminotran_5; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Lyase; Phosphoprotein; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..432
FT /note="Selenocysteine lyase"
FT /id="PRO_0000317013"
FT ACT_SITE 375
FT /note="S-selanylcysteine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q68FT9"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96I15"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96I15"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:Q68FT9"
FT VAR_SEQ 284..432
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_030855"
FT CONFLICT 146
FT /note="N -> S (in Ref. 2; BAC29465)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="R -> W (in Ref. 2; BAC29465/BAC29563)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 432 AA; 47174 MW; AFC1800A1BC349D4 CRC64;
MDAARNGALG SVESLPDRKV YMDYNATTPL EPEVIQAVTE AMKEAWGNPS SSYVSGRKAK
DIINAARASL AKMIGGKPQD IIFTSGGTES NNLVIHSMVR CFHEQQTLKG NMVDQHSPEE
GTRPHFITCT VEHDSIRLPL EHLVENQMAE VTFVPVSKVN GQAEVEDILA AVRPTTCLVT
IMLANNETGV IMPVSEISRR IKALNQIRAA SGLPRVLVHT DAAQALGKRR VDVEDLGVDF
LTIVGHKFYG PRIGALYVRG VGKLTPLYPM LFGGGQERNF RPGTENTPMI AGLGKAADLV
SENCETYEAH MRDIRDYLEE RLEAEFGKRI HLNSRFPGVE RLPNTCNFSI QGSQLQGYTV
LAQCRTLLAS VGASCHSNHE DRPSPVLLSC GIPVDVARNA VRLSVGRGTT RADVDLIVQD
LKQAVAQLEG RL
