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Cystathionine beta-synthase (EC 4.2.1.22) (Beta-thionase) (Serine sulfhydrase)

 CBS_MOUSE               Reviewed;         561 AA.
Q91WT9; Q91WU3;
28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 138.
RecName: Full=Cystathionine beta-synthase {ECO:0000305};
EC=4.2.1.22 {ECO:0000250|UniProtKB:P35520};
AltName: Full=Beta-thionase;
AltName: Full=Serine sulfhydrase;
Name=Cbs;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, Liver, Pancreas, and Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Hydro-lyase catalyzing the first step of the
transsulfuration pathway, where the hydroxyl group of L-serine is
displaced by L-homocysteine in a beta-replacement reaction to form
L-cystathionine, the precursor of L-cysteine. This catabolic route
allows the elimination of L-methionine and the toxic metabolite L-
homocysteine (By similarity). Also involved in the production of
hydrogen sulfide, a gasotransmitter with signaling and
cytoprotective effects on neurons (By similarity).
{ECO:0000250|UniProtKB:P32232, ECO:0000250|UniProtKB:P35520}.
-!- CATALYTIC ACTIVITY:
Reaction=L-homocysteine + L-serine = H2O + L,L-cystathionine;
Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22;
Evidence={ECO:0000250|UniProtKB:P35520};
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250|UniProtKB:P35520};
-!- ACTIVITY REGULATION: Allosterically activated by S-adenosyl-
methionine/AdoMet. Activated by S-adenosylhomocysteine/AdoHcy.
Binds non-covalently to a heme group that may control the redox
sensitivity of the enzyme. {ECO:0000250|UniProtKB:P35520}.
-!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
cysteine from L-homocysteine and L-serine: step 1/2.
{ECO:0000250|UniProtKB:P35520}.
-!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P35520}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P35520}.
Nucleus {ECO:0000250|UniProtKB:P35520}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q91WT9-1; Sequence=Displayed;
Name=2;
IsoId=Q91WT9-2; Sequence=VSP_021790;
-!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AK077669; BAC36943.1; -; mRNA.
EMBL; BC013472; AAH13472.1; -; mRNA.
EMBL; BC013480; AAH13480.1; -; mRNA.
EMBL; BC026595; AAH26595.1; -; mRNA.
CCDS; CCDS28609.1; -. [Q91WT9-1]
CCDS; CCDS28610.1; -. [Q91WT9-2]
RefSeq; NP_001258282.1; NM_001271353.1. [Q91WT9-2]
RefSeq; NP_659104.1; NM_144855.3. [Q91WT9-1]
RefSeq; NP_835742.1; NM_178224.3. [Q91WT9-2]
RefSeq; XP_006523612.1; XM_006523549.3. [Q91WT9-1]
RefSeq; XP_006523613.1; XM_006523550.3. [Q91WT9-1]
RefSeq; XP_006523614.1; XM_006523551.3. [Q91WT9-1]
UniGene; Mm.206417; -.
UniGene; Mm.486781; -.
ProteinModelPortal; Q91WT9; -.
SMR; Q91WT9; -.
DIP; DIP-60823N; -.
IntAct; Q91WT9; 2.
MINT; Q91WT9; -.
STRING; 10090.ENSMUSP00000066878; -.
iPTMnet; Q91WT9; -.
PhosphoSitePlus; Q91WT9; -.
SwissPalm; Q91WT9; -.
PaxDb; Q91WT9; -.
PeptideAtlas; Q91WT9; -.
PRIDE; Q91WT9; -.
Ensembl; ENSMUST00000067801; ENSMUSP00000066878; ENSMUSG00000024039. [Q91WT9-1]
Ensembl; ENSMUST00000078509; ENSMUSP00000077597; ENSMUSG00000024039. [Q91WT9-2]
Ensembl; ENSMUST00000118504; ENSMUSP00000113209; ENSMUSG00000024039. [Q91WT9-2]
GeneID; 12411; -.
KEGG; mmu:12411; -.
UCSC; uc008bvl.2; mouse. [Q91WT9-1]
UCSC; uc008bvm.2; mouse. [Q91WT9-2]
CTD; 875; -.
MGI; MGI:88285; Cbs.
eggNOG; KOG1252; Eukaryota.
eggNOG; COG0031; LUCA.
GeneTree; ENSGT00510000047027; -.
HOGENOM; HOG000217392; -.
HOVERGEN; HBG000918; -.
InParanoid; Q91WT9; -.
KO; K01697; -.
OMA; IGYRMVQ; -.
OrthoDB; EOG091G02TP; -.
PhylomeDB; Q91WT9; -.
TreeFam; TF300784; -.
BRENDA; 4.2.1.22; 3474.
Reactome; R-MMU-1614603; Cysteine formation from homocysteine.
UniPathway; UPA00136; UER00201.
ChiTaRS; Cbs; mouse.
PRO; PR:Q91WT9; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024039; Expressed in 193 organ(s), highest expression level in dorsal pancreas.
CleanEx; MM_CBS; -.
ExpressionAtlas; Q91WT9; baseline and differential.
Genevisible; Q91WT9; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0070025; F:carbon monoxide binding; ISO:MGI.
GO; GO:0004122; F:cystathionine beta-synthase activity; IMP:MGI.
GO; GO:0004124; F:cysteine synthase activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0020037; F:heme binding; ISO:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0072341; F:modified amino acid binding; ISO:MGI.
GO; GO:0070026; F:nitric oxide binding; ISO:MGI.
GO; GO:0050421; F:nitrite reductase (NO-forming) activity; ISO:MGI.
GO; GO:0019825; F:oxygen binding; ISO:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
GO; GO:1904047; F:S-adenosyl-L-methionine binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:MGI.
GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
GO; GO:0021587; P:cerebellum morphogenesis; IMP:MGI.
GO; GO:0019344; P:cysteine biosynthetic process; IMP:MGI.
GO; GO:0006535; P:cysteine biosynthetic process from serine; IBA:GO_Central.
GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:InterPro.
GO; GO:0001958; P:endochondral ossification; IMP:MGI.
GO; GO:0043418; P:homocysteine catabolic process; ISS:UniProtKB.
GO; GO:0050667; P:homocysteine metabolic process; IMP:MGI.
GO; GO:0070814; P:hydrogen sulfide biosynthetic process; ISS:UniProtKB.
GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
GO; GO:0060135; P:maternal process involved in female pregnancy; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0050880; P:regulation of blood vessel size; IMP:MGI.
GO; GO:0043506; P:regulation of JUN kinase activity; IMP:MGI.
GO; GO:0010749; P:regulation of nitric oxide mediated signal transduction; IMP:MGI.
GO; GO:0051593; P:response to folic acid; IMP:MGI.
GO; GO:0006801; P:superoxide metabolic process; IMP:MGI.
GO; GO:0019346; P:transsulfuration; ISO:MGI.
InterPro; IPR000644; CBS_dom.
InterPro; IPR005857; Cysta_beta_synth.
InterPro; IPR001216; P-phosphate_BS.
InterPro; IPR001926; PLP-dep.
InterPro; IPR036052; Trypto_synt_PLP_dependent.
Pfam; PF00571; CBS; 1.
Pfam; PF00291; PALP; 1.
SMART; SM00116; CBS; 1.
SUPFAM; SSF53686; SSF53686; 1.
TIGRFAMs; TIGR01137; cysta_beta; 1.
PROSITE; PS51371; CBS; 1.
PROSITE; PS00901; CYS_SYNTHASE; 1.
1: Evidence at protein level;
Alternative splicing; Amino-acid biosynthesis; CBS domain;
Complete proteome; Cysteine biosynthesis; Cytoplasm; Heme; Iron;
Isopeptide bond; Lyase; Metal-binding; Nucleus; Phosphoprotein;
Pyridoxal phosphate; Reference proteome; Ubl conjugation.
CHAIN 1 561 Cystathionine beta-synthase.
/FTId=PRO_0000262592.
DOMAIN 414 474 CBS. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
REGION 253 257 Pyridoxal phosphate binding.
{ECO:0000250|UniProtKB:P35520}.
METAL 49 49 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P35520}.
METAL 62 62 Iron (heme axial ligand).
{ECO:0000250|UniProtKB:P35520}.
BINDING 146 146 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P35520}.
BINDING 346 346 Pyridoxal phosphate.
{ECO:0000250|UniProtKB:P35520}.
MOD_RES 116 116 N6-(pyridoxal phosphate)lysine.
{ECO:0000250|UniProtKB:P35520}.
MOD_RES 196 196 Phosphoserine.
{ECO:0000250|UniProtKB:P35520}.
CROSSLNK 208 208 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:P35520}.
VAR_SEQ 514 528 SRDQAWSGVVGGPTD -> Y (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_021790.
SEQUENCE 561 AA; 61544 MW; 072CF81AFE10372E CRC64;
MPSGTSQCED GSAGGFQHLD MHSEKRQLEK GPSGDKDRVW IRPDTPSRCT WQLGRAMADS
PHYHTVLTKS PKILPDILRK IGNTPMVRIN KISKNAGLKC ELLAKCEFFN AGGSVKDRIS
LRMIEDAERA GNLKPGDTII EPTSGNTGIG LALAAAVKGY RCIIVMPEKM SMEKVDVLRA
LGAEIVRTPT NARFDSPESH VGVAWRLKNE IPNSHILDQY RNASNPLAHY DDTAEEILQQ
CDGKLDMLVA SAGTGGTITG IARKLKEKCP GCKIIGVDPE GSILAEPEEL NQTEQTAYEV
EGIGYDFIPT VLDRAVVDKW FKSNDEDSFA FARMLIAQEG LLCGGSSGSA MAVAVKAARE
LQEGQRCVVI LPDSVRNYMS KFLSDKWMLQ KGFMKEELSV KRPWWWRLRV QELSLSAPLT
VLPTVTCEDT IAILREKGFD QAPVVNESGA ILGMVTLGNM LSSLLAGKVR PSDEVCKVLY
KQFKPIHLTD TLGTLSHILE MDHFALVVHE QIQSRDQAWS GVVGGPTDCS NGMSSKQQMV
FGVVTAIDLL NFVAAREQTQ T


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