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Cystathionine beta-synthase (EC 4.2.1.22) (Beta-thionase) (Hemoprotein H-450) (Serine sulfhydrase)

 CBS_RAT                 Reviewed;         561 AA.
P32232;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
23-MAY-2018, entry version 163.
RecName: Full=Cystathionine beta-synthase {ECO:0000305};
EC=4.2.1.22 {ECO:0000250|UniProtKB:P35520};
AltName: Full=Beta-thionase;
AltName: Full=Hemoprotein H-450;
AltName: Full=Serine sulfhydrase;
Name=Cbs;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ALTERNATIVE
SPLICING (ISOFORMS I; II; III AND IV).
TISSUE=Liver;
PubMed=1597473;
Swaroop M., Bradley K., Ohura T., Tahara T., Roper M.D.,
Rosenberg L.E., Kraus J.P.;
"Rat cystathionine beta-synthase. Gene organization and alternative
splicing.";
J. Biol. Chem. 267:11455-11461(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-23 AND 39-48, AND
TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=2089036;
Ishihara S., Morohashi K., Sadano H., Kawabata S., Gotoh O., Omura T.;
"Molecular cloning and sequence analysis of cDNA coding for rat liver
hemoprotein H-450.";
J. Biochem. 108:899-902(1990).
[3]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=8558235;
Abe K., Kimura H.;
"The possible role of hydrogen sulfide as an endogenous
neuromodulator.";
J. Neurosci. 16:1066-1071(1996).
[4]
FUNCTION.
PubMed=20149843; DOI=10.1016/j.neuroscience.2010.02.006;
Tay A.S., Hu L.F., Lu M., Wong P.T., Bian J.S.;
"Hydrogen sulfide protects neurons against hypoxic injury via
stimulation of ATP-sensitive potassium channel/protein kinase
C/extracellular signal-regulated kinase/heat shock protein 90
pathway.";
Neuroscience 167:277-286(2010).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- 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 (PubMed:20149843,
PubMed:8558235). {ECO:0000250|UniProtKB:P35520,
ECO:0000269|PubMed:20149843, ECO:0000269|PubMed:8558235}.
-!- CATALYTIC ACTIVITY: L-serine + L-homocysteine = L-cystathionine +
H(2)O. {ECO:0000250|UniProtKB:P35520}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000250|UniProtKB:P35520};
-!- ENZYME 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=4;
Name=I;
IsoId=P32232-1; Sequence=Displayed;
Name=II;
IsoId=P32232-4; Sequence=Not described;
Name=III;
IsoId=P32232-2; Sequence=VSP_001218;
Name=IV;
IsoId=P32232-3; Sequence=VSP_001220, VSP_001221;
-!- TISSUE SPECIFICITY: Expressed in liver, kidney and brain. Highly
expressed in the hippocamus and cerebellum.
{ECO:0000269|PubMed:2089036, ECO:0000269|PubMed:8558235}.
-!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
synthase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; M88344; AAB02042.1; -; mRNA.
EMBL; M88346; AAA42024.1; -; mRNA.
EMBL; D01098; BAA00883.1; -; mRNA.
PIR; A42790; A42790.
PIR; C42790; C42790.
RefSeq; NP_036654.2; NM_012522.2. [P32232-2]
UniGene; Rn.87853; -.
ProteinModelPortal; P32232; -.
SMR; P32232; -.
STRING; 10116.ENSRNOP00000039968; -.
iPTMnet; P32232; -.
PhosphoSitePlus; P32232; -.
PaxDb; P32232; -.
PRIDE; P32232; -.
Ensembl; ENSRNOT00000042432; ENSRNOP00000039968; ENSRNOG00000029528. [P32232-1]
Ensembl; ENSRNOT00000045275; ENSRNOP00000042958; ENSRNOG00000029528. [P32232-2]
GeneID; 24250; -.
KEGG; rno:24250; -.
UCSC; RGD:2287; rat. [P32232-1]
CTD; 875; -.
RGD; 2287; Cbs.
eggNOG; KOG1252; Eukaryota.
eggNOG; COG0031; LUCA.
GeneTree; ENSGT00510000047027; -.
HOGENOM; HOG000217392; -.
HOVERGEN; HBG000918; -.
InParanoid; P32232; -.
KO; K01697; -.
OMA; SYLSKFA; -.
OrthoDB; EOG091G02TP; -.
PhylomeDB; P32232; -.
BioCyc; MetaCyc:MONOMER-8583; -.
Reactome; R-RNO-1614603; Cysteine formation from homocysteine.
SABIO-RK; P32232; -.
UniPathway; UPA00136; UER00201.
PRO; PR:P32232; -.
Proteomes; UP000002494; Chromosome 20.
Bgee; ENSRNOG00000029528; -.
Genevisible; P32232; RN.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0004122; F:cystathionine beta-synthase activity; IDA:RGD.
GO; GO:0020037; F:heme binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
GO; GO:0098605; F:selenocystathionine beta-synthase activity; TAS:Reactome.
GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0021587; P:cerebellum morphogenesis; IEA:Ensembl.
GO; GO:0006535; P:cysteine biosynthetic process from serine; TAS:RGD.
GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:InterPro.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0043418; P:homocysteine catabolic process; ISS:UniProtKB.
GO; GO:0050667; P:homocysteine metabolic process; IDA:RGD.
GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IDA:UniProtKB.
GO; GO:0006563; P:L-serine metabolic process; ISS:UniProtKB.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0050880; P:regulation of blood vessel size; IEA:Ensembl.
GO; GO:0030823; P:regulation of cGMP metabolic process; IEA:Ensembl.
GO; GO:0043506; P:regulation of JUN kinase activity; IEA:Ensembl.
GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
GO; GO:0006801; P:superoxide metabolic process; IEA:Ensembl.
GO; GO:0019346; P:transsulfuration; IDA:RGD.
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;
Direct protein sequencing; Heme; Iron; Isopeptide bond; Lyase;
Metal-binding; Nucleus; Phosphoprotein; Pyridoxal phosphate;
Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:2089036}.
CHAIN 2 561 Cystathionine beta-synthase.
/FTId=PRO_0000167134.
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 42 42 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
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 450 478 AILGMVTLGNMLSSLLAGKVRPSDEVCKV -> LRQSKDIC
HPTKRHIIQAHGLRKVPDTEA (in isoform IV).
{ECO:0000305}.
/FTId=VSP_001220.
VAR_SEQ 479 561 Missing (in isoform IV). {ECO:0000305}.
/FTId=VSP_001221.
VAR_SEQ 514 528 SRDQAWSGVVGGPTD -> Y (in isoform III).
{ECO:0000305}.
/FTId=VSP_001218.
CONFLICT 415 415 L -> P (in Ref. 2; BAA00883).
{ECO:0000305}.
SEQUENCE 561 AA; 61455 MW; 0199FCAF492AE3A2 CRC64;
MPSGTSQCED GSAGCPQDLE VQPEKGQLEK GASGDKERVW ISPDTPSRCT WQLGRPMADS
PHYHTVPTKS PKILPDILRK IGNTPMVRIN RISKNAGLKC ELLAKCEFFN AGGSVKDRIS
LRMIEDAERA GTLKPGDTII EPTSGNTGIG LALAAAVKGY RCIIVMPEKM SMEKVDVLRA
LGAEIVRTPT NARFDSPESH VGVAWRLKNE IPNSHILDQY RNASNPLAHY DDTAEEILQQ
CDGKVDMLVA SAGTGGTITG IARKLKEKCP GCKIIGVDPE GSILAEPEEL NQTEQTAYEV
EGIGYDFIPT VLDRAVVDRW FKSNDDDSFA FARMLISQEG LLCGGSSGSA MAVAVKAAQE
LKEGQRCVVI LPDSVRNYMS KFLSDKWMLQ KGFMKEELSV KRPWWWHLRV QELSLSAPLT
VLPTVTCEHT IAILREKGFD QAPVVNESGA ILGMVTLGNM LSSLLAGKVR PSDEVCKVLY
KQFKPIHLTD TLGMLSHILE MDHFALVVHE QIQSRDQAWS GVVGGPTDRN NGVSSKQLMV
FGVVTAIDLL NFVAAREQTR K


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