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Protein

Serine racemase

Gene

Srr

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.5 Publications

Catalytic activityi

L-serine = D-serine.
L-serine = pyruvate + NH3.
D-serine = pyruvate + NH3.

Cofactori

pyridoxal 5'-phosphate2 Publications

Enzyme regulationi

Allosterically activated by magnesium, and possibly also other divalent metal cations. Allosterically activated by ATP, ADP or GTP.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei51 – 511ATPCurated
Active sitei56 – 561Proton acceptorBy similarity
Active sitei84 – 841Proton acceptorBy similarity
Binding sitei121 – 1211ATPBy similarity
Binding sitei135 – 1351SubstrateBy similarity
Metal bindingi210 – 2101MagnesiumBy similarity
Metal bindingi214 – 2141Magnesium; via carbonyl oxygenBy similarity
Metal bindingi216 – 2161MagnesiumBy similarity

GO - Molecular functioni

  1. ATP binding Source: MGI
  2. calcium ion binding Source: MGI
  3. D-serine ammonia-lyase activity Source: GO_Central
  4. glycine binding Source: MGI
  5. L-serine ammonia-lyase activity Source: MGI
  6. magnesium ion binding Source: MGI
  7. PDZ domain binding Source: MGI
  8. protein homodimerization activity Source: MGI
  9. pyridoxal phosphate binding Source: MGI
  10. serine racemase activity Source: MGI
  11. threonine racemase activity Source: MGI

GO - Biological processi

  1. aging Source: Ensembl
  2. brain development Source: GO_Central
  3. D-serine biosynthetic process Source: MGI
  4. D-serine metabolic process Source: MGI
  5. L-serine metabolic process Source: MGI
  6. protein homotetramerization Source: MGI
  7. pyruvate biosynthetic process Source: MGI
  8. response to drug Source: Ensembl
  9. response to lipopolysaccharide Source: Ensembl
  10. response to morphine Source: Ensembl
  11. serine family amino acid metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Lyase

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding, Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi5.1.1.18. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine racemase (EC:4.3.1.17, EC:4.3.1.18, EC:5.1.1.18)
Alternative name(s):
D-serine ammonia-lyase
D-serine dehydratase
L-serine ammonia-lyase
L-serine dehydratase
Gene namesi
Name:Srr
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1351636. Srr.

Subcellular locationi

GO - Cellular componenti

  1. apical part of cell Source: Ensembl
  2. cytoplasm Source: MGI
  3. neuronal cell body Source: MGI
  4. plasma membrane Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi51 – 511K → A: Impairs ATP-binding inducing a 80% decrease in enzyme activity.
Mutagenesisi113 – 1131C → S: Abolishes S-nitrosylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 339339Serine racemasePRO_0000185651Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei56 – 561N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei113 – 1131S-nitrosocysteine1 Publication

Post-translational modificationi

S-nitrosylated, leading to decrease the enzyme activity.1 Publication

Keywords - PTMi

S-nitrosylation

Proteomic databases

MaxQBiQ9QZX7.
PaxDbiQ9QZX7.
PRIDEiQ9QZX7.

PTM databases

PhosphoSiteiQ9QZX7.

Expressioni

Tissue specificityi

Detected in brain (at protein level). Brain.

Gene expression databases

BgeeiQ9QZX7.
CleanExiMM_SRR.
ExpressionAtlasiQ9QZX7. baseline and differential.
GenevestigatoriQ9QZX7.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi205172. 4 interactions.
IntActiQ9QZX7. 2 interactions.
MINTiMINT-5202279.

Structurei

3D structure databases

ProteinModelPortaliQ9QZX7.
SMRiQ9QZX7. Positions 3-324.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni238 – 2392Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1171.
GeneTreeiENSGT00550000075026.
HOVERGENiHBG023167.
InParanoidiQ9QZX7.
KOiK12235.
OMAiWKEEYLT.
OrthoDBiEOG7HB5B2.
PhylomeDBiQ9QZX7.
TreeFamiTF313346.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9QZX7-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MCAQYCISFA DVEKAHINIQ DSIHLTPVLT SSILNQIAGR NLFFKCELFQ
60 70 80 90 100
KTGSFKIRGA LNAIRGLIPD TPEEKPKAVV THSSGNHGQA LTYAAKLEGI
110 120 130 140 150
PAYIVVPQTA PNCKKLAIQA YGASIVYCDP SDESREKVTQ RIMQETEGIL
160 170 180 190 200
VHPNQEPAVI AGQGTIALEV LNQVPLVDAL VVPVGGGGMV AGIAITIKAL
210 220 230 240 250
KPSVKVYAAE PSNADDCYQS KLKGELTPNL HPPETIADGV KSSIGLNTWP
260 270 280 290 300
IIRDLVDDVF TVTEDEIKYA TQLVWGRMKL LIEPTAGVAL AAVLSQHFQT
310 320 330
VSPEVKNVCI VLSGGNVDLT SLNWVGQAER PAPYQTVSV
Length:339
Mass (Da):36,359
Last modified:May 1, 2000 - v1
Checksum:iB9AE9A9336358728
GO
Isoform 2 (identifier: Q9QZX7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     174-198: Missing.

Show »
Length:314
Mass (Da):34,030
Checksum:i0BB6492649FF8491
GO
Isoform 3 (identifier: Q9QZX7-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     183-339: Missing.

Note: No experimental confirmation available.

Show »
Length:182
Mass (Da):19,694
Checksum:i23075946C01AF288
GO

Sequence cautioni

The sequence CAI24255.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111P → T in BAC25712. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei174 – 19825Missing in isoform 2. 1 PublicationVSP_025013Add
BLAST
Alternative sequencei183 – 339157Missing in isoform 3. CuratedVSP_025014Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148321 mRNA. Translation: AAF08701.1.
AK031687 mRNA. Translation: BAC27514.1.
AK028034 mRNA. Translation: BAC25712.1.
AK043738 mRNA. Translation: BAC31637.1.
AK157122 mRNA. Translation: BAE33968.1.
AK170096 mRNA. Translation: BAE41561.1.
AL604066 Genomic DNA. Translation: CAI24252.1.
AL604066 Genomic DNA. Translation: CAI24253.1.
AL604066 Genomic DNA. Translation: CAI24254.1.
AL604066 Genomic DNA. Translation: CAI24255.1. Sequence problems.
BC011164 mRNA. Translation: AAH11164.1.
AB232340 mRNA. Translation: BAE19920.1.
AB232341 mRNA. Translation: BAE19921.1.
AB232342 mRNA. Translation: BAE19922.1.
AB232343 mRNA. Translation: BAE19923.1.
AB235396 mRNA. Translation: BAE44529.1.
CCDSiCCDS25038.1. [Q9QZX7-1]
RefSeqiNP_001156783.1. NM_001163311.1. [Q9QZX7-1]
NP_038789.1. NM_013761.4. [Q9QZX7-1]
XP_006533520.1. XM_006533457.1. [Q9QZX7-1]
XP_006533521.1. XM_006533458.1. [Q9QZX7-1]
UniGeneiMm.131443.
Mm.220843.
Mm.412219.

Genome annotation databases

EnsembliENSMUST00000065211; ENSMUSP00000067552; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000108447; ENSMUSP00000104086; ENSMUSG00000001323. [Q9QZX7-2]
ENSMUST00000108448; ENSMUSP00000104087; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000121738; ENSMUSP00000113372; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000128556; ENSMUSP00000120012; ENSMUSG00000001323. [Q9QZX7-3]
GeneIDi27364.
KEGGimmu:27364.
UCSCiuc007kcr.2. mouse. [Q9QZX7-1]
uc007kcu.2. mouse. [Q9QZX7-3]
uc011xzd.1. mouse. [Q9QZX7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF148321 mRNA. Translation: AAF08701.1.
AK031687 mRNA. Translation: BAC27514.1.
AK028034 mRNA. Translation: BAC25712.1.
AK043738 mRNA. Translation: BAC31637.1.
AK157122 mRNA. Translation: BAE33968.1.
AK170096 mRNA. Translation: BAE41561.1.
AL604066 Genomic DNA. Translation: CAI24252.1.
AL604066 Genomic DNA. Translation: CAI24253.1.
AL604066 Genomic DNA. Translation: CAI24254.1.
AL604066 Genomic DNA. Translation: CAI24255.1. Sequence problems.
BC011164 mRNA. Translation: AAH11164.1.
AB232340 mRNA. Translation: BAE19920.1.
AB232341 mRNA. Translation: BAE19921.1.
AB232342 mRNA. Translation: BAE19922.1.
AB232343 mRNA. Translation: BAE19923.1.
AB235396 mRNA. Translation: BAE44529.1.
CCDSiCCDS25038.1. [Q9QZX7-1]
RefSeqiNP_001156783.1. NM_001163311.1. [Q9QZX7-1]
NP_038789.1. NM_013761.4. [Q9QZX7-1]
XP_006533520.1. XM_006533457.1. [Q9QZX7-1]
XP_006533521.1. XM_006533458.1. [Q9QZX7-1]
UniGeneiMm.131443.
Mm.220843.
Mm.412219.

3D structure databases

ProteinModelPortaliQ9QZX7.
SMRiQ9QZX7. Positions 3-324.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205172. 4 interactions.
IntActiQ9QZX7. 2 interactions.
MINTiMINT-5202279.

Chemistry

BindingDBiQ9QZX7.
ChEMBLiCHEMBL1075306.

PTM databases

PhosphoSiteiQ9QZX7.

Proteomic databases

MaxQBiQ9QZX7.
PaxDbiQ9QZX7.
PRIDEiQ9QZX7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065211; ENSMUSP00000067552; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000108447; ENSMUSP00000104086; ENSMUSG00000001323. [Q9QZX7-2]
ENSMUST00000108448; ENSMUSP00000104087; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000121738; ENSMUSP00000113372; ENSMUSG00000001323. [Q9QZX7-1]
ENSMUST00000128556; ENSMUSP00000120012; ENSMUSG00000001323. [Q9QZX7-3]
GeneIDi27364.
KEGGimmu:27364.
UCSCiuc007kcr.2. mouse. [Q9QZX7-1]
uc007kcu.2. mouse. [Q9QZX7-3]
uc011xzd.1. mouse. [Q9QZX7-2]

Organism-specific databases

CTDi63826.
MGIiMGI:1351636. Srr.

Phylogenomic databases

eggNOGiCOG1171.
GeneTreeiENSGT00550000075026.
HOVERGENiHBG023167.
InParanoidiQ9QZX7.
KOiK12235.
OMAiWKEEYLT.
OrthoDBiEOG7HB5B2.
PhylomeDBiQ9QZX7.
TreeFamiTF313346.

Enzyme and pathway databases

BRENDAi5.1.1.18. 3474.

Miscellaneous databases

NextBioi305244.
PROiQ9QZX7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZX7.
CleanExiMM_SRR.
ExpressionAtlasiQ9QZX7. baseline and differential.
GenevestigatoriQ9QZX7.

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. TrpB-like_PLP-dep.
[Graphical view]
PfamiPF00291. PALP. 1 hit.
[Graphical view]
SUPFAMiSSF53686. SSF53686. 1 hit.
PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Serine racemase: a glial enzyme synthesizing D-serine to regulate glutamate-N-methyl-D-aspartate neurotransmission."
    Wolosker H., Blackshaw S., Snyder S.H.
    Proc. Natl. Acad. Sci. U.S.A. 96:13409-13414(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
    Strain: BALB/c.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J and NOD.
    Tissue: Brain cortex, Spleen and Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Liver.
  5. "Multiple splice variants in 5'UTR of mouse serine racemase."
    Ohba H., Ohnishi T., Yoshikawa T.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-56 (ISOFORMS 1/2/3).
    Tissue: Brain.
  6. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 15-40, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  7. "Allosteric regulation of mouse brain serine racemase."
    Neidle A., Dunlop D.S.
    Neurochem. Res. 27:1719-1724(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ENZYME REGULATION.
  8. "Cofactors of serine racemase that physiologically stimulate the synthesis of the N-methyl-D-aspartate (NMDA) receptor coagonist D-serine."
    De Miranda J., Panizzutti R., Foltyn V.N., Wolosker H.
    Proc. Natl. Acad. Sci. U.S.A. 99:14542-14547(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION.
  9. "Serine racemase modulates intracellular D-serine levels through an alpha,beta-elimination activity."
    Foltyn V.N., Bendikov I., De Miranda J., Panizzutti R., Dumin E., Shleper M., Li P., Toney M.D., Kartvelishvily E., Wolosker H.
    J. Biol. Chem. 280:1754-1763(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY.
  10. "Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition of D-serine formation."
    Mustafa A.K., Kumar M., Selvakumar B., Ho G.P., Ehmsen J.T., Barrow R.K., Amzel L.M., Snyder S.H.
    Proc. Natl. Acad. Sci. U.S.A. 104:2950-2955(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, S-NITROSYLATION AT CYS-113, ATP-BINDING, MUTAGENESIS OF CYS-113.

Entry informationi

Entry nameiSRR_MOUSE
AccessioniPrimary (citable) accession number: Q9QZX7
Secondary accession number(s): Q401M7
, Q5SWE4, Q5SWE5, Q5SWE7, Q8BT19, Q8CD11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: May 1, 2000
Last modified: February 4, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.