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Q9QZX7

- SRR_MOUSE

UniProt

Q9QZX7 - SRR_MOUSE

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Protein

Serine racemase

Gene
Srr
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.4 Publications
L-serine = pyruvate + NH3.4 Publications
D-serine = pyruvate + NH3.4 Publications

Cofactori

Pyridoxal phosphate.2 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 – 511ATP Inferred
Active sitei56 – 561Proton acceptor By similarity
Active sitei84 – 841Proton acceptor By similarity
Binding sitei121 – 1211ATP By similarity
Binding sitei135 – 1351Substrate By similarity
Metal bindingi210 – 2101Magnesium By similarity
Metal bindingi214 – 2141Magnesium; via carbonyl oxygen By similarity
Metal bindingi216 – 2161Magnesium By similarity

GO - Molecular functioni

  1. ATP binding Source: MGI
  2. calcium ion binding Source: MGI
  3. D-serine ammonia-lyase activity Source: UniProtKB-EC
  4. glycine binding Source: MGI
  5. L-serine ammonia-lyase activity Source: UniProtKB-EC
  6. magnesium ion binding Source: Ensembl
  7. protein 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: Ensembl
  3. D-serine biosynthetic process Source: MGI
  4. L-serine metabolic process Source: MGI
  5. protein homotetramerization Source: MGI
  6. pyruvate biosynthetic process Source: Ensembl
  7. response to drug Source: Ensembl
  8. response to lipopolysaccharide Source: Ensembl
  9. response to morphine Source: Ensembl
  10. 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: Ensembl
  3. neuronal cell body Source: Ensembl
  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)lysine By similarity
Modified residuei113 – 1131S-nitrosocysteine1 Publication

Post-translational modificationi

S-nitrosylated, leading to decrease the enzyme activity.

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

ArrayExpressiQ9QZX7.
BgeeiQ9QZX7.
CleanExiMM_SRR.
GenevestigatoriQ9QZX7.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi205172. 3 interactions.
IntActiQ9QZX7. 2 interactions.
MINTiMINT-5202279.

Structurei

3D structure databases

ProteinModelPortaliQ9QZX7.
SMRiQ9QZX7. Positions 3-324.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

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

Family and domain databases

InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[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

MCAQYCISFA DVEKAHINIQ DSIHLTPVLT SSILNQIAGR NLFFKCELFQ    50
KTGSFKIRGA LNAIRGLIPD TPEEKPKAVV THSSGNHGQA LTYAAKLEGI 100
PAYIVVPQTA PNCKKLAIQA YGASIVYCDP SDESREKVTQ RIMQETEGIL 150
VHPNQEPAVI AGQGTIALEV LNQVPLVDAL VVPVGGGGMV AGIAITIKAL 200
KPSVKVYAAE PSNADDCYQS KLKGELTPNL HPPETIADGV KSSIGLNTWP 250
IIRDLVDDVF TVTEDEIKYA TQLVWGRMKL LIEPTAGVAL AAVLSQHFQT 300
VSPEVKNVCI VLSGGNVDLT SLNWVGQAER PAPYQTVSV 339
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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei174 – 19825Missing in isoform 2. VSP_025013Add
BLAST
Alternative sequencei183 – 339157Missing in isoform 3. VSP_025014Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111P → T in BAC25712. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS25038.1. [Q9QZX7-1 ]
RefSeqi NP_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 ]
UniGenei Mm.131443.
Mm.220843.
Mm.412219.

3D structure databases

ProteinModelPortali Q9QZX7.
SMRi Q9QZX7. Positions 3-324.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 205172. 3 interactions.
IntActi Q9QZX7. 2 interactions.
MINTi MINT-5202279.

Chemistry

ChEMBLi CHEMBL1075306.

PTM databases

PhosphoSitei Q9QZX7.

Proteomic databases

MaxQBi Q9QZX7.
PaxDbi Q9QZX7.
PRIDEi Q9QZX7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000065211 ; ENSMUSP00000067552 ; ENSMUSG00000001323 . [Q9QZX7-1 ]
ENSMUST00000108447 ; ENSMUSP00000104086 ; ENSMUSG00000001323 . [Q9QZX7-2 ]
ENSMUST00000108448 ; ENSMUSP00000104087 ; ENSMUSG00000001323 . [Q9QZX7-1 ]
ENSMUST00000121738 ; ENSMUSP00000113372 ; ENSMUSG00000001323 . [Q9QZX7-1 ]
ENSMUST00000128556 ; ENSMUSP00000120012 ; ENSMUSG00000001323 . [Q9QZX7-3 ]
GeneIDi 27364.
KEGGi mmu:27364.
UCSCi uc007kcr.2. mouse. [Q9QZX7-1 ]
uc007kcu.2. mouse. [Q9QZX7-3 ]
uc011xzd.1. mouse. [Q9QZX7-2 ]

Organism-specific databases

CTDi 63826.
MGIi MGI:1351636. Srr.

Phylogenomic databases

eggNOGi COG1171.
GeneTreei ENSGT00550000075026.
HOVERGENi HBG023167.
InParanoidi Q9QZX7.
KOi K12235.
OMAi VEHYEAP.
OrthoDBi EOG7HB5B2.
PhylomeDBi Q9QZX7.
TreeFami TF313346.

Enzyme and pathway databases

BRENDAi 5.1.1.18. 3474.

Miscellaneous databases

NextBioi 305244.
PROi Q9QZX7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9QZX7.
Bgeei Q9QZX7.
CleanExi MM_SRR.
Genevestigatori Q9QZX7.

Family and domain databases

InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view ]
Pfami PF00291. PALP. 1 hit.
[Graphical view ]
SUPFAMi SSF53686. SSF53686. 1 hit.
PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 110 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