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Q9DCJ9 (NPL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-acetylneuraminate lyase

Short name=NALase
EC=4.1.3.3
Alternative name(s):
N-acetylneuraminate pyruvate-lyase
N-acetylneuraminic acid aldolase
Sialate lyase
Sialate-pyruvate lyase
Sialic acid aldolase
Sialic acid lyase
Gene names
Name:Npl
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. Ref.3

Catalytic activity

N-acetylneuraminate = N-acetyl-D-mannosamine + pyruvate. Ref.3

Pathway

Amino-sugar metabolism; N-acetylneuraminate degradation. Ref.3

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the DapA family. NanA subfamily.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   LigandSchiff base
   Molecular functionLyase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processN-acetylneuraminate catabolic process

Traceable author statement Ref.3. Source: UniProtKB

carbohydrate metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionN-acetylneuraminate lyase activity

Inferred from direct assay Ref.3. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320N-acetylneuraminate lyase
PRO_0000273353

Regions

Region51 – 522Substrate binding By similarity

Sites

Active site1731Schiff-base intermediate with substrate By similarity
Site1431Involved in proton transfer during cleavage By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DCJ9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 9426AD7CC8438468

FASTA32035,130
        10         20         30         40         50         60 
MAFPKKKLRG LVAATITPMT ENGEINFPVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV 

        70         80         90        100        110        120 
SERRQVAEEW VNQGRNKLDQ VVIHVGALNV KESQELAQHA AEIGADGIAV IAPFFFKSQN 

       130        140        150        160        170        180 
KDALISFLRE VAAAAPTLPF YYYHMPSMTG VKIRAEELLD GIQDKIPTFQ GLKFTDTDLL 

       190        200        210        220        230        240 
DFGQCVDQNH QRQFALLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDLA 

       250        260        270        280        290        300 
SALSYQFRIQ RFINYVIKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKATQ EFTAKAEAKL 

       310        320 
KSLDFLSSPS VKEGKPLASA 

« Hide

References

« Hide 'large scale' references
[1]"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. expand/collapse author list , 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].
Strain: C57BL/6J and NOD.
Tissue: Kidney and Thymus.
[2]"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].
Tissue: Eye.
[3]"Metabolism of vertebrate amino sugars with N-glycolyl groups: elucidating the intracellular fate of the non-human sialic acid N-glycolylneuraminic acid."
Bergfeld A.K., Pearce O.M., Diaz S.L., Pham T., Varki A.
J. Biol. Chem. 287:28865-28881(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002734 mRNA. Translation: BAB22314.1.
AK088859 mRNA. Translation: BAC40618.1.
BC022734 mRNA. Translation: AAH22734.1.
CCDSCCDS15374.1.
RefSeqNP_083025.1. NM_028749.1.
UniGeneMm.24887.

3D structure databases

ProteinModelPortalQ9DCJ9.
SMRQ9DCJ9. Positions 8-280.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DCJ9. 1 interaction.
MINTMINT-4128676.
STRING10090.ENSMUSP00000037454.

PTM databases

PhosphoSiteQ9DCJ9.

Proteomic databases

MaxQBQ9DCJ9.
PaxDbQ9DCJ9.
PRIDEQ9DCJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000041874; ENSMUSP00000037454; ENSMUSG00000042684.
GeneID74091.
KEGGmmu:74091.
UCSCuc007dac.1. mouse.

Organism-specific databases

CTD80896.
MGIMGI:1921341. Npl.

Phylogenomic databases

eggNOGCOG0329.
GeneTreeENSGT00530000063604.
HOGENOMHOG000218206.
HOVERGENHBG082055.
InParanoidQ9DCJ9.
KOK01639.
OMALKPWNKD.
OrthoDBEOG7NKKKP.
PhylomeDBQ9DCJ9.
TreeFamTF353639.

Enzyme and pathway databases

UniPathwayUPA00629.

Gene expression databases

BgeeQ9DCJ9.
CleanExMM_NPL.
GenevestigatorQ9DCJ9.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
[Graphical view]
PANTHERPTHR12128. PTHR12128. 1 hit.
PfamPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFPIRSF001365. DHDPS. 1 hit.
PRINTSPR00146. DHPICSNTHASE.
ProtoNetSearch...

Other

NextBio339741.
PROQ9DCJ9.
SOURCESearch...

Entry information

Entry nameNPL_MOUSE
AccessionPrimary (citable) accession number: Q9DCJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot