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Protein

N-acylneuraminate-9-phosphatase

Gene

Nanp

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by vanadate and calcium.1 Publication

Pathwayi: N-acetylneuraminate biosynthesis

This protein is involved in the pathway N-acetylneuraminate biosynthesis, which is part of Amino-sugar metabolism.
View all proteins of this organism that are known to be involved in the pathway N-acetylneuraminate biosynthesis and in Amino-sugar metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei164 – 1641SubstrateBy similarity

GO - Molecular functioni

  • N-acylneuraminate-9-phosphatase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14517.
ReactomeiR-RNO-4085001. Sialic acid metabolism.
SABIO-RKQ5M969.
UniPathwayiUPA00630.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acylneuraminate-9-phosphatase (EC:3.1.3.29)
Alternative name(s):
Haloacid dehalogenase-like hydrolase domain-containing protein 4
Neu5Ac-9-Pase
Gene namesi
Name:NanpBy similarity
Synonyms:Hdhd4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi1306009. Nanp.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 248248N-acylneuraminate-9-phosphatasePRO_0000233379Add
BLAST

Proteomic databases

PaxDbiQ5M969.
PRIDEiQ5M969.

Expressioni

Gene expression databases

GenevisibleiQ5M969. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011315.

Structurei

3D structure databases

ProteinModelPortaliQ5M969.
SMRiQ5M969. Positions 1-247.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni12 – 143Substrate bindingBy similarity
Regioni131 – 1322Substrate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
COG1011. LUCA.
GeneTreeiENSGT00390000003094.
HOGENOMiHOG000248345.
HOVERGENiHBG051895.
InParanoidiQ5M969.
KOiK01097.
OMAiVRATVWI.
OrthoDBiEOG7JDQZJ.
PhylomeDBiQ5M969.
TreeFamiTF324589.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011950. HAD-SF_hydro_IA_CTE7.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02253. CTE7. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5M969-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLSRVRAVF FDLDNTLIDT AGASRRGMLE VIKLLQSKYH YKEEAEVICD
60 70 80 90 100
KVQVKLSKEC FHPYSTCITD VRTSHWEEAI QETKGGADNR KLAEECYFLW
110 120 130 140 150
KSTRLQHMTL EEDVKAMLTE LRKEVRLLLL TNGDRQTQRE KIEACACQSY
160 170 180 190 200
FDAIVVGGEQ KEEKPAPSIF YHCCDLLGVQ PGDCVMVGDT LETDIQGGLN
210 220 230 240
AGLKATVWIN KSGGVPLTSS PMPHYMVSSV LELPALLQSI DCKVSMSV
Length:248
Mass (Da):27,741
Last modified:February 1, 2005 - v1
Checksum:i7ABF6063C67BF1AB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087587 mRNA. Translation: AAH87587.1.
RefSeqiNP_001009409.1. NM_001009409.1.
UniGeneiRn.210573.

Genome annotation databases

EnsembliENSRNOT00000011315; ENSRNOP00000011315; ENSRNOG00000008307.
GeneIDi311530.
KEGGirno:311530.
UCSCiRGD:1306009. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC087587 mRNA. Translation: AAH87587.1.
RefSeqiNP_001009409.1. NM_001009409.1.
UniGeneiRn.210573.

3D structure databases

ProteinModelPortaliQ5M969.
SMRiQ5M969. Positions 1-247.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011315.

Proteomic databases

PaxDbiQ5M969.
PRIDEiQ5M969.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000011315; ENSRNOP00000011315; ENSRNOG00000008307.
GeneIDi311530.
KEGGirno:311530.
UCSCiRGD:1306009. rat.

Organism-specific databases

CTDi140838.
RGDi1306009. Nanp.

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
COG1011. LUCA.
GeneTreeiENSGT00390000003094.
HOGENOMiHOG000248345.
HOVERGENiHBG051895.
InParanoidiQ5M969.
KOiK01097.
OMAiVRATVWI.
OrthoDBiEOG7JDQZJ.
PhylomeDBiQ5M969.
TreeFamiTF324589.

Enzyme and pathway databases

UniPathwayiUPA00630.
BioCyciMetaCyc:MONOMER-14517.
ReactomeiR-RNO-4085001. Sialic acid metabolism.
SABIO-RKQ5M969.

Miscellaneous databases

NextBioi663755.
PROiQ5M969.

Gene expression databases

GenevisibleiQ5M969. RN.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
InterProiIPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011950. HAD-SF_hydro_IA_CTE7.
[Graphical view]
PfamiPF13419. HAD_2. 1 hit.
[Graphical view]
PRINTSiPR00413. HADHALOGNASE.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR02253. CTE7. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: Brain.
  2. "Identification of the sequence encoding N-acetylneuraminate-9-phosphate phosphatase."
    Maliekal P., Vertommen D., Delpierre G., Van Schaftingen E.
    Glycobiology 16:165-172(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION.

Entry informationi

Entry nameiNANP_RAT
AccessioniPrimary (citable) accession number: Q5M969
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: February 1, 2005
Last modified: May 11, 2016
This is version 87 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

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.