Q9CPT3 (NANP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Nanp
Synonyms:	Hdhd4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	248 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	N-acylneuraminate 9-phosphate + H2O = N-acylneuraminate + phosphate.
Cofactor	Magnesium By similarity.
Enzyme regulation	Inhibited by vanadate and calcium By similarity.
Pathway	Amino-sugar metabolism; N-acetylneuraminate biosynthesis.
Sequence similarities	Belongs to the HAD-like hydrolase superfamily. NANP family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Ligand	Magnesium
Molecular function	Hydrolase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	N-acetylneuraminate biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	N-acylneuraminate-9-phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB phosphoglycolate phosphatase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 248

248

N-acylneuraminate-9-phosphatase

PRO_0000083939

Regions

Region

12 – 14

3

Substrate binding

Region

131 – 132

2

Substrate binding

Sites

Binding site

164

1

Substrate

Secondary structure

1

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248

Helix Strand Turn

Details...

Beta strand

8 – 11

4

Turn

15 – 17

3

Helix

20 – 37

18

Helix

44 – 57

14

Helix

68 – 84

17

Helix

90 – 106

17

Helix

112 – 122

11

Beta strand

125 – 131

7

Helix

135 – 145

11

Helix

148 – 150

3

Beta strand

152 – 156

5

Helix

157 – 159

3

Beta strand

160 – 162

3

Helix

167 – 177

11

Helix

181 – 183

3

Beta strand

184 – 189

6

Turn

191 – 193

3

Helix

194 – 200

7

Beta strand

204 – 209

6

Beta strand

224 – 229

6

Helix

230 – 232

3

Helix

233 – 240

8

Sequences

	Sequence		Length	Mass (Da)
	Q9CPT3 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: FA1703873D7CC069	FASTA	248	27,808
	10 20 30 40 50 60 MGLSRVRAVF FDLDNTLIDT AGASRRGMLE VIKLLQSKYH YKEEAEIICD KVQVKLSKEC 70 80 90 100 110 120 FHPYSTCITD VRTSHWEEAI QETKGGADNR KLAEECYFLW KSTRLQHMIL ADDVKAMLTE 130 140 150 160 170 180 LRKEVRLLLL TNGDRQTQRE KIEACACQSY FDAIVIGGEQ KEEKPAPSIF YHCCDLLGVQ 190 200 210 220 230 240 PGDCVMVGDT LETDIQGGLN AGLKATVWIN KSGRVPLTSS PMPHYMVSSV LELPALLQSI DCKVSMSV

References

	« Hide 'large scale' referencesShow '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. , 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Mammary gland and Placenta.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Limb and Mammary gland.
[3]	"Crystal structure of protein C20orf147 homolog (17391249) from Mus musculus at 1.90 A resolution." Joint center for structural genomics (JCSG) Submitted (MAR-2011) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH PHOSPHATE IONS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AK005566 mRNA. Translation: BAB24126.1.
AK021344 mRNA. Translation: BAB32381.1.
BC018527 mRNA. Translation: AAH18527.1.
BC083086 mRNA. Translation: AAH83086.1.

IPI

IPI00131952.

RefSeq

NP_080362.1. NM_026086.2.

UniGene

Mm.480682.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2GFH	X-ray	1.90	A	1-248	[»]

ProteinModelPortal

Q9CPT3.

SMR

Q9CPT3. Positions 1-247.

ModBase

Search...

Protein-protein interaction databases

STRING

Q9CPT3.

PTM databases

PhosphoSite

Q9CPT3.

Proteomic databases

PRIDE

Q9CPT3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000057074; ENSMUSP00000094869; ENSMUSG00000043346.
ENSMUST00000066640; ENSMUSP00000063895; ENSMUSG00000053916.

GeneID

67311.

KEGG

mmu:67311.

NMPDR

fig|10090.3.peg.7122.

Organism-specific databases

CTD

140838.

MGI

MGI:1914561. Nanp.

Phylogenomic databases

GeneTree

ENSGT00390000003094.

HOGENOM

HBG716739.

HOVERGEN

HBG051895.

InParanoid

Q9CPT3.

OMA

HYIVSSV.

OrthoDB

EOG483D5Q.

PhylomeDB

Q9CPT3.

Gene expression databases

Bgee

Q9CPT3.

Genevestigator

Q9CPT3.

GermOnline

ENSMUSG00000043346. Mus musculus.
ENSMUSG00000053916. Mus musculus.

Family and domain databases

InterPro

IPR005834. Dehalogen-like_hydro.
IPR023214. HAD-like_dom.
IPR011950. HAD-SF_hydro_IA_CTE7.
IPR006439. HAD-SF_hydro_IA_v1.
IPR005833. Haloacid_DH/epoxide_hydro.
[Graphical view]

Gene3D

G3DSA:3.40.50.1000. HAD-like_dom. 1 hit.

KO

K01097.

Pfam

PF00702. Hydrolase. 1 hit.
[Graphical view]

PRINTS

PR00413. HADHALOGNASE.

SUPFAM

SSF56784. HAD-like_dom. 1 hit.

TIGRFAMs

TIGR02253. CTE7. 1 hit.
TIGR01549. HAD-SF-IA-v1. 1 hit.

ProtoNet

Search...

Other

NextBio

324202.

SOURCE

Search...

Entry information

Entry name

NANP_MOUSE

Accession

Primary (citable) accession number: Q9CPT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 30, 2003
Last sequence update:	June 1, 2001
Last modified:	November 16, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program