Reviewed, UniProtKB/Swiss-Prot Q9Y3R4 (NEUR2_HUMAN)

Names and origin

Protein names

Recommended name:
    Sialidase-2
    EC=3.2.1.18
Alternative name(s):
    Cytosolic sialidase
    N-acetyl-alpha-neuraminidase 2

Gene names

Name:

NEU2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes sialylated compounds.
Catalytic activity	Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Subcellular location	Cytoplasm By similarity.
Tissue specificity	Expressed in skeletal muscle, fetal liver and embryonic carcinoma cell line NT2D1.
Sequence similarities	Belongs to the glycosyl hydrolase 33 family. Contains 2 BNR repeats.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Polymorphism
Domain	Repeat
Molecular function	Glycosidase Hydrolase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Traceable author statement. Source: ProtInc
Molecular function	exo-alpha-sialidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 380

380

Sialidase-2

PRO_0000208899

Regions

Repeat

127 – 138

12

BNR 1

Repeat

197 – 208

12

BNR 2

Motif

20 – 23

4

FRIP motif

Sites

Active site

46

1

Proton acceptor By similarity

Active site

334

1

Nucleophile By similarity

Active site

355

1

Potential

Binding site

21

1

Substrate By similarity

Binding site

237

1

Substrate Potential

Binding site

304

1

Substrate By similarity

Natural variations

Natural variant

11

1

S → R: dbSNP rs2233384.

VAR_024461

Natural variant

41

1

R → Q Reduced activity; increased sensitivity to inhibition by oseltamivir carboxylate. dbSNP rs2233385. Ref.6

VAR_024462

Natural variant

145

1

A → T: dbSNP rs2233390.

VAR_049204

Natural variant

168

1

H → N: dbSNP rs2233391.

VAR_055311

Natural variant

182

1

R → Q: dbSNP rs2233393.

VAR_055312

Secondary structure

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380

Helix Strand Turn

Details...

Beta strand

7 – 14

8

Beta strand

16 – 28

13

Helix

29 – 31

3

Beta strand

33 – 41

9

Beta strand

51 – 60

10

Helix

61 – 63

3

Beta strand

65 – 68

4

Beta strand

82 – 92

11

Turn

93 – 96

4

Beta strand

97 – 106

10

Helix

112 – 115

4

Beta strand

116 – 118

3

Beta strand

123 – 131

9

Helix

143 – 147

5

Helix

148 – 153

6

Beta strand

154 – 159

6

Beta strand

174 – 182

9

Beta strand

191 – 201

11

Beta strand

213 – 224

12

Beta strand

231 – 250

20

Beta strand

258 – 265

8

Turn

268 – 270

3

Beta strand

275 – 280

6

Beta strand

291 – 298

8

Beta strand

301 – 314

14

Helix

318 – 320

3

Beta strand

325 – 342

18

Beta strand

346 – 356

11

Turn

357 – 360

4

Beta strand

361 – 368

8

Helix

369 – 372

4

Turn

374 – 376

3

Sequences

	Sequence		Length	Mass (Da)
	Q9Y3R4-1 [UniParc]. Last modified May 5, 2009. Version 2. Checksum: AD7B08C478F4D0D9	FASTA	380	42,254
	10 20 30 40 50 60 MASLPVLQKE SVFQSGAHAY RIPALLYLPG QQSLLAFAEQ RASKKDEHAE LIVLRRGDYD 70 80 90 100 110 120 APTHQVQWQA QEVVAQARLD GHRSMNPCPL YDAQTGTLFL FFIAIPGQVT EQQQLQTRAN 130 140 150 160 170 180 VTRLCQVTST DHGRTWSSPR DLTDAAIGPA YREWSTFAVG PGHCLQLHDR ARSLVVPAYA 190 200 210 220 230 240 YRKLHPIQRP IPSAFCFLSH DHGRTWARGH FVAQDTLECQ VAEVETGEQR VVTLNARSHL 250 260 270 280 290 300 RARVQAQSTN DGLDFQESQL VKKLVEPPPQ GCQGSVISFP SPRSGPGSPA QWLLYTHPTH 310 320 330 340 350 360 SWQRADLGAY LNPRPPAPEA WSEPVLLAKG SCAYSDLQSM GTGPDGSPLF GCLYEANDYE 370 380 EIVFLMFTLK QAFPAEYLPQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases." Monti E., Preti A., Rossi E., Ballabio A., Borsani G. Genomics 57:137-143(1999) [PubMed: 10191093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ASN-168.
[2]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed: 15815621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ASN-168.
[5]	"Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition." Chavas L.M.G., Tringali C., Fusi P., Venerando B., Tettamanti G., Kato R., Monti E., Wakatsuki S. J. Biol. Chem. 280:469-475(2005) [PubMed: 15501818] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS).
[6]	"A nonsynonymous SNP in human cytosolic sialidase in a small Asian population results in reduced enzyme activity: potential link with severe adverse reactions to oseltamivir." Li C.-Y., Yu Q., Ye Z.-Q., Sun Y., He Q., Li X.-M., Zhang W., Luo J., Gu X., Zheng X., Wei L. Cell Res. 17:357-362(2007) [PubMed: 17426694] [Abstract] Cited for: CHARACTERIZATION OF VARIANT GLN-41.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y16535 Genomic DNA. Translation: CAB41449.1.
AC106876 Genomic DNA. Translation: AAY24360.1.
CH471063 Genomic DNA. Translation: EAW71028.1.
BC069151 mRNA. Translation: AAH69151.1.
BC107053 mRNA. Translation: AAI07054.1.

IPI

IPI00022482.

RefSeq

NP_005374.2.

UniGene

Hs.532681

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1SNT	X-ray	1.75	A	1-380	[»]
1SO7	X-ray	1.49	A	1-380	[»]
1VCU	X-ray	2.85	A/B	1-380	[»]
2F0Z	X-ray	2.80	A	1-380	[»]
2F10	X-ray	2.90	A	1-380	[»]
2F11	X-ray	2.57	A	1-380	[»]
2F12	X-ray	2.27	A	1-380	[»]
2F13	X-ray	2.26	A	1-380	[»]
2F24	X-ray	1.76	A	1-380	[»]
2F25	X-ray	1.95	A/B	1-380	[»]
2F26	X-ray	1.58	A	1-380	[»]
2F27	X-ray	2.15	A/B	1-380	[»]
2F28	X-ray	1.67	A	1-380	[»]
2F29	X-ray	2.92	A/B	1-380	[»]

DisProt

DP00261.

ModBase

Search...

Protein family/group databases

CAZy

GH33. Glycoside Hydrolase Family 33.

PTM databases

PhosphoSite

Q9Y3R4.

Genome annotation databases

Ensembl

ENSG00000115488. Homo sapiens. [Contig view]

GeneID

4759.

KEGG

hsa:4759.

Organism-specific databases

GeneCards

GC02P233605.

H-InvDB

HIX0029978.

HGNC

HGNC:7759. NEU2.

MIM

605528. gene.

PharmGKB

PA31561.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9Y3R4.

HOVERGEN

Q9Y3R4.

Enzyme and pathway databases

BRENDA

3.2.1.18. 247.

Gene expression databases

ArrayExpress

Q9Y3R4.

Bgee

Q9Y3R4.

CleanEx

HS_NEU2.

GermOnline

ENSG00000115488. Homo sapiens.

Family and domain databases

ProtoNet

Search...

Other Resources

NextBio

18332.

SOURCE

Search...

Entry information

Entry name

NEUR2_HUMAN

Accession

Primary (citable) accession number: Q9Y3R4
Secondary accession number(s): Q3KNW4, Q6NTB4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 16, 2001
Last sequence update:	May 5, 2009
Last modified:	June 16, 2009
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)