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Q02734 (SIAT6_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase

EC=2.4.99.6
Alternative name(s):
Beta-galactoside alpha-2,3-sialyltransferase 3
Short name=Alpha 2,3-ST 3
Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase
N-acetyllactosaminide alpha-2,3-sialyltransferase
ST3Gal III
Short name=ST3GalIII
ST3N
Sialyltransferase 6
Gene names
Name:St3gal3
Synonyms:Siat6
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length374 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- or NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc By similarity.

Catalytic activity

CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-glycoprotein.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Secreted. Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.

Tissue specificity

Found in all tissues tested. High expression found in brain, liver, kidney, colon, heart and lung.

Post-translational modification

The soluble form derives from the membrane form by proteolytic processing.

Sequence similarities

Belongs to the glycosyltransferase 29 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 374374CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
PRO_0000012143
Chain48 – 374327CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase soluble form
PRO_0000012144

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2820Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 374346Lumenal Potential

Sites

Site46 – 472Cleavage; partial

Amino acid modifications

Glycosylation791N-linked (GlcNAc...) Potential
Glycosylation1701N-linked (GlcNAc...) Potential
Disulfide bond159 ↔ 313 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q02734 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 16BAD1458963024C

FASTA37442,082
        10         20         30         40         50         60 
MGLLVFVRNL LLALCLFLVL GFLYYSAWKL HLLQWEDSNS LILSLDSAGQ TLGTEYDRLG 

        70         80         90        100        110        120 
FLLKLDSKLP AELATKYANF SEGACKPGYA SAMMTAIFPR FSKPAPMFLD DSFRKWARIR 

       130        140        150        160        170        180 
EFVPPFGIKG QDNLIKAILS VTKEYRLTPA LDSLHCRRCI IVGNGGVLAN KSLGSRIDDY 

       190        200        210        220        230        240 
DIVIRLNSAP VKGFEKDVGS KTTLRITYPE GAMQRPEQYE RDSLFVLAGF KWQDFKWLKY 

       250        260        270        280        290        300 
IVYKERVSAS DGFWKSVATR VPKEPPEIRI LNPYFIQEAA FTLIGLPFNN GLMGRGNIPT 

       310        320        330        340        350        360 
LGSVAVTMAL DGCDEVAVAG FGYDMNTPNA PLHYYETVRM AAIKESWTHN IQREKEFLRK 

       370 
LVKARVITDL SSGI 

« Hide

References

[1]"Primary structure of Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase determined by mass spectrometry sequence analysis and molecular cloning. Evidence for a protein motif in the sialyltransferase gene family."
Wen D.X., Livingston B.D., Medzihradszky K.F., Kelm S., Burlingame A.L., Paulson J.C.
J. Biol. Chem. 267:21011-21019(1992) [PubMed: 1400416] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97754 mRNA. Translation: AAA42146.1.
IPIIPI00210122.
PIRA45074.
RefSeqNP_113885.1. NM_031697.1.
UniGeneRn.44390.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ02734.

Protein family/group databases

CAZyGT29. Glycosyltransferase Family 29.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64445.
KEGGrno:64445.

Organism-specific databases

CTD6487.
RGD68414. St3gal3.

Phylogenomic databases

eggNOGroNOG05023.
GeneTreeENSGT00550000074199.
HOVERGENHBG056676.
InParanoidQ02734.

Enzyme and pathway databases

BRENDA2.4.99.6. 5301.

Gene expression databases

ArrayExpressQ02734.
GenevestigatorQ02734.
GermOnlineENSRNOG00000019843. Rattus norvegicus.

Family and domain databases

InterProIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
KOK00781.
PfamPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFPIRSF005557. Sialyl_trans. 1 hit.
ProtoNetSearch...

Other

NextBio613178.

Entry information

Entry nameSIAT6_RAT
AccessionPrimary (citable) accession number: Q02734
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: November 16, 2011
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families