Q11205 (SIA4B_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
Short name=Alpha 2,3-ST 2
Short name=Beta-galactoside alpha-2,3-sialyltransferase 2
EC=2.4.99.4

Alternative name(s):
Gal-NAc6S
Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase
ST3Gal II
Short name=ST3GalII
ST3GalA.2
Sialyltransferase 4B
Short name=SIAT4-B

Gene names

Name:	St3gal2
Synonyms:	Siat4b, Siat5

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	350 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	It may be responsible for the synthesis of the sequence NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found in terminal carbohydrate groups of certain glycoproteins, oligosaccharides and glycolipids. SIAT4A and SIAT4B sialylate the same acceptor substrates but exhibit different Km values.
Catalytic activity	CMP-N-acetylneuraminate + beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl-R.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid.
Post-translational modification	The soluble form derives from the membrane form by proteolytic processing.
Sequence similarities	Belongs to the glycosyltransferase 29 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein glycosylation Inferred from direct assay Ref.1. Source: RGD
Cellular_component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to Golgi membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	beta-galactoside (CMP) alpha-2,3-sialyltransferase activity Inferred from electronic annotation. Source: EC sialyltransferase activity Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 350	350	CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2		PRO_0000149261
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 27	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	28 – 350	323	Lumenal Potential
Amino acid modifications
	Glycosylation	92	1	N-linked (GlcNAc...) Potential
	Glycosylation	211	1	N-linked (GlcNAc...) Potential
	Disulfide bond	152 ↔ 291		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q11205 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 87E6494FB02D0BE1	FASTA	350	40,166
	10 20 30 40 50 60 MKCSLRVWFL SMAFLLVFIM SLLFTYSHHS MATLPYLDSG TLGGTHRVKL VPGYTGQQRL 70 80 90 100 110 120 VKEGLSGKSC TCSRCMGDAG TSEWFDSHFD SNISPVWTRD NMNLTPDVQR WWMMLQPQFK 130 140 150 160 170 180 SHNTNEVLEK LFQIVPGENP YRFRDPQQCR RCAVVGNSGN LRGSGYGQEV DSHNFIMRMN 190 200 210 220 230 240 QAPTVGFEKD VGSRTTHHFM YPESAKNLPA NVSFVLVPFK ALDLMWIASA LSTGQIRFTY 250 260 270 280 290 300 APVKSFLRVD KEKVQIYNPA FFKYIHDRWT EHHGRYPSTG MLVLFFALHV CDEVNVYGFG 310 320 330 340 350 ADSRGNWHHY WENNRYAGEF RKTGVHDADF EAHIIDILAK ASKIEVYRGN

References

[1]	"Cloning and expression of cDNA for a new type of Gal beta 1,3GalNAc alpha 2,3-sialyltransferase." Lee Y.-C., Kojima N., Wada E., Kurosawa N., Nakaoka T., Hamamoto T., Tsuji S. J. Biol. Chem. 269:10028-10033(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X76988 mRNA. Translation: CAA54293.1.
IPI	IPI00210638.
PIR	B54420.
RefSeq	NP_113883.2. NM_031695.2.
UniGene	Rn.33216.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000024248.
Protein family/group databases
CAZy	GT29. Glycosyltransferase Family 29.
Proteomic databases
PRIDE	Q11205.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	64442.
KEGG	rno:64442.
UCSC	RGD:68413. rat.
Organism-specific databases
CTD	6483.
RGD	68413. St3gal2.
Phylogenomic databases
eggNOG	NOG249462.
HOGENOM	HOG000126811.
HOVERGEN	HBG054227.
InParanoid	Q11205.
KO	K03368.
OrthoDB	EOG4PNXH3.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Genevestigator	Q11205.
GermOnline	ENSRNOG00000017932. Rattus norvegicus.
Family and domain databases
InterPro	IPR001675. Glyco_trans_29. IPR012163. Sialyl_trans. [Graphical view]
Pfam	PF00777. Glyco_transf_29. 1 hit. [Graphical view]
PIRSF	PIRSF005557. Sialyl_trans. 1 hit.
ProtoNet	Search...
Other
NextBio	613166.

Entry information

Entry name

SIA4B_RAT

Accession

Primary (citable) accession number: Q11205

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	April 3, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program