O88829 (SIAT9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Lactosylceramide alpha-2,3-sialyltransferase
EC=2.4.99.9

Alternative name(s):
CMP-NeuAc:lactosylceramide alpha-2,3-sialyltransferase
Ganglioside GM3 synthase
ST3Gal V
Short name=ST3GalV
Sialyltransferase 9

Gene names

Name:	St3gal5
Synonyms:	GM3S, Siat9

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [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 › Mus › Mus

Protein attributes

Sequence length	414 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the formation of ganglioside GM3 (alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1, 4-beta-D-glucosylceramide). Ref.8
Catalytic activity	CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein Potential.
Disruption phenotype	Mice are viable and fertile, and do not show any obvious abnormality apart from an increased sensitivity to insulin. Ref.8
Sequence similarities	Belongs to the glycosyltransferase 29 family.
Sequence caution	The sequence AAF66147.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA33491.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA76467.1 differs from that shown. Reason: Erroneous initiation. The sequence BAB28571.1 differs from that shown. Reason: Erroneous initiation. The sequence BAE34763.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA75235.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA75236.1 differs from that shown. Reason: Erroneous initiation. The sequence CAC79655.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein glycosylation Inferred from electronic annotation. Source: InterPro
Cellular_component	integral to Golgi membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	lactosylceramide alpha-2,3-sialyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O88829-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O88829-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MHTEAVGGAARRPQKLRSQAAAPACR → MGAPGELRRCGRGAA

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 414	414	Lactosylceramide alpha-2,3-sialyltransferase		PRO_0000149303
Regions
	Topological domain	1 – 65	65	Cytoplasmic Potential
	Transmembrane	66 – 86	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	87 – 414	328	Lumenal Potential
Amino acid modifications
	Modified residue	18	1	Phosphoserine Ref.9
	Glycosylation	235	1	N-linked (GlcNAc...) Potential
	Glycosylation	279	1	N-linked (GlcNAc...) Potential
	Glycosylation	389	1	N-linked (GlcNAc...) Potential
	Disulfide bond	194 ↔ 352		By similarity
Natural variations
	Alternative sequence	1 – 26	26	MHTEA…APACR → MGAPGELRRCGRGAA in isoform 2.		VSP_033689
Experimental info
	Sequence conflict	139	1	N → K in BAE34763. Ref.4
	Sequence conflict	183	1	P → S in CAA75235. Ref.1
	Sequence conflict	183	1	P → S in CAA75236. Ref.1
	Sequence conflict	232	1	H → Y in BAE34763. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 20, 2008. Version 2. Checksum: 3BC5AEE20D7627DD	FASTA	414	47,360
	10 20 30 40 50 60 MHTEAVGGAA RRPQKLRSQA AAPACRAMPS EFTSAKLRSD CSRTSLQWYT RTQHKMRRPS 70 80 90 100 110 120 LLIKDICKCT LVAFGVWLLY ILILNYTAEE CDMKRMHYVD PDRIKRAQSY AQEVLQKECR 130 140 150 160 170 180 PRYAKTAMAL LFEDRYSINL EPFVQKVPTA SEAELKYDPP FGFRKFSSKV QSLLDMLPEH 190 200 210 220 230 240 DFPEHLRAKA CKRCVVVGNG GILHGLELGH ALNQFDVVIR LNSAPVEGYS EHVGNKTTIR 250 260 270 280 290 300 MTYPEGAPLS DVEYYANDLF VTVLFKSVDF KWLQAMVKNE SLPFWVRLFF WKQVAEKVPL 310 320 330 340 350 360 QPKHFRILNP VIIKETAFDI LQYSEPQSRF WGHDKNIPTI GVIAVVLATH LCDEVSLAGF 370 380 390 400 410 GYDLSQPRTP LHYFDSQCMG AMHWQVMHNV TTETKFLLKL LKEGVVEDLS GGIH
	Isoform 2 [UniParc]. Checksum: 9B344FEADD62FCA8	FASTA	403	46,127
	10 20 30 40 50 60 MGAPGELRRC GRGAAAMPSE FTSAKLRSDC SRTSLQWYTR TQHKMRRPSL LIKDICKCTL 70 80 90 100 110 120 VAFGVWLLYI LILNYTAEEC DMKRMHYVDP DRIKRAQSYA QEVLQKECRP RYAKTAMALL 130 140 150 160 170 180 FEDRYSINLE PFVQKVPTAS EAELKYDPPF GFRKFSSKVQ SLLDMLPEHD FPEHLRAKAC 190 200 210 220 230 240 KRCVVVGNGG ILHGLELGHA LNQFDVVIRL NSAPVEGYSE HVGNKTTIRM TYPEGAPLSD 250 260 270 280 290 300 VEYYANDLFV TVLFKSVDFK WLQAMVKNES LPFWVRLFFW KQVAEKVPLQ PKHFRILNPV 310 320 330 340 350 360 IIKETAFDIL QYSEPQSRFW GHDKNIPTIG VIAVVLATHL CDEVSLAGFG YDLSQPRTPL 370 380 390 400 HYFDSQCMGA MHWQVMHNVT TETKFLLKLL KEGVVEDLSG GIH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and characterization of fifth type of beta-galactoside alpha-2,3-sialyltransferase (ST3Gal V; GM3 synthase)." Kono M., Takashima S., Liu H., Inoue M., Kojima N., Young-Choon L., Hamamoto T., Tsuji S. Biochem. Biophys. Res. Commun. 253:170-175(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Strain: ICR. Tissue: Brain.
[2]	"Mouse GM3 Synthase cDNA." Ishii A., Saito M. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Brain.
[3]	"Combinatorial PCR in homologous cloning: cloning of GM3 synthase (ST-I)." Kapitonov D., Yu R.K. Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Strain: C57BL/6J.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6. Tissue: Visual cortex.
[5]	"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] (ISOFORM 1). Tissue: Brain.
[6]	"Expression cloning of mouse cDNA of CMP-NeuAc: lactosylceramide alpha2,3-sialyltransferase, an enzyme that initiates the synthesis of gangliosides." Fukumoto S., Miyazaki H., Goto G., Urano T., Furukawa K., Furukawa K. J. Biol. Chem. 274:9271-9276(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-414. Strain: BALB/c.
[7]	Shuichi T. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-414. Strain: ICR. Tissue: Brain.
[8]	"Enhanced insulin sensitivity in mice lacking ganglioside GM3." Yamashita T., Hashiramoto A., Haluzik M., Mizukami H., Beck S., Norton A., Kono M., Tsuji S., Daniotti J.L., Werth N., Sandhoff R., Sandhoff K., Proia R.L. Proc. Natl. Acad. Sci. U.S.A. 100:3445-3449(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[9]	"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, MASS SPECTROMETRY. Tissue: Teratocarcinoma.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

ST3Gal V

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y15003 mRNA. Translation: CAA75235.1. Different initiation. Y15003 mRNA. Translation: CAA75236.1. Different initiation. AB018048 mRNA. Translation: BAA33491.1. Different initiation. AF119416 mRNA. Translation: AAF66147.1. Different initiation. AK012961 mRNA. Translation: BAB28571.1. Different initiation. AK159000 mRNA. Translation: BAE34763.1. Different initiation. AK165726 mRNA. Translation: BAE38355.1. BC138557 mRNA. Translation: AAI38558.1. BC138559 mRNA. Translation: AAI38560.1. AB013302 mRNA. Translation: BAA76467.1. Different initiation. Y18022 Genomic DNA. Translation: CAC79654.1. Y18023 Genomic DNA. Translation: CAC79655.1. Sequence problems.
IPI	IPI00349830. IPI00655172.
PIR	JE0364.
RefSeq	NP_001030305.1. NM_001035228.1. NP_035505.2. NM_011375.2.
UniGene	Mm.38248.
3D structure databases
ProteinModelPortal	O88829.
SMR	O88829. Positions 132-363.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000070414.
Protein family/group databases
CAZy	GT29. Glycosyltransferase Family 29.
PTM databases
PhosphoSite	O88829.
Proteomic databases
PaxDb	O88829.
PRIDE	O88829.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000069994; ENSMUSP00000070414; ENSMUSG00000056091. ENSMUST00000114112; ENSMUSP00000109747; ENSMUSG00000056091.
GeneID	20454.
KEGG	mmu:20454.
UCSC	uc009chy.1. mouse. uc009chz.1. mouse.
Organism-specific databases
CTD	8869.
MGI	MGI:1339963. St3gal5.
Phylogenomic databases
eggNOG	NOG257001.
GeneTree	ENSGT00620000087815.
HOVERGEN	HBG056676.
InParanoid	B2RRS1.
KO	K03370.
OMA	FFWKQVA.
OrthoDB	EOG47PX6C.
Gene expression databases
ArrayExpress	O88829.
Bgee	O88829.
Genevestigator	O88829.
GermOnline	ENSMUSG00000056091. Mus musculus.
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
ChiTaRS	ST3GAL5. mouse.
NextBio	298530.
SOURCE	Search...

Entry information

Entry name

SIAT9_MOUSE

Accession

Primary (citable) accession number: O88829
Secondary accession number(s): B2RRS1 , Q3TMT6, Q3TY01, Q91YF2, Q91YF3, Q9CZ65, Q9QWF8, Q9QWF9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2002
Last sequence update:	May 20, 2008
Last modified:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program