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O88829 (SIAT9_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length414 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 414414Lactosylceramide alpha-2,3-sialyltransferase
PRO_0000149303

Regions

Topological domain1 – 6565Cytoplasmic Potential
Transmembrane66 – 8621Helical; Signal-anchor for type II membrane protein; Potential
Topological domain87 – 414328Lumenal Potential

Amino acid modifications

Glycosylation2351N-linked (GlcNAc...) Potential
Glycosylation2791N-linked (GlcNAc...) Potential
Glycosylation3891N-linked (GlcNAc...) Potential
Disulfide bond194 ↔ 352 By similarity

Natural variations

Alternative sequence1 – 2626MHTEA…APACR → MGAPGELRRCGRGAA in isoform 2.
VSP_033689

Experimental info

Sequence conflict1391N → K in BAE34763. Ref.4
Sequence conflict1831P → S in CAA75235. Ref.1
Sequence conflict1831P → S in CAA75236. Ref.1
Sequence conflict2321H → Y in BAE34763. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 3BC5AEE20D7627DD

FASTA41447,360
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 9B344FEADD62FCA8
Show »

FASTA40346,127

References

« Hide '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. expand/collapse author list , 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.
+Additional computationally mapped references.

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.
CCDSCCDS20237.1. [O88829-1]
PIRJE0364.
RefSeqNP_001030305.1. NM_001035228.2. [O88829-1]
NP_035505.2. NM_011375.3.
XP_006505880.1. XM_006505817.1.
UniGeneMm.38248.

3D structure databases

ProteinModelPortalO88829.
SMRO88829. Positions 132-363.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000070414.

Protein family/group databases

CAZyGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteO88829.

Proteomic databases

PaxDbO88829.
PRIDEO88829.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000069994; ENSMUSP00000070414; ENSMUSG00000056091. [O88829-1]
ENSMUST00000114112; ENSMUSP00000109747; ENSMUSG00000056091.
GeneID20454.
KEGGmmu:20454.
UCSCuc009chy.1. mouse. [O88829-1]

Organism-specific databases

CTD8869.
MGIMGI:1339963. St3gal5.

Phylogenomic databases

eggNOGNOG257001.
GeneTreeENSGT00620000087815.
HOVERGENHBG056676.
InParanoidB2RRS1.
KOK03370.
OMAFFWKQVA.
OrthoDBEOG76X609.
PhylomeDBO88829.
TreeFamTF352819.

Gene expression databases

ArrayExpressO88829.
BgeeO88829.
GenevestigatorO88829.

Family and domain databases

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

Other

ChiTaRSST3GAL5. mouse.
NextBio298530.
PROO88829.
SOURCESearch...

Entry information

Entry nameSIAT9_MOUSE
AccessionPrimary (citable) accession number: O88829
Secondary accession number(s): B2RRS1 expand/collapse secondary AC list , 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: July 9, 2014
This is version 107 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot