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Protein

Lactosylceramide alpha-2,3-sialyltransferase

Gene

St3gal5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalyzes the formation of ganglioside GM3 (alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1, 4-beta-D-glucosylceramide).1 Publication

Catalytic activityi

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.

GO - Molecular functioni

  1. lactosylceramide alpha-2,3-sialyltransferase activity Source: UniProtKB

GO - Biological processi

  1. protein glycosylation Source: InterPro
  2. sialylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

ReactomeiREACT_202500. Sialic acid metabolism.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

Names & Taxonomyi

Protein namesi
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 namesi
Name:St3gal5
Synonyms:GM3S, Siat9
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 6

Organism-specific databases

MGIiMGI:1339963. St3gal5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6565CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei66 – 8621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini87 – 414328LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of Golgi membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are viable and fertile, and do not show any obvious abnormality apart from an increased sensitivity to insulin.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 414414Lactosylceramide alpha-2,3-sialyltransferasePRO_0000149303Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi194 ↔ 352By similarity
Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO88829.
PaxDbiO88829.
PRIDEiO88829.

PTM databases

PhosphoSiteiO88829.

Expressioni

Gene expression databases

BgeeiO88829.
ExpressionAtlasiO88829. baseline and differential.
GenevestigatoriO88829.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070414.

Structurei

3D structure databases

ProteinModelPortaliO88829.
SMRiO88829. Positions 132-363.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 29 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG257001.
GeneTreeiENSGT00760000119095.
HOVERGENiHBG056676.
InParanoidiO88829.
KOiK03370.
OMAiFFWKQVA.
OrthoDBiEOG76X609.
PhylomeDBiO88829.
TreeFamiTF352819.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFiPIRSF005557. Sialyl_trans. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O88829-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MHTEAVGGAA RRPQKLRSQA AAPACRAMPS EFTSAKLRSD CSRTSLQWYT
60 70 80 90 100
RTQHKMRRPS LLIKDICKCT LVAFGVWLLY ILILNYTAEE CDMKRMHYVD
110 120 130 140 150
PDRIKRAQSY AQEVLQKECR PRYAKTAMAL LFEDRYSINL EPFVQKVPTA
160 170 180 190 200
SEAELKYDPP FGFRKFSSKV QSLLDMLPEH DFPEHLRAKA CKRCVVVGNG
210 220 230 240 250
GILHGLELGH ALNQFDVVIR LNSAPVEGYS EHVGNKTTIR MTYPEGAPLS
260 270 280 290 300
DVEYYANDLF VTVLFKSVDF KWLQAMVKNE SLPFWVRLFF WKQVAEKVPL
310 320 330 340 350
QPKHFRILNP VIIKETAFDI LQYSEPQSRF WGHDKNIPTI GVIAVVLATH
360 370 380 390 400
LCDEVSLAGF GYDLSQPRTP LHYFDSQCMG AMHWQVMHNV TTETKFLLKL
410
LKEGVVEDLS GGIH
Length:414
Mass (Da):47,360
Last modified:May 20, 2008 - v2
Checksum:i3BC5AEE20D7627DD
GO
Isoform 2 (identifier: O88829-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:403
Mass (Da):46,127
Checksum:i9B344FEADD62FCA8
GO

Sequence cautioni

The sequence AAF66147.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA33491.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA76467.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB28571.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE34763.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA75235.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAA75236.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence CAC79655.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391N → K in BAE34763. (PubMed:16141072)Curated
Sequence conflicti183 – 1831P → S in CAA75235. (PubMed:9875239)Curated
Sequence conflicti183 – 1831P → S in CAA75236. (PubMed:9875239)Curated
Sequence conflicti232 – 2321H → Y in BAE34763. (PubMed:16141072)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MHTEA…APACR → MGAPGELRRCGRGAA in isoform 2. 1 PublicationVSP_033689Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20237.1. [O88829-1]
PIRiJE0364.
RefSeqiNP_001030305.1. NM_001035228.2. [O88829-1]
NP_035505.2. NM_011375.3.
XP_006505880.1. XM_006505817.1.
UniGeneiMm.38248.

Genome annotation databases

EnsembliENSMUST00000069994; ENSMUSP00000070414; ENSMUSG00000056091. [O88829-1]
ENSMUST00000114112; ENSMUSP00000109747; ENSMUSG00000056091.
GeneIDi20454.
KEGGimmu:20454.
UCSCiuc009chy.1. mouse. [O88829-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

ST3Gal V

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS20237.1. [O88829-1]
PIRiJE0364.
RefSeqiNP_001030305.1. NM_001035228.2. [O88829-1]
NP_035505.2. NM_011375.3.
XP_006505880.1. XM_006505817.1.
UniGeneiMm.38248.

3D structure databases

ProteinModelPortaliO88829.
SMRiO88829. Positions 132-363.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000070414.

Protein family/group databases

CAZyiGT29. Glycosyltransferase Family 29.

PTM databases

PhosphoSiteiO88829.

Proteomic databases

MaxQBiO88829.
PaxDbiO88829.
PRIDEiO88829.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000069994; ENSMUSP00000070414; ENSMUSG00000056091. [O88829-1]
ENSMUST00000114112; ENSMUSP00000109747; ENSMUSG00000056091.
GeneIDi20454.
KEGGimmu:20454.
UCSCiuc009chy.1. mouse. [O88829-1]

Organism-specific databases

CTDi8869.
MGIiMGI:1339963. St3gal5.

Phylogenomic databases

eggNOGiNOG257001.
GeneTreeiENSGT00760000119095.
HOVERGENiHBG056676.
InParanoidiO88829.
KOiK03370.
OMAiFFWKQVA.
OrthoDBiEOG76X609.
PhylomeDBiO88829.
TreeFamiTF352819.

Enzyme and pathway databases

ReactomeiREACT_202500. Sialic acid metabolism.

Miscellaneous databases

ChiTaRSiSt3gal5. mouse.
NextBioi298530.
PROiO88829.
SOURCEiSearch...

Gene expression databases

BgeeiO88829.
ExpressionAtlasiO88829. baseline and differential.
GenevestigatoriO88829.

Family and domain databases

InterProiIPR001675. Glyco_trans_29.
IPR012163. Sialyl_trans.
[Graphical view]
PfamiPF00777. Glyco_transf_29. 1 hit.
[Graphical view]
PIRSFiPIRSF005557. Sialyl_trans. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiSIAT9_MOUSE
AccessioniPrimary (citable) accession number: O88829
Secondary accession number(s): B2RRS1
, Q3TMT6, Q3TY01, Q91YF2, Q91YF3, Q9CZ65, Q9QWF8, Q9QWF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: May 20, 2008
Last modified: February 4, 2015
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.