SIAT2_RAT
ID SIAT2_RAT Reviewed; 525 AA.
AC Q701R3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 2;
DE Short=Alpha 2,6-ST 2;
DE EC=2.4.99.1 {ECO:0000250|UniProtKB:Q96JF0};
DE AltName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 2;
DE AltName: Full=ST6Gal II;
DE Short=ST6GalII;
DE AltName: Full=Sialyltransferase 2;
GN Name=St6gal2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar;
RX PubMed=15843597; DOI=10.1093/glycob/cwi063;
RA Harduin-Lepers A., Mollicone R., Delannoy P., Oriol R.;
RT "The animal sialyltransferases and sialyltransferase-related genes: a
RT phylogenetic approach.";
RL Glycobiology 15:805-817(2005).
CC -!- FUNCTION: Transfers sialic acid from the donor of substrate CMP-sialic
CC acid to galactose containing acceptor substrates. Has alpha-2,6-
CC sialyltransferase activity toward oligosaccharides that have the Gal-
CC beta-1,4-GlcNAc sequence at the non-reducing end of their carbohydrate
CC groups, but it has weak or no activities toward glycoproteins and
CC glycolipids. {ECO:0000250|UniProtKB:Q96JF0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-
CC acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP +
CC H(+); Xref=Rhea:RHEA:52104, ChEBI:CHEBI:15378, ChEBI:CHEBI:28034,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:136398;
CC EC=2.4.99.1; Evidence={ECO:0000250|UniProtKB:Q96JF0};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; AJ627626; CAF29494.1; -; mRNA.
DR RefSeq; NP_001094358.1; NM_001100888.1.
DR RefSeq; XP_006244322.1; XM_006244260.3.
DR RefSeq; XP_006244326.1; XM_006244264.3.
DR RefSeq; XP_006244327.1; XM_006244265.3.
DR RefSeq; XP_008764978.1; XM_008766756.2.
DR RefSeq; XP_008764979.1; XM_008766757.2.
DR RefSeq; XP_017451813.1; XM_017596324.1.
DR AlphaFoldDB; Q701R3; -.
DR SMR; Q701R3; -.
DR STRING; 10116.ENSRNOP00000067395; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; Q701R3; 3 sites.
DR iPTMnet; Q701R3; -.
DR PhosphoSitePlus; Q701R3; -.
DR PaxDb; Q701R3; -.
DR Ensembl; ENSRNOT00000072796; ENSRNOP00000067395; ENSRNOG00000046515.
DR GeneID; 301155; -.
DR KEGG; rno:301155; -.
DR CTD; 84620; -.
DR RGD; 1559663; St6gal2.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000158714; -.
DR HOGENOM; CLU_038334_1_0_1; -.
DR InParanoid; Q701R3; -.
DR OMA; WRQRMLC; -.
DR OrthoDB; 494294at2759; -.
DR PhylomeDB; Q701R3; -.
DR BRENDA; 2.4.99.1; 5301.
DR Reactome; R-RNO-4085001; Sialic acid metabolism.
DR PRO; PR:Q701R3; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000046515; Expressed in frontal cortex.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003835; F:beta-galactoside alpha-2,6-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008373; F:sialyltransferase activity; ISO:RGD.
DR GO; GO:0009311; P:oligosaccharide metabolic process; ISS:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR GO; GO:0097503; P:sialylation; IBA:GO_Central.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..525
FT /note="Beta-galactoside alpha-2,6-sialyltransferase 2"
FT /id="PRO_0000314788"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..525
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 85..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 521
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 249..515
FT /evidence="ECO:0000250"
FT DISULFID 292..444
FT /evidence="ECO:0000250"
FT DISULFID 462..473
FT /evidence="ECO:0000250"
SQ SEQUENCE 525 AA; 59917 MW; E68DE58A6F73634F CRC64;
MKPHLKQWRQ RMLFAIFVWG LLFLAIFIYF TNSNPAAPMP SSFSFLESRG LLPVQGKQRV
IMGALQEPSL PRSLEPSKVL MDGHSASPFN SWPGDPQKGD QAQDGFDNGD EFFTSQVGRK
SQSAFYPEED NYFFVAGQPG LYHHRQGALG LPSPGESSWQ SGPGQPKQEK LRHPRRGSLP
EEAYDSDMLS TSMSRAFLYR LWKGTVSSKM LNPRLQKAMR YYMSFNKHGV RFSRRGRREA
RRTGPELLCE MRKRVRVRTL DGKEAPFSGL GWRPLVPGVP LSQLHPRGLR SCAVVMSAGA
ILNSSLGEEI DSHDAVLRFN SAPTRGYEKD VGNKTTVRII NSQILANPSH HFIDSSLYKD
VILVAWDPAP YSANLNLWYK KPDYNLFTPY IQHRLKYPTQ PFYILHPKFI WQLWDIIQEN
TREKIQPNPP SSGFIGILVM MSMCQEVHVY EYIPSVRQTE LCHYHELYYD AACTLGAYHP
LLYEKLLVQR LNTGTQADLH HKGKVVLPGF QTLRCPVTRP NNTNT
