ID   SIA4B_RAT               Reviewed;         350 AA.
AC   Q11205;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-APR-2013, entry version 88.
DE   RecName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2;
DE            Short=Alpha 2,3-ST 2;
DE            Short=Beta-galactoside alpha-2,3-sialyltransferase 2;
DE            EC=2.4.99.4;
DE   AltName: Full=Gal-NAc6S;
DE   AltName: Full=Gal-beta-1,3-GalNAc-alpha-2,3-sialyltransferase;
DE   AltName: Full=ST3Gal II;
DE            Short=ST3GalII;
DE   AltName: Full=ST3GalA.2;
DE   AltName: Full=Sialyltransferase 4B;
DE            Short=SIAT4-B;
GN   Name=St3gal2; Synonyms=Siat4b, Siat5;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8144500;
RA   Lee Y.-C., Kojima N., Wada E., Kurosawa N., Nakaoka T., Hamamoto T.,
RA   Tsuji S.;
RT   "Cloning and expression of cDNA for a new type of Gal beta 1,3GalNAc
RT   alpha 2,3-sialyltransferase.";
RL   J. Biol. Chem. 269:10028-10033(1994).
CC   -!- FUNCTION: It may be responsible for the synthesis of the sequence
CC       NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- found in terminal
CC       carbohydrate groups of certain glycoproteins, oligosaccharides and
CC       glycolipids. SIAT4A and SIAT4B sialylate the same acceptor
CC       substrates but exhibit different Km values.
CC   -!- CATALYTIC ACTIVITY: CMP-N-acetylneuraminate + beta-D-galactosyl-
CC       1,3-N-acetyl-alpha-D-galactosaminyl-R = CMP + alpha-N-
CC       acetylneuraminyl-2,3-beta-D-galactosyl-1,3-N-acetyl-alpha-D-
CC       galactosaminyl-R.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane;
CC       Single-pass type II membrane protein. Secreted. Note=Membrane-
CC       bound form in trans cisternae of Golgi. Secreted into the body
CC       fluid.
CC   -!- PTM: The soluble form derives from the membrane form by
CC       proteolytic processing.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
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DR   EMBL; X76988; CAA54293.1; -; mRNA.
DR   IPI; IPI00210638; -.
DR   PIR; B54420; B54420.
DR   RefSeq; NP_113883.2; NM_031695.2.
DR   UniGene; Rn.33216; -.
DR   STRING; 10116.ENSRNOP00000024248; -.
DR   CAZy; GT29; Glycosyltransferase Family 29.
DR   PRIDE; Q11205; -.
DR   GeneID; 64442; -.
DR   KEGG; rno:64442; -.
DR   UCSC; RGD:68413; rat.
DR   CTD; 6483; -.
DR   RGD; 68413; St3gal2.
DR   eggNOG; NOG249462; -.
DR   HOGENOM; HOG000126811; -.
DR   HOVERGEN; HBG054227; -.
DR   InParanoid; Q11205; -.
DR   KO; K03368; -.
DR   OrthoDB; EOG4PNXH3; -.
DR   UniPathway; UPA00378; -.
DR   NextBio; 613166; -.
DR   Genevestigator; Q11205; -.
DR   GermOnline; ENSRNOG00000017932; Rattus norvegicus.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030173; C:integral to Golgi membrane; IEA:InterPro.
DR   GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IEA:EC.
DR   GO; GO:0008373; F:sialyltransferase activity; IDA:RGD.
DR   GO; GO:0006486; P:protein glycosylation; IDA:RGD.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR012163; Sialyl_trans.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   PIRSF; PIRSF005557; Sialyl_trans; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Membrane; Reference proteome; Secreted;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN         1    350       CMP-N-acetylneuraminate-beta-
FT                                galactosamide-alpha-2,3-sialyltransferase
FT                                2.
FT                                /FTId=PRO_0000149261.
FT   TOPO_DOM      1      6       Cytoplasmic (Potential).
FT   TRANSMEM      7     27       Helical; Signal-anchor for type II
FT                                membrane protein; (Potential).
FT   TOPO_DOM     28    350       Lumenal (Potential).
FT   CARBOHYD     92     92       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    211    211       N-linked (GlcNAc...) (Potential).
FT   DISULFID    152    291       By similarity.
SQ   SEQUENCE   350 AA;  40166 MW;  87E6494FB02D0BE1 CRC64;
     MKCSLRVWFL SMAFLLVFIM SLLFTYSHHS MATLPYLDSG TLGGTHRVKL VPGYTGQQRL
     VKEGLSGKSC TCSRCMGDAG TSEWFDSHFD SNISPVWTRD NMNLTPDVQR WWMMLQPQFK
     SHNTNEVLEK LFQIVPGENP YRFRDPQQCR RCAVVGNSGN LRGSGYGQEV DSHNFIMRMN
     QAPTVGFEKD VGSRTTHHFM YPESAKNLPA NVSFVLVPFK ALDLMWIASA LSTGQIRFTY
     APVKSFLRVD KEKVQIYNPA FFKYIHDRWT EHHGRYPSTG MLVLFFALHV CDEVNVYGFG
     ADSRGNWHHY WENNRYAGEF RKTGVHDADF EAHIIDILAK ASKIEVYRGN
//

ID   G3V8B2_RAT              Unreviewed;       350 AA.
AC   G3V8B2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   03-APR-2013, entry version 11.
DE   SubName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2;
DE   SubName: Full=ST3 beta-galactoside alpha-2,3-sialyltransferase 2, isoform CRA_a;
GN   Name=St3gal2; ORFNames=rCG_51602;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN;
RX   PubMed=15632090; DOI=10.1101/gr.2889405;
RA   Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA   Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA   Istrail S., Li P., Sutton G.;
RT   "Gene and alternative splicing annotation with AIR.";
RL   Genome Res. 15:54-66(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN;
RA   Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA   Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA   Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L.,
RA   Lu F., Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C.,
RA   Sutton G.G., Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway;
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
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DR   EMBL; AABR06098696; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH473972; EDL92552.1; -; Genomic_DNA.
DR   EMBL; CH473972; EDL92553.1; -; Genomic_DNA.
DR   RefSeq; NP_113883.2; NM_031695.2.
DR   UniGene; Rn.33216; -.
DR   Ensembl; ENSRNOT00000024248; ENSRNOP00000024248; ENSRNOG00000017932.
DR   GeneID; 64442; -.
DR   KEGG; rno:64442; -.
DR   CTD; 6483; -.
DR   RGD; 68413; St3gal2.
DR   GeneTree; ENSGT00620000087743; -.
DR   KO; K03368; -.
DR   OMA; DVQRWWM; -.
DR   NextBio; 613166; -.
DR   GO; GO:0030173; C:integral to Golgi membrane; IEA:InterPro.
DR   GO; GO:0003836; F:beta-galactoside (CMP) alpha-2,3-sialyltransferase activity; IEA:Compara.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR012163; Sialyl_trans.
DR   Pfam; PF00777; Glyco_transf_29; 1.
DR   PIRSF; PIRSF005557; Sialyl_trans; 1.
PE   4: Predicted;
KW   Complete proteome; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Transferase; Transmembrane; Transmembrane helix.
SQ   SEQUENCE   350 AA;  40184 MW;  87E6494FB0281FE1 CRC64;
     MKCSLRVWFL SMAFLLVFIM SLLFTYSHHS MATLPYLDSG TLGGTHRVKL VPGYTGQQRL
     VKEGLSGKSC TCSRCMGDAG TSEWFDSHFD SNISPVWTRD NMNLTPDVQR WWMMLQPQFK
     SHNTNEVLEK LFQIVPGENP YRFRDPQQCR RCAVVGNSGN LRGSGYGQEV DSHNFIMRMN
     QAPTVGFEKD VGSRTTHHFM YPESAKNLPA NVSFVLVPFK ALDLMWIASA LSTGQIRFTY
     APVKSFLRVD KEKVQIYNPA FFKYIHDRWT EHHGRYPSTG MLVLFFALHV CDEVNVYGFG
     ADSRGNWHHY WENNRYAGEF RKTGVHDADF EAHIIDMLAK ASKIEVYRGN
//