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STLP1_ORYSI
ID   STLP1_ORYSI             Reviewed;         393 AA.
AC   A2WX64;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 59.
DE   RecName: Full=Sialyltransferase-like protein 1 {ECO:0000305};
DE            EC=2.4.99.- {ECO:0000305};
GN   Name=STLP1 {ECO:0000305}; ORFNames=OsI_04506 {ECO:0000312|EMBL:EAY76560.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
CC   -!- FUNCTION: Possesses sialyltransferase-like activity in vitro. Transfers
CC       sialic acid to the oligosaccharide Gal-beta-1,3-GalNAc and to
CC       glycoproteins such as asialofetuin, alpha-1-acid glycoprotein (NeuAc-
CC       alpha-2,3-Gal-beta-1,3-GalNAc-) and andasialo-alpha-1-acid
CC       glycoprotein. The transferred sialic acid is linked to galactose of
CC       Gal-beta-1,3-GalNAc through alpha-2,6-linkage.
CC       {ECO:0000250|UniProtKB:Q94DD4}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000250|UniProtKB:Q9SGD2}; Single-pass type II membrane protein
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC       {ECO:0000305}.
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DR   EMBL; CM000126; EAY76560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2WX64; -.
DR   SMR; A2WX64; -.
DR   STRING; 39946.A2WX64; -.
DR   EnsemblPlants; BGIOSGA004835-TA; BGIOSGA004835-PA; BGIOSGA004835.
DR   Gramene; BGIOSGA004835-TA; BGIOSGA004835-PA; BGIOSGA004835.
DR   HOGENOM; CLU_044787_1_0_1; -.
DR   OMA; MVCNSSH; -.
DR   Proteomes; UP000007015; Chromosome 1.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008373; F:sialyltransferase activity; IEA:EnsemblPlants.
DR   GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR   Gene3D; 3.90.1480.20; -; 1.
DR   InterPro; IPR001675; Glyco_trans_29.
DR   InterPro; IPR038578; GT29-like_sf.
DR   Pfam; PF00777; Glyco_transf_29; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW   Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..393
FT                   /note="Sialyltransferase-like protein 1"
FT                   /id="PRO_0000434313"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        9..27
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..393
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        258
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   393 AA;  43512 MW;  6B2B17E29DF77BC0 CRC64;
     MKRPLRRPFA VLLFVVLCAA ASFPSVLRRS VGPAPVLAPL PPLDPARLNA TLLRLAAADP
     SEAPLRRDVD DLLEGRLPAS SARARAWRLR GDRLHLHLRH HQFPVYRRGH HPDHDHDPLL
     HPLPRQELLL DPSLRRALRS WHRLRRHDPG VLRNLPSLLS LPGRIPSCAV VGNSGILLGA
     SHGALIDSHA AVFRLNNARI SGFAANVGAK TNLSFINSNV LHLCARRPNC FCHPYGDGVP
     ILLYICQAAH FLDVASCNAS SRSLHAASIS VTDPRLDVLC ARIVKYYSLR RFVAETGRAA
     EEWSSTRDAA MFHYSSGMQA IMVAVGVCDR VSVFGFGKAA DAKHHYHSNQ KAELDLHDYK
     AEYAFYRDLA DRPEVVPFLN DAGIAVPPVV FYH
 
 
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