ID   G3ST3_MOUSE             Reviewed;         431 AA.
AC   P61315;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Galactose-3-O-sulfotransferase 3;
DE            Short=Gal3ST-3;
DE            EC=2.8.2.-;
DE   AltName: Full=Beta-galactose-3-O-sulfotransferase 3;
DE   AltName: Full=Gal-beta-1, 3-GalNAc 3'-sulfotransferase 3;
GN   Name=Gal3st3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Transfers a sulfate to position 3 of non-reducing beta-
CC       galactosyl residues in N-glycans and core2-branched O-glycans. Has high
CC       activity towards Gal-beta-1,4-GlcNAc, Gal-beta-1,4(Fuc-alpha-1,3)GlcNAc
CC       and lower activity towards Gal-beta-1,3(Fuc-alpha-1,4)GlcNAc (By
CC       similarity). {ECO:0000250}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Protein modification; carbohydrate sulfation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the galactose-3-O-sulfotransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC066996; AAH66996.1; -; mRNA.
DR   CCDS; CCDS29455.1; -.
DR   RefSeq; NP_001019888.1; NM_001024717.2.
DR   AlphaFoldDB; P61315; -.
DR   STRING; 10090.ENSMUSP00000061517; -.
DR   GlyConnect; 2317; 3 N-Linked glycans (3 sites).
DR   GlyGen; P61315; 4 sites, 2 N-linked glycans (3 sites).
DR   PhosphoSitePlus; P61315; -.
DR   MaxQB; P61315; -.
DR   PaxDb; P61315; -.
DR   PRIDE; P61315; -.
DR   ProteomicsDB; 271625; -.
DR   Antibodypedia; 2654; 45 antibodies from 15 providers.
DR   Ensembl; ENSMUST00000061169; ENSMUSP00000061517; ENSMUSG00000047658.
DR   GeneID; 545276; -.
DR   KEGG; mmu:545276; -.
DR   UCSC; uc008gco.2; mouse.
DR   CTD; 89792; -.
DR   MGI; MGI:3617843; Gal3st3.
DR   VEuPathDB; HostDB:ENSMUSG00000047658; -.
DR   eggNOG; ENOG502QPNT; Eukaryota.
DR   GeneTree; ENSGT00950000182923; -.
DR   HOGENOM; CLU_040616_1_0_1; -.
DR   InParanoid; P61315; -.
DR   OMA; PDEKDSM; -.
DR   OrthoDB; 1385827at2759; -.
DR   PhylomeDB; P61315; -.
DR   TreeFam; TF314802; -.
DR   UniPathway; UPA00353; -.
DR   BioGRID-ORCS; 545276; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Gal3st3; mouse.
DR   PRO; PR:P61315; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; P61315; protein.
DR   Bgee; ENSMUSG00000047658; Expressed in Ammon's horn and 39 other tissues.
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:0050694; F:galactose 3-O-sulfotransferase activity; ISO:MGI.
DR   GO; GO:0001733; F:galactosylceramide sulfotransferase activity; IEA:InterPro.
DR   GO; GO:0008146; F:sulfotransferase activity; IBA:GO_Central.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR009729; Gal-3-0_sulfotransfrase.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR14647; PTHR14647; 1.
DR   Pfam; PF06990; Gal-3-0_sulfotr; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Golgi apparatus; Magnesium; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..431
FT                   /note="Galactose-3-O-sulfotransferase 3"
FT                   /id="PRO_0000085207"
FT   TOPO_DOM        1..19
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        20..40
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        41..431
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   REGION          400..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        177
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   431 AA;  49277 MW;  4D8FE6B50242E037 CRC64;
     MPPILQRLQQ STKMMSHRKI LLLVLGCSTV SLLIHQGSQL SWYPKLFPLS CPPLRESPPR
     AKHMAVAFLK THKTAGTTVQ NILFRFAERH NLTVALPHPS CEHQFCYPRN FSAHFVHPAT
     RPPHMLASHL RFDRAELERL MPPDTIYVTI LREPAAMFES LFSYYNQYCP AFRRVPNASL
     ETFLRAPEAY YRPGEHFAMF AHNTLAYDLG GDNERSPRDD AAYLAGLIRQ VEEVFSLVMI
     AEYFDESLVL LRRLLAWDLD DVLYAKLNAR AASSRLATIP EALARAARTW NALDAGLYDH
     FNATFWRRVA RAGRACVERE ARELREARQR LLRRCFGDEP VLRPAAQIRT KQLQPWQPSR
     KVDIMGYDLP SGGAGPTTEA CLKLAMPEVQ YSNYLLRKQK RRGGVRSRPE SVLDNPPPRP
     IRALPRIPQG T