ID   G3ST2_PIG               Reviewed;         398 AA.
AC   Q6XQG9;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Galactose-3-O-sulfotransferase 2;
DE            Short=Gal3ST-2;
DE            EC=2.8.2.-;
DE   AltName: Full=Beta-galactose-3-O-sulfotransferase 2;
DE   AltName: Full=Gal-beta-1, 3-GalNAc 3'-sulfotransferase 2;
GN   Name=GAL3ST2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Colon;
RA   Seko A., Yamashita K.;
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transfers a sulfate group to the hydroxyl group at C3 of non-
CC       reducing beta-galactosyl residues. Acts both on type 1 (Gal-beta-1,3-
CC       GlcNAc) and type 2 (Gal-beta-1,4-GlcNAc) chains with similar efficiency
CC       (By similarity). {ECO:0000250}.
CC   -!- ACTIVITY REGULATION: Strongly inhibited by Cu(2+) and Zn(2+).
CC       {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}.
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DR   EMBL; AY216523; AAP51033.1; -; mRNA.
DR   RefSeq; NP_998943.1; NM_213778.1.
DR   AlphaFoldDB; Q6XQG9; -.
DR   Ensembl; ENSSSCT00015103931; ENSSSCP00015043399; ENSSSCG00015076715.
DR   Ensembl; ENSSSCT00070008659; ENSSSCP00070007131; ENSSSCG00070004586.
DR   GeneID; 396666; -.
DR   KEGG; ssc:396666; -.
DR   CTD; 64090; -.
DR   InParanoid; Q6XQG9; -.
DR   OrthoDB; 1385827at2759; -.
DR   UniPathway; UPA00353; -.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Chromosome 15.
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; IBA:GO_Central.
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   GO; GO:0009101; P:glycoprotein biosynthetic process; IBA:GO_Central.
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.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..398
FT                   /note="Galactose-3-O-sulfotransferase 2"
FT                   /id="PRO_0000085205"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..29
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..398
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        77
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        133
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        180
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        288
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        330
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        360
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   398 AA;  45769 MW;  D95518EEB262BF61 CRC64;
     MLSALGGLQR CFWAILLLAL TVSLLAGFLH KDVRLLMPLL KGQAEGPPIT NVMFLKTHKT
     ASSTVLNILF RFAETHNLSV ALPAGQRVHL GYPWLFLARY VEGVEEGGPE QRFNIMCNHL
     RFNLPEVRKV MPNDTFYFSI LRNPVFQLES SFIYYKGYVP AFRDVVSLEA FLASPGTYYN
     ESQGLRNAYA RNGMWFDLGF DNNAPAEDAY VRARLADVER RFQLVLIAEH FDESMVLLRH
     LLRWRLDDVV SFPLNLRSPG SVTSLTPEGQ ERAKRWCALD WRLYQHFNRT FWARLRTELG
     PRRLRSEVAQ LQARQRELQA LCVQDGAPKN KSQITDLRLR PYQSGEADIL GYSLRPGLDN
     QTVQLCQRMV TPELQYTARL YTQQFPEKPP KNIPFLGA