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B3GN5_PIG
ID   B3GN5_PIG               Reviewed;         377 AA.
AC   Q864U8;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase;
DE            EC=2.4.1.206 {ECO:0000250|UniProtKB:Q8BGY6};
DE   AltName: Full=Lactotriaosylceramide synthase;
DE            Short=Lc(3)Cer synthase;
DE            Short=Lc3 synthase;
DE   AltName: Full=UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5;
DE            Short=BGnT-5;
DE            Short=Beta-1,3-Gn-T5;
DE            Short=Beta-1,3-N-acetylglucosaminyltransferase 5;
DE            Short=Beta3Gn-T5;
GN   Name=B3GNT5;
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=Small intestine;
RX   PubMed=16130451; DOI=10.1111/j.1439-0388.2005.00490.x;
RA   Python P., Jorg H., Neuenschwander S., Asai-Coakwell M., Hagger C.,
RA   Burgi E., Bertschinger H.U., Stranzinger G., Vogeli P.;
RT   "Inheritance of the F4ab, F4ac and F4ad E. coli receptors in swine and
RT   examination of four candidate genes for F4acR.";
RL   J. Anim. Breed. Genet. 122:5-14(2005).
CC   -!- FUNCTION: Beta-1,3-N-acetylglucosaminyltransferase that plays a key
CC       role in the synthesis of lacto- or neolacto-series carbohydrate chains
CC       on glycolipids, notably by participating in biosynthesis of HNK-1 and
CC       Lewis X carbohydrate structures. Has strong activity toward
CC       lactosylceramide (LacCer) and neolactotetraosylceramide (nLc(4)Cer;
CC       paragloboside), resulting in the synthesis of Lc(3)Cer and
CC       neolactopentaosylceramide (nLc(5)Cer), respectively. Probably plays a
CC       central role in regulating neolacto-series glycolipid synthesis during
CC       embryonic development. {ECO:0000250|UniProtKB:Q9BYG0}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + UDP-N-
CC         acetyl-alpha-D-glucosamine = a beta-D-GlcNAc-(1->3)-beta-D-Gal-
CC         (1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H(+) + UDP;
CC         Xref=Rhea:RHEA:13905, ChEBI:CHEBI:15378, ChEBI:CHEBI:17103,
CC         ChEBI:CHEBI:17950, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223;
CC         EC=2.4.1.206; Evidence={ECO:0000250|UniProtKB:Q9BYG0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13906;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYG0};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a neolactoside nLc4Cer(d18:1(4E)) + UDP-N-acetyl-alpha-D-
CC         glucosamine = a neolactoside IV(3)-beta-GlcNAc-nLc4Cer(d18:1(4E)) +
CC         H(+) + UDP; Xref=Rhea:RHEA:23004, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17006, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:142448; Evidence={ECO:0000250|UniProtKB:Q9BYG0};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23005;
CC         Evidence={ECO:0000250|UniProtKB:Q9BYG0};
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC       {ECO:0000305}.
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DR   EMBL; AY253338; AAO92023.1; -; mRNA.
DR   RefSeq; NP_999492.1; NM_214327.1.
DR   RefSeq; XP_005670075.1; XM_005670018.2.
DR   RefSeq; XP_013837686.1; XM_013982232.1.
DR   RefSeq; XP_013837687.1; XM_013982233.1.
DR   RefSeq; XP_013837688.1; XM_013982234.1.
DR   RefSeq; XP_013837689.1; XM_013982235.1.
DR   RefSeq; XP_013837690.1; XM_013982236.1.
DR   RefSeq; XP_013837691.1; XM_013982237.1.
DR   AlphaFoldDB; Q864U8; -.
DR   SMR; Q864U8; -.
DR   STRING; 9823.ENSSSCP00000023905; -.
DR   CAZy; GT31; Glycosyltransferase Family 31.
DR   PaxDb; Q864U8; -.
DR   PRIDE; Q864U8; -.
DR   Ensembl; ENSSSCT00000030536; ENSSSCP00000023905; ENSSSCG00000024393.
DR   Ensembl; ENSSSCT00000040962; ENSSSCP00000051412; ENSSSCG00000024393.
DR   Ensembl; ENSSSCT00000053206; ENSSSCP00000043405; ENSSSCG00000024393.
DR   Ensembl; ENSSSCT00000067752; ENSSSCP00000068897; ENSSSCG00000024393.
DR   Ensembl; ENSSSCT00005040685; ENSSSCP00005024891; ENSSSCG00005025642.
DR   Ensembl; ENSSSCT00005040711; ENSSSCP00005024908; ENSSSCG00005025642.
DR   Ensembl; ENSSSCT00005040722; ENSSSCP00005024917; ENSSSCG00005025642.
DR   Ensembl; ENSSSCT00015030812; ENSSSCP00015012195; ENSSSCG00015023174.
DR   Ensembl; ENSSSCT00015030861; ENSSSCP00015012214; ENSSSCG00015023174.
DR   Ensembl; ENSSSCT00015030976; ENSSSCP00015012261; ENSSSCG00015023174.
DR   Ensembl; ENSSSCT00015031019; ENSSSCP00015012274; ENSSSCG00015023174.
DR   Ensembl; ENSSSCT00025051345; ENSSSCP00025021908; ENSSSCG00025037728.
DR   Ensembl; ENSSSCT00025051355; ENSSSCP00025021914; ENSSSCG00025037728.
DR   Ensembl; ENSSSCT00025051367; ENSSSCP00025021918; ENSSSCG00025037728.
DR   Ensembl; ENSSSCT00025051373; ENSSSCP00025021920; ENSSSCG00025037728.
DR   Ensembl; ENSSSCT00030051330; ENSSSCP00030023364; ENSSSCG00030036904.
DR   Ensembl; ENSSSCT00030051373; ENSSSCP00030023388; ENSSSCG00030036904.
DR   Ensembl; ENSSSCT00030051391; ENSSSCP00030023397; ENSSSCG00030036904.
DR   Ensembl; ENSSSCT00030051407; ENSSSCP00030023407; ENSSSCG00030036904.
DR   Ensembl; ENSSSCT00035098954; ENSSSCP00035041843; ENSSSCG00035073064.
DR   Ensembl; ENSSSCT00035098963; ENSSSCP00035041850; ENSSSCG00035073064.
DR   Ensembl; ENSSSCT00035098971; ENSSSCP00035041852; ENSSSCG00035073064.
DR   Ensembl; ENSSSCT00035098978; ENSSSCP00035041858; ENSSSCG00035073064.
DR   Ensembl; ENSSSCT00040056034; ENSSSCP00040023295; ENSSSCG00040041893.
DR   Ensembl; ENSSSCT00040056129; ENSSSCP00040023340; ENSSSCG00040041893.
DR   Ensembl; ENSSSCT00040056165; ENSSSCP00040023356; ENSSSCG00040041893.
DR   Ensembl; ENSSSCT00040056203; ENSSSCP00040023374; ENSSSCG00040041893.
DR   Ensembl; ENSSSCT00045036520; ENSSSCP00045025426; ENSSSCG00045021347.
DR   Ensembl; ENSSSCT00045036554; ENSSSCP00045025455; ENSSSCG00045021347.
DR   Ensembl; ENSSSCT00045036584; ENSSSCP00045025469; ENSSSCG00045021347.
DR   Ensembl; ENSSSCT00045036611; ENSSSCP00045025484; ENSSSCG00045021347.
DR   Ensembl; ENSSSCT00050081803; ENSSSCP00050035125; ENSSSCG00050060042.
DR   Ensembl; ENSSSCT00050081808; ENSSSCP00050035127; ENSSSCG00050060042.
DR   Ensembl; ENSSSCT00050081809; ENSSSCP00050035128; ENSSSCG00050060042.
DR   Ensembl; ENSSSCT00050081814; ENSSSCP00050035130; ENSSSCG00050060042.
DR   Ensembl; ENSSSCT00055004738; ENSSSCP00055003665; ENSSSCG00055002483.
DR   Ensembl; ENSSSCT00055004747; ENSSSCP00055003673; ENSSSCG00055002483.
DR   Ensembl; ENSSSCT00055004750; ENSSSCP00055003675; ENSSSCG00055002483.
DR   Ensembl; ENSSSCT00055004758; ENSSSCP00055003682; ENSSSCG00055002483.
DR   Ensembl; ENSSSCT00060073825; ENSSSCP00060031827; ENSSSCG00060054230.
DR   Ensembl; ENSSSCT00060073836; ENSSSCP00060031831; ENSSSCG00060054230.
DR   Ensembl; ENSSSCT00060073843; ENSSSCP00060031835; ENSSSCG00060054230.
DR   Ensembl; ENSSSCT00060073853; ENSSSCP00060031840; ENSSSCG00060054230.
DR   Ensembl; ENSSSCT00065070200; ENSSSCP00065030589; ENSSSCG00065051251.
DR   Ensembl; ENSSSCT00065070203; ENSSSCP00065030591; ENSSSCG00065051251.
DR   Ensembl; ENSSSCT00065070210; ENSSSCP00065030596; ENSSSCG00065051251.
DR   Ensembl; ENSSSCT00065070213; ENSSSCP00065030598; ENSSSCG00065051251.
DR   Ensembl; ENSSSCT00070040372; ENSSSCP00070033857; ENSSSCG00070020341.
DR   Ensembl; ENSSSCT00070040376; ENSSSCP00070033860; ENSSSCG00070020341.
DR   Ensembl; ENSSSCT00070040377; ENSSSCP00070033861; ENSSSCG00070020341.
DR   GeneID; 397599; -.
DR   KEGG; ssc:397599; -.
DR   CTD; 84002; -.
DR   VGNC; VGNC:85726; B3GNT5.
DR   eggNOG; KOG2287; Eukaryota.
DR   GeneTree; ENSGT00940000159676; -.
DR   HOGENOM; CLU_036849_2_4_1; -.
DR   InParanoid; Q864U8; -.
DR   OrthoDB; 1037602at2759; -.
DR   TreeFam; TF318639; -.
DR   Reactome; R-SSC-913709; O-linked glycosylation of mucins.
DR   UniPathway; UPA00378; -.
DR   Proteomes; UP000008227; Chromosome 13.
DR   Proteomes; UP000314985; Chromosome 13.
DR   Bgee; ENSSSCG00000024393; Expressed in epididymis and 41 other tissues.
DR   ExpressionAtlas; Q864U8; baseline and differential.
DR   Genevisible; Q864U8; SS.
DR   GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008457; F:beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0047256; F:lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0007420; P:brain development; IBA:GO_Central.
DR   GO; GO:0007417; P:central nervous system development; ISS:UniProtKB.
DR   GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR   InterPro; IPR002659; Glyco_trans_31.
DR   PANTHER; PTHR11214; PTHR11214; 1.
DR   Pfam; PF01762; Galactosyl_T; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW   Lipid metabolism; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..377
FT                   /note="Lactosylceramide 1,3-N-acetyl-beta-D-
FT                   glucosaminyltransferase"
FT                   /id="PRO_0000289211"
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..377
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        166
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   377 AA;  43971 MW;  F09DD970FE5DAC03 CRC64;
     MFGSGRRVKK WQFIQIFATC FVLSLMFFWG PIDNHIVSHM KSYSYRYLIN SYDFVNDSLS
     LKRSEDGTPR YQYLINHEEK CQAQDVLLLL FVKTAPENYN RRSAIRNTWG NEKYVQSQLN
     ANIKTLFVLG TPSDPLMRER LQRRLVWEDH MYSDIIQQDF VDSFYNLTLK FLLQFKWANS
     FCPHAKFLMT ADDDIFIHMP NLIEYLQSLE QMGVQDFWIG RVHHGAPPVR DKSSKYYVSY
     DMYQWPAYPD YTAGAAYVIS GDVATKVYEA SQTLNSSLYI DDVFMGLCAN KIGLVPQSHA
     FFSGEGKTPY HPCIYEKMMT SHGHVEDLQD LWKDATDPKV KMISKGFFGQ IYCRIIKIVL
     LCKLTYLDTY PCRAAFA
 
 
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