ID H2PYV6_PANTR Unreviewed; 372 AA.
AC H2PYV6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Beta-1,4-galactosyltransferase {ECO:0000256|RuleBase:RU368121};
DE Short=Beta-1,4-GalTase {ECO:0000256|RuleBase:RU368121};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU368121};
GN Name=B4GALT2 {ECO:0000313|Ensembl:ENSPTRP00000001130.6,
GN ECO:0000313|VGNC:VGNC:8909};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000001130.6, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000001130.6, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000001130.6}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Responsible for the synthesis of complex-type N-linked
CC oligosaccharides in many glycoproteins as well as the carbohydrate
CC moieties of glycolipids. {ECO:0000256|RuleBase:RU368121}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|RuleBase:RU368121};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000256|ARBA:ARBA00004922, ECO:0000256|RuleBase:RU368121}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU368121}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU368121}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 7 family.
CC {ECO:0000256|ARBA:ARBA00005735, ECO:0000256|RuleBase:RU368121}.
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DR EMBL; AACZ04032999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003308088.2; XM_003308040.3.
DR RefSeq; XP_009454106.2; XM_009455831.2.
DR RefSeq; XP_016816543.1; XM_016961054.1.
DR RefSeq; XP_016816548.1; XM_016961059.1.
DR RefSeq; XP_016816558.1; XM_016961069.1.
DR AlphaFoldDB; H2PYV6; -.
DR Ensembl; ENSPTRT00000001243.6; ENSPTRP00000001130.6; ENSPTRG00000000649.6.
DR GeneID; 456522; -.
DR KEGG; ptr:456522; -.
DR CTD; 8704; -.
DR VGNC; VGNC:8909; B4GALT2.
DR eggNOG; KOG3916; Eukaryota.
DR GeneTree; ENSGT00940000159367; -.
DR HOGENOM; CLU_044391_0_0_1; -.
DR OMA; RPMYTNV; -.
DR OrthoDB; 306273at2759; -.
DR TreeFam; TF312834; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000002277; Chromosome 1.
DR Bgee; ENSPTRG00000000649; Expressed in superior frontal gyrus and 21 other cell types or tissues.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniRule.
DR CDD; cd00899; b4GalT; 1.
DR InterPro; IPR003859; Galactosyl_T.
DR InterPro; IPR027791; Galactosyl_T_C.
DR InterPro; IPR027995; Galactosyl_T_N.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR19300; BETA-1,4-GALACTOSYLTRANSFERASE; 1.
DR PANTHER; PTHR19300:SF32; BETA-1,4-GALACTOSYLTRANSFERASE 2; 1.
DR Pfam; PF02709; Glyco_transf_7C; 1.
DR Pfam; PF13733; Glyco_transf_7N; 1.
DR PRINTS; PR02050; B14GALTRFASE.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW ECO:0000256|RuleBase:RU368121};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU368121};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU368121}; Manganese {ECO:0000256|RuleBase:RU368121};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU368121};
KW Metal-binding {ECO:0000256|RuleBase:RU368121};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW ECO:0000256|RuleBase:RU368121};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU368121};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU368121};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU368121}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU368121"
FT DOMAIN 97..230
FT /note="Galactosyltransferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13733"
FT DOMAIN 235..312
FT /note="Galactosyltransferase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02709"
FT REGION 56..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 372 AA; 41974 MW; B0ACBCFF4D7BDD9A CRC64;
MSRLLGGTLE RVCKAVLLLC LLHFLVAVIL YFDVYAQHLA FFSRFSARGP AHALHPAASS
SSSSSNCSRP NATASSSGLP EVPSALPGPT APMLPPCPDS PPGLVGRLLI EFTSPMPLER
VQRENPGVLM GGRYTPPDCT PAQTVAVIIP FRHREHHLRY WLHYLHPILR RQRLRYGVYV
INQHGEDTFN RAKLLNVGFL EALKEDAAYD CFIFSDVDLV PMDDRNLYRC GDQPRHFAIA
MDKFGFRLPY AGYFGGVSGL SKAQFLKING FPNEYWGWGG EDDDIFNRIS LTGMKISRPD
IRIGRYRMIK HDRDKHNEPN PQRFTKIQNT KLTMKRDGIG SVRYQVLEVS RQPLFTNITV
DIGRPPSWPP RG
//
