ID I3M5D1_ICTTR Unreviewed; 987 AA.
AC I3M5D1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Beta-1,4-N-acetylgalactosaminyltransferase {ECO:0000256|RuleBase:RU364016};
DE EC=2.4.1.244 {ECO:0000256|RuleBase:RU364016};
GN Name=B4GALNT3 {ECO:0000313|Ensembl:ENSSTOP00000004526.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000004526.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000004526.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to
CC N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-
CC diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked
CC glycans and probably O-linked glycans. {ECO:0000256|RuleBase:RU364016}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-
CC alpha-D-galactosamine = an N-acetyl-beta-D-galactosaminyl-(1->4)-N-
CC acetyl-beta-D-glucosaminyl derivative + H(+) + UDP;
CC Xref=Rhea:RHEA:20493, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:61631, ChEBI:CHEBI:67138, ChEBI:CHEBI:138027;
CC EC=2.4.1.244; Evidence={ECO:0000256|RuleBase:RU364016};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000256|RuleBase:RU364016}; Single-pass type II membrane protein
CC {ECO:0000256|RuleBase:RU364016}. Membrane
CC {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the chondroitin N-
CC acetylgalactosaminyltransferase family. {ECO:0000256|ARBA:ARBA00009239,
CC ECO:0000256|RuleBase:RU364016}.
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DR EMBL; AGTP01074421; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074422; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074424; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01074426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3M5D1; -.
DR STRING; 43179.ENSSTOP00000004526; -.
DR Ensembl; ENSSTOT00000005046.3; ENSSTOP00000004526.3; ENSSTOG00000005026.3.
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR HOGENOM; CLU_011195_1_0_1; -.
DR InParanoid; I3M5D1; -.
DR TreeFam; TF318303; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0047238; F:glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase activity; IEA:UniProt.
DR GO; GO:0033842; F:N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IEA:UniProt.
DR InterPro; IPR008428; Chond_GalNAc.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR PANTHER; PTHR12369:SF15; BETA-1,4-N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 1.
DR PANTHER; PTHR12369; CHONDROITIN SYNTHASE; 1.
DR Pfam; PF05679; CHGN; 1.
DR Pfam; PF07691; PA14; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR PROSITE; PS51820; PA14; 1.
PE 3: Inferred from homology;
KW Golgi apparatus {ECO:0000256|RuleBase:RU364016};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Signal-anchor {ECO:0000256|RuleBase:RU364016};
KW Transferase {ECO:0000256|RuleBase:RU364016};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 117..279
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 301..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 113728 MW; 4DADBC75EA910B01 CRC64;
MGSPRAALLL LLLRPVKLLR RRFRLLLVLA VVSVGLWTLY LELVASAQVG GNPLNRRYGS
WRELAKALAS RNIPAVDPNI QFYRPQRLNL KDQEIDQSGN SNNSYLRWNK PVPWLSEFRG
RANLHVFEDW CGTSIQQLRR NLHFPLYPHI RTTLRKLAVS PKWTNYGLRI FGYLHPFTDG
KIQFAIAADD NAEFWLSRDD QVSGLQLLAS VGKTGKEWTA PGEFGKFRSQ ISKPVSLSAS
HRYYFEVLHK QNDEGTDHVE VAWRRNDPGA KFTIIDSPSL SLFTNETILR MDEVGHIPQT
AASHVGSSDP LARDEQPPAD MLRPDPRDTL YQVPLIPKSH LRHILPDCPY KPSYLVDGLP
LQRYQGLRFV HLSFVYPNDY TRLSHMETHN KCFYQENQQP SLSSWEKIEN SDEEWLLLTG
FEEDLLEESQ YEEVAEETPA SQDQDTRIRE GKQTVASVPG QEVTDYRLRS LRKLLAQPQG
APLPPISKHN STGPFPVRAS DIPVLSPRKP SPEPSRDSPH SDKRAPGNLP QIKRPRPTGD
QPQKALEQSQ WLNQVESYIA EQRRGDRMEP LAPKWGWHGE EEVVAAAGQE GQAEGEEEGE
EEEEEDMSEV FEYVPVFDPV VNWDQTFSAR NLDFQALRTD WIDLNCNTSG NLLLPEQEAL
EVTRVFLKKL NQRSRGRYQL QRIVNVEKRQ DQLRGGRYLL ELELLEQGQR LVRLSEYVST
RGWQGVDPAG GEETEARNLQ GLVWSPHRRR RHVLNARDPE PKLCWPQGFS WNHRAVVHFV
VPVKNQARWV QQFIRDMENL FQVTSDPHFN IIITDYSSED MDIETALKRS KLRSYQYMKL
SGNFERSAGL QAGIDLVKDP HSIIFLCDLH IHFPAGVIDT IRKHCVEGKM AFAPMVMRLH
CGATPQWPEG YWEVNGFGLL GIYKSDLDKI GGMNTKEFRD RWGGEDWELL DRILQAGLEV
ERLSLRNFFH HFHSKRGMWN RRQMKMP
//
