ID G1SV46_RABIT Unreviewed; 999 AA.
AC G1SV46;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 67.
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:ENSOCUP00000007277.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000007277.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000007277.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000007277.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000007277.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000007277.3};
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; AAGW02051708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02051709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02051710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02051711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02051712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002712828.1; XM_002712782.3.
DR AlphaFoldDB; G1SV46; -.
DR SMR; G1SV46; -.
DR STRING; 9986.ENSOCUP00000007277; -.
DR PaxDb; 9986-ENSOCUP00000007277; -.
DR Ensembl; ENSOCUT00000008422.4; ENSOCUP00000007277.3; ENSOCUG00000008418.4.
DR GeneID; 100351156; -.
DR KEGG; ocu:100351156; -.
DR CTD; 283358; -.
DR eggNOG; KOG3588; Eukaryota.
DR GeneTree; ENSGT01050000244857; -.
DR HOGENOM; CLU_011195_0_0_1; -.
DR InParanoid; G1SV46; -.
DR OMA; VDPHLQF; -.
DR OrthoDB; 2907318at2759; -.
DR TreeFam; TF318303; -.
DR Proteomes; UP000001811; Chromosome 8.
DR Bgee; ENSOCUG00000008418; Expressed in skin of back and 14 other cell types or tissues.
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:UP000001811};
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 116..278
FT /note="PA14"
FT /evidence="ECO:0000259|PROSITE:PS51820"
FT REGION 300..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..619
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 999 AA; 114288 MW; 8EC75ABA04D7066E CRC64;
MGSPRAALLL LLRPAKLLRR RFRLLLALAL VSVGLWTLYL ELVASAQVGG NPLNRRYGSW
RELAKALASR NIPAVDPHLQ FYRPQRLNLK DQEVDRDGSS NRSYLKWNKP VPWLSEFRGR
ANLHVFEDWC GSSIQQLRRN LHFPLYPHIR TTLRKLAVSP KWTNYGLRIF GYLHPFTDGT
VQFAIAADDN AEFWLSHDDQ VTGLQLLASV GKTGKEWTAP GEFGKFRSQI SKPVSLSASH
RYYFEVLHKQ NDQGTDHVEV AWRRSDPGAK FTIIDSPSLS LFTNETVLKM DEVGHIPQTA
ASHAGSADSH PRDEQPPADM LRPDPRDTLY QVPLIPKSHL RHVLPDCPYK PSYLVDGLPL
QRYQGLRFVH LSFVYPNDYT RLSHMETHNK CFYQENAYYQ DRFSFQDYIK IDQPEKQGLE
RPGLEEDLLE ESQYEDVAEE TPASNARHTA MPEGKETPAA SPEQEATDYR LRSLRKLLGQ
PQAGLLAPFS KRNSTPFLGR PGDLRAQLPQ ERKRRPRPAP SPGLPPADRW PPGHLARSLP
QRKRPRPTAA GPGKMLGQAQ WLSQVESYIA EQRRGDGAEP QAPGPAWRGE EPVVAAAGLE
EQTEAEEEGE AEEEEEEEMS EVFEYVPVFD PVVNWDQTFS ARNLDFQALR TDWIDLNCNT
SGNLLLPEPE ALEVARVFLK RLNQRSRGRY QLQRIVNVEK RQDQLRGGRY LLELELLEQG
GRLVRLSEYV SARGWQGIDP VGGEEAEARN LQGLIWSPHN RQGQVLNVRA PEPKLCWPQG
FSWNHRAVVH FIVPVKNQAR WVQQFIKDME TLLQTTGDPH FNVVITDYSS EDMDVEMALQ
RSKLRSYQYM KLTGNFERSA GLQAGIDLVK DPHSIVFLCD LHIHFPAGVI DAIRKHCVEG
KMAFAPMVMR LHCGATPQWP EGYWEVNGFG LLGIYKSDLD KIGGMNTKEF RDRWGGEDWE
LLDRILQAGL EVERLSLRNF FHHFHSKRGM WNRRQMKMP
//
