GALT5_RAT
ID GALT5_RAT Reviewed; 930 AA.
AC O88422;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 5;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 5;
DE Short=GalNAc-T5;
DE Short=pp-GaNTase 5;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 5;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5;
GN Name=Galnt5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Sublingual gland;
RX PubMed=9765313; DOI=10.1074/jbc.273.42.27749;
RA Ten Hagen K.G., Hagen F.K., Balys M.M., Beres T.M., Van Wuyckhuyse B.,
RA Tabak L.A.;
RT "Cloning and expression of a novel, tissue specifically expressed member of
RT the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family.";
RL J. Biol. Chem. 273:27749-27754(1998).
CC -!- FUNCTION: Catalyzes the initial reaction in O-linked oligosaccharide
CC biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a
CC serine or threonine residue on the protein receptor. Has activity
CC toward EA2 peptide substrate, but has a weak activity toward Muc2,
CC Muc1b, rMuc-2 or mG-Muc substrates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-
CC [N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:23956, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12788,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:53604,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:67138; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:9765313};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-
CC O-[N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:52424, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:67138, ChEBI:CHEBI:87075; EC=2.4.1.41;
CC Evidence={ECO:0000269|PubMed:9765313};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Interacts with EXT2. Does not interact with EXT1, EXTL1 or
CC EXTL3 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in sublingual gland.
CC Expressed at lower level in stomach and small intestine. Weakly or not
CC expressed in submandibular gland, parotid gland, kidney, liver, heart,
CC brain, spleen, lung, skeletal muscle, testis, ovary, cervix and uterus.
CC {ECO:0000269|PubMed:9765313}.
CC -!- DOMAIN: There are two conserved domains in the glycosyltransferase
CC region: the N-terminal domain (domain A, also called GT1 motif), which
CC is probably involved in manganese coordination and substrate binding
CC and the C-terminal domain (domain B, also called Gal/GalNAc-T motif),
CC which is probably involved in catalytic reaction and UDP-Gal binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and contributes
CC to the glycopeptide specificity. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
CC subfamily. {ECO:0000305}.
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DR EMBL; AF049344; AAC69708.1; -; mRNA.
DR RefSeq; NP_113984.1; NM_031796.1.
DR AlphaFoldDB; O88422; -.
DR SMR; O88422; -.
DR STRING; 10116.ENSRNOP00000006319; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; O88422; 12 sites.
DR PaxDb; O88422; -.
DR PRIDE; O88422; -.
DR Ensembl; ENSRNOT00000006319; ENSRNOP00000006319; ENSRNOG00000004645.
DR GeneID; 83627; -.
DR KEGG; rno:83627; -.
DR UCSC; RGD:620361; rat.
DR CTD; 11227; -.
DR RGD; 620361; Galnt5.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000159241; -.
DR HOGENOM; CLU_013477_1_0_1; -.
DR InParanoid; O88422; -.
DR OMA; VQPDQMK; -.
DR OrthoDB; 606683at2759; -.
DR PhylomeDB; O88422; -.
DR TreeFam; TF313267; -.
DR BRENDA; 2.4.1.41; 5301.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR PRO; PR:O88422; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000004645; Expressed in jejunum and 12 other tissues.
DR Genevisible; O88422; RN.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; ISO:RGD.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR CDD; cd02510; pp-GalNAc-T; 1.
DR CDD; cd00161; RICIN; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR045885; GalNAc-T.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR Pfam; PF00652; Ricin_B_lectin; 1.
DR SMART; SM00458; RICIN; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS50231; RICIN_B_LECTIN; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Glycosyltransferase; Golgi apparatus; Lectin;
KW Manganese; Membrane; Metal-binding; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..930
FT /note="Polypeptide N-acetylgalactosaminyltransferase 5"
FT /id="PRO_0000059112"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 13..35
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 36..930
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 794..925
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 163..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..594
FT /note="Catalytic subdomain A"
FT REGION 654..716
FT /note="Catalytic subdomain B"
FT COMPBIAS 163..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 555
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 578
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 579
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 580
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 713
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 716
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 721
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z7M9"
FT CARBOHYD 178
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 309
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 817
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 835
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 902
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 476..708
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 699..779
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 812..825
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 848..863
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 898..913
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
SQ SEQUENCE 930 AA; 105120 MW; 1C906A76F320A225 CRC64;
MNKIRKFFRG SGRVLAFIFV ASVIWLLFDM AALRLSFSEI NTGILKEDIM RREQTGFRVE
ADQMTILSPS SRGMRPPRNG AGGKESFRKA ENRVLKVEEN VDQVQRKGKM QFLLGRGKAV
SLWHRTHVQT LPVTLPMQKT QGRDSKPEVS SLHMMSKQTT VLGSEKDSFT VSRGVPLNKT
AEHTETLDKK QEAPENYNLS SDTSKQASQR ALNVTISVRT DRSKQQSQTV TKSSIQFASL
PILKPEEVTV TKKTEAQGKD LKYEAHKARP LLKFTADVGH LKKQSTNETG LGVLPEADGA
KVAPGKKLNF SESQIVIITK EEGQKTDTKE VPNSKIQTVF PKLLGESQGK HIPRSQSQTL
SSPLAPKRAV SQSKPTLAEE LHTARSNLTA KATTVGHQQS HANISENPGK HHVLRIDVTL
SPRDLNAPGQ FGRPVVVPPG KKKEAEQRWK EGNFNVYLSD LIPVDRAIED TRPAGCAEQL
VHNDLPTTSI IMCFVDEVWS ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK DYLKANLDKY
MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK
KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWRTIP PDVIAKNGIK ETDIIRCPVM
AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG GEIEIIPCSR VGHIFRNDNP
YSFPKDRMKT VERNLVRVAE VWLDEYKELF YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCQ
SFKWYLDNVF PDLKAPVVRA SGVFINLALG KCVSIKNITV VLEDCDGSSE LQQFNYTWVR
LIKHGEWCVA PIPDKGSLTL YPCDNRNNRL KWLHRSASAF HPELVDHIVF ESYQQLLCME
GNFSQKTLKL AACNPTEPQQ KWKFEKYYDV
