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Polypeptide N-acetylgalactosaminyltransferase 1 (EC 2.4.1.41) (Polypeptide GalNAc transferase 1) (GalNAc-T1) (pp-GaNTase 1) (Protein-UDP acetylgalactosaminyltransferase 1) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 1 soluble form]

 GALT1_RAT               Reviewed;         559 AA.
Q10473;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
22-NOV-2017, entry version 141.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 1;
Short=GalNAc-T1;
Short=pp-GaNTase 1;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 1;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1;
Contains:
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1 soluble form;
Name=Galnt1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Sublingual gland;
PubMed=8748168; DOI=10.1007/BF00731252;
Hagen F., Gregorie C.A., Tabak L.A.;
"Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-
acetylgalactosaminyltransferase.";
Glycoconj. J. 12:901-909(1995).
[2]
MUTAGENESIS OF CYS-106; CYS-212; CYS-214; CYS-235; CYS-330; CYS-339
AND CYS-408.
PubMed=12199709; DOI=10.1046/j.1432-1033.2002.03123.x;
Tenno M., Toba S., Kezdy F.J., Elhammer A.P., Kurosaka A.;
"Identification of two cysteine residues involved in the binding of
UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
1 (GalNAc-T1).";
Eur. J. Biochem. 269:4308-4316(2002).
[3]
MUTAGENESIS OF CYS-442; ASP-444; GLY-455; PHE-457; CYS-459; ASN-465;
GLN-466; PHE-468; CYS-482; ASP-484; CYS-497; CYS-523; ASP-525 AND
CYS-540.
PubMed=12364335; DOI=10.1074/jbc.M207369200;
Tenno M., Saeki A., Kezdy F.J., Elhammer A.P., Kurosaka A.;
"The lectin domain of UDP-GalNAc:polypeptide N-
acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a
polypeptide with multiple acceptor sites.";
J. Biol. Chem. 277:47088-47096(2002).
[4]
MUTAGENESIS OF ASP-444; ASP-484 AND ASP-525.
PubMed=12419318; DOI=10.1016/S0006-291X(02)02549-4;
Tenno M., Kezdy F.J., Elhammer A.P., Kurosaka A.;
"Function of the lectin domain of polypeptide N-
acetylgalactosaminyltransferase 1.";
Biochem. Biophys. Res. Commun. 298:755-759(2002).
-!- FUNCTION: Catalyzes the initial reaction in O-linked
oligosaccharide biosynthesis, the transfer of an N-acetyl-D-
galactosamine residue to a serine or threonine residue on the
protein receptor. Has a broad spectrum of substrates for peptides
such as EA2, Muc5AC, Muc1a, Muc1b and Muc7.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Polypeptide N-
acetylgalactosaminyltransferase 1: Golgi apparatus, Golgi stack
membrane {ECO:0000250}; Single-pass type II membrane protein
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Polypeptide N-
acetylgalactosaminyltransferase 1 soluble form: Secreted
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Heart, brain, spleen, liver, skeletal muscle
and kidney.
-!- DOMAIN: There are two conserved domains in the glycosyltransferase
region: the N-terminal domain (domain A, also called GT1 motif),
which is probably involved in manganese coordination and substrate
binding and the C-terminal domain (domain B, also called
Gal/GalNAc-T motif), which is probably involved in catalytic
reaction and UDP-Gal binding.
-!- DOMAIN: The ricin B-type lectin domain directs the glycopeptide
specificity. It is required in the glycopeptide specificity of
enzyme activity but not for activity with naked peptide
substrates, suggesting that it triggers the catalytic domain to
act on GalNAc-glycopeptide substrates.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U35890; AAC52511.1; -; mRNA.
RefSeq; NP_077349.1; NM_024373.1.
RefSeq; XP_006254533.1; XM_006254471.3.
UniGene; Rn.10266; -.
ProteinModelPortal; Q10473; -.
SMR; Q10473; -.
MINT; MINT-4566270; -.
STRING; 10116.ENSRNOP00000022117; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
PaxDb; Q10473; -.
PRIDE; Q10473; -.
Ensembl; ENSRNOT00000022117; ENSRNOP00000022117; ENSRNOG00000016207.
GeneID; 79214; -.
KEGG; rno:79214; -.
UCSC; RGD:620358; rat.
CTD; 2589; -.
RGD; 620358; Galnt1.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
HOVERGEN; HBG051699; -.
InParanoid; Q10473; -.
KO; K00710; -.
OMA; IMSDDLC; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q10473; -.
TreeFam; TF313267; -.
BRENDA; 2.4.1.41; 5301.
Reactome; R-RNO-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-RNO-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
PRO; PR:Q10473; -.
Proteomes; UP000002494; Chromosome 18.
Bgee; ENSRNOG00000016207; -.
Genevisible; Q10473; RN.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IMP:RGD.
GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
GO; GO:0018242; P:protein O-linked glycosylation via serine; ISO:RGD.
GO; GO:0018243; P:protein O-linked glycosylation via threonine; ISO:RGD.
CDD; cd00161; RICIN; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00535; Glycos_transf_2; 1.
Pfam; PF00652; Ricin_B_lectin; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Glycosyltransferase;
Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
Reference proteome; Secreted; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 559 Polypeptide N-
acetylgalactosaminyltransferase 1.
/FTId=PRO_0000223390.
CHAIN 41 559 Polypeptide N-
acetylgalactosaminyltransferase 1 soluble
form.
/FTId=PRO_0000012263.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 559 Lumenal. {ECO:0000255}.
DOMAIN 429 551 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 115 225 Catalytic subdomain A.
REGION 285 347 Catalytic subdomain B.
METAL 209 209 Manganese. {ECO:0000250}.
METAL 211 211 Manganese. {ECO:0000250}.
METAL 344 344 Manganese. {ECO:0000250}.
BINDING 156 156 Substrate. {ECO:0000250}.
BINDING 186 186 Substrate. {ECO:0000250}.
BINDING 316 316 Substrate. {ECO:0000250}.
BINDING 347 347 Substrate. {ECO:0000250}.
BINDING 352 352 Substrate. {ECO:0000250}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 552 552 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 106 339 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 330 408 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 442 459 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 482 497 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 523 540 {ECO:0000255|PROSITE-ProRule:PRU00174}.
MUTAGEN 106 106 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12199709}.
MUTAGEN 212 212 C->A: Loss of enzyme activity due to
absence of interaction between UDP moiety
and UDP-GalNAC.
{ECO:0000269|PubMed:12199709}.
MUTAGEN 214 214 C->A: Loss of enzyme activity due to
absence of interaction between UDP moiety
and UDP-GalNAC.
{ECO:0000269|PubMed:12199709}.
MUTAGEN 235 235 C->A: No effect.
{ECO:0000269|PubMed:12199709}.
MUTAGEN 330 330 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12199709}.
MUTAGEN 339 339 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12199709}.
MUTAGEN 408 408 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12199709}.
MUTAGEN 442 442 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 444 444 D->A: Induces a strong decrease in
activity; loss of function; when
associated with A-484 and A-525.
{ECO:0000269|PubMed:12364335,
ECO:0000269|PubMed:12419318}.
MUTAGEN 455 455 G->Q: Induces a decrease in activity.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 457 457 F->A: Little or no effect.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 459 459 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 465 465 N->A: Little or no effect.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 466 466 Q->A: Induces a decrease in activity.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 468 468 F->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 468 468 F->W,Y: Little or no effect.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 482 482 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 484 484 D->A: Loss of enzyme activity; when
associated with A-444 and A-525.
{ECO:0000269|PubMed:12364335,
ECO:0000269|PubMed:12419318}.
MUTAGEN 497 497 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 523 523 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12364335}.
MUTAGEN 525 525 D->A: Loss of enzyme activity; when
associated with A-444 and A-484.
{ECO:0000269|PubMed:12364335,
ECO:0000269|PubMed:12419318}.
MUTAGEN 540 540 C->A: Loss of enzyme activity.
{ECO:0000269|PubMed:12364335}.
SEQUENCE 559 AA; 64229 MW; 5E36A95D9422C853 CRC64;
MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKKER GLPAGDVLEL VQKPHEGPGE
MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIAFNRSLPD VRLEGCKTKV YPDSLPTTSV
VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE IVLVDDASER DFLKRPLESY VKKLKVPVHV
IRMEQRSGLI RARLKGAAVS KGQVITFLDA HCECTVGWLE PLLARIKHDR RTVVCPIIDV
ISDDTFEYMA GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT PYTFPGGTGQ
IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRV GLRHKLQCKP FSWYLENIYP
DSQIPRHYFS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD
LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC
TGSRSQQWLL RNVTLPEIF


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