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Polypeptide N-acetylgalactosaminyltransferase 4 (pp-GaNTase 4) (EC 2.4.1.41) (Protein-UDP acetylgalactosaminyltransferase 4) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4)

 GALT4_CAEEL             Reviewed;         589 AA.
Q8I136; O61390;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
10-OCT-2018, entry version 129.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 4;
Short=pp-GaNTase 4;
EC=2.4.1.41;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 4;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4;
Name=gly-4; ORFNames=Y116F11B.12;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND ENZYME ACTIVITY.
STRAIN=Bristol N2;
PubMed=9525933; DOI=10.1074/jbc.273.14.8268;
Hagen F.K., Nehrke K.;
"cDNA cloning and expression of a family of UDP-N-acetyl-D-
galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence
homologs from Caenorhabditis elegans.";
J. Biol. Chem. 273:8268-8277(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
-!- 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.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
{ECO:0000269|PubMed:9525933}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250};
Single-pass type II membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=a;
IsoId=Q8I136-1; Sequence=Displayed;
Name=b;
IsoId=Q8I136-2; Sequence=VSP_011236, VSP_011237;
Note=No experimental confirmation available.;
-!- 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. {ECO:0000250}.
-!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
contributes to the glycopeptide specificity. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
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EMBL; AF031834; AAC13670.1; -; mRNA.
EMBL; AL132943; CAB81985.3; -; Genomic_DNA.
EMBL; AL132943; CAC14394.1; -; Genomic_DNA.
PIR; T42244; T42244.
RefSeq; NP_001024216.1; NM_001029045.3. [Q8I136-1]
RefSeq; NP_507850.2; NM_075449.7. [Q8I136-2]
UniGene; Cel.19666; -.
ProteinModelPortal; Q8I136; -.
SMR; Q8I136; -.
BioGrid; 45263; 2.
DIP; DIP-26941N; -.
IntAct; Q8I136; 1.
STRING; 6239.Y116F11B.12a.1; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
EPD; Q8I136; -.
PaxDb; Q8I136; -.
PeptideAtlas; Q8I136; -.
PRIDE; Q8I136; -.
EnsemblMetazoa; Y116F11B.12a.1; Y116F11B.12a.1; WBGene00001629. [Q8I136-1]
EnsemblMetazoa; Y116F11B.12a.2; Y116F11B.12a.2; WBGene00001629. [Q8I136-1]
EnsemblMetazoa; Y116F11B.12b.1; Y116F11B.12b.1; WBGene00001629. [Q8I136-2]
EnsemblMetazoa; Y116F11B.12b.2; Y116F11B.12b.2; WBGene00001629. [Q8I136-2]
EnsemblMetazoa; Y116F11B.12b.3; Y116F11B.12b.3; WBGene00001629. [Q8I136-2]
GeneID; 180302; -.
KEGG; cel:CELE_Y116F11B.12; -.
UCSC; Y116F11B.12b.1; c. elegans. [Q8I136-1]
CTD; 180302; -.
WormBase; Y116F11B.12a; CE26046; WBGene00001629; gly-4. [Q8I136-1]
WormBase; Y116F11B.12b; CE32074; WBGene00001629; gly-4. [Q8I136-2]
eggNOG; KOG3738; Eukaryota.
eggNOG; ENOG410XPRX; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
InParanoid; Q8I136; -.
KO; K00710; -.
OMA; GNQEWAL; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q8I136; -.
Reactome; R-CEL-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-CEL-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
PRO; PR:Q8I136; -.
Proteomes; UP000001940; Chromosome V.
Bgee; WBGene00001629; Expressed in 5 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:WormBase.
GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA:WormBase.
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; 2.
2: Evidence at transcript level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
Metal-binding; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 589 Polypeptide N-
acetylgalactosaminyltransferase 4.
/FTId=PRO_0000059147.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.
TRANSMEM 12 31 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 32 589 Lumenal. {ECO:0000255}.
DOMAIN 458 589 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 150 255 Catalytic subdomain A.
REGION 315 377 Catalytic subdomain B.
COMPBIAS 37 72 Pro-rich.
METAL 239 239 Manganese. {ECO:0000250}.
METAL 241 241 Manganese. {ECO:0000250}.
METAL 374 374 Manganese. {ECO:0000250}.
BINDING 191 191 Substrate. {ECO:0000250}.
BINDING 216 216 Substrate. {ECO:0000250}.
BINDING 240 240 Substrate. {ECO:0000250}.
BINDING 346 346 Substrate. {ECO:0000250}.
BINDING 377 377 Substrate. {ECO:0000250}.
BINDING 380 380 Substrate. {ECO:0000250}.
BINDING 382 382 Substrate. {ECO:0000250}.
CARBOHYD 523 523 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 140 369 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 360 438 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 471 488 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 514 531 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 553 571 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 453 453 E -> D (in isoform b). {ECO:0000305}.
/FTId=VSP_011236.
VAR_SEQ 454 589 Missing (in isoform b). {ECO:0000305}.
/FTId=VSP_011237.
SEQUENCE 589 AA; 67031 MW; 108D621D91A329D2 CRC64;
MLPRMLKMKT VGTVLAVIWL FGLAFIYVQS TSSSLRPPGR HPPPLPQLDP LIPQNPPQND
EIRPKKSAPP IPTINLAEDT TIHERTEKDV TWKTFDVEKF LNKGKWHQGE DKYKANSFNQ
EASDALNPTR KIPDSREPQC RDVDYSKVGM QPTTVIITYH NEARSSLLRT VFSVFNQSPE
ELLLEIVLVD DNSQDVEIGK ELAQIQRITV LRNNQREGLI RSRVKGAQVA RAPVLTFLDS
HIECNQKWLE PLLARIAENP KAVVAPIIDV INVDNFNYVG ASADLRGGFD WTLVFRWEFM
NEQLRKERHA HPTAPIRSPT MAGGLFAISK EWFNELGTYD LDMEVWGGEN LEMSFRVWQC
GGSLEIMPCS RVGHVFRKKH PYTFPGGSGN VFQKNTRRAA EVWMDEYKAI YLKNVPSARF
VNFGDITDRL AIRDRLQCKS FKWYLENVYP QLEIPRKTPG KSFQMKIGNL CLDSMARKES
EAPGLFGCHG TGGNQEWVFD QLTKTFKNAI SQLCLDFSSN TENKTVTMVK CENLRPDTMV
VEKNGWLTQG GKCLTVNQGS GGDWLIYGAH CELNNGAQRW IFEKLDTYE


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