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Polypeptide N-acetylgalactosaminyltransferase 5 (pp-GaNTase 5) (EC 2.4.1.41) (Protein-UDP acetylgalactosaminyltransferase 5) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5)

 GALT5_CAEEL             Reviewed;         626 AA.
Q95ZJ1; O61391; O61392; O61393; Q95ZJ2; Q9U2J8;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
16-AUG-2004, sequence version 2.
10-OCT-2018, entry version 137.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 5;
Short=pp-GaNTase 5;
EC=2.4.1.41;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 5;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5;
Name=gly-5; ORFNames=Y39E4B.12;
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis.
NCBI_TaxID=6239;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
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].
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.
-!- 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=3;
Name=a; Synonyms=GLY5b, GLY-5b;
IsoId=Q95ZJ1-1; Sequence=Displayed;
Name=b; Synonyms=GLY5a, GLY-5a;
IsoId=Q95ZJ1-2; Sequence=VSP_011238;
Name=c; Synonyms=GLY5c, GLY-5c;
IsoId=Q95ZJ1-3; Sequence=VSP_011239;
-!- 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; AF031835; AAC13671.1; -; mRNA.
EMBL; AF031836; AAC13672.1; -; mRNA.
EMBL; AF031837; AAC13673.1; -; mRNA.
EMBL; AL110487; CAB54435.1; -; Genomic_DNA.
EMBL; AL110487; CAC42369.1; -; Genomic_DNA.
EMBL; AL110487; CAC42368.1; -; Genomic_DNA.
PIR; T42245; T42245.
PIR; T42246; T42246.
PIR; T42247; T42247.
RefSeq; NP_001022850.1; NM_001027679.4. [Q95ZJ1-1]
RefSeq; NP_001022851.1; NM_001027680.4. [Q95ZJ1-2]
RefSeq; NP_001022852.1; NM_001027681.5. [Q95ZJ1-3]
UniGene; Cel.19665; -.
ProteinModelPortal; Q95ZJ1; -.
SMR; Q95ZJ1; -.
BioGrid; 41908; 4.
DIP; DIP-26207N; -.
IntAct; Q95ZJ1; 3.
STRING; 6239.Y39E4B.12a.1; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
EPD; Q95ZJ1; -.
PaxDb; Q95ZJ1; -.
PeptideAtlas; Q95ZJ1; -.
PRIDE; Q95ZJ1; -.
EnsemblMetazoa; Y39E4B.12a.1; Y39E4B.12a.1; WBGene00001630. [Q95ZJ1-1]
EnsemblMetazoa; Y39E4B.12a.2; Y39E4B.12a.2; WBGene00001630. [Q95ZJ1-1]
EnsemblMetazoa; Y39E4B.12a.3; Y39E4B.12a.3; WBGene00001630. [Q95ZJ1-1]
EnsemblMetazoa; Y39E4B.12b.1; Y39E4B.12b.1; WBGene00001630. [Q95ZJ1-2]
EnsemblMetazoa; Y39E4B.12b.2; Y39E4B.12b.2; WBGene00001630. [Q95ZJ1-2]
EnsemblMetazoa; Y39E4B.12b.3; Y39E4B.12b.3; WBGene00001630. [Q95ZJ1-2]
EnsemblMetazoa; Y39E4B.12c.1; Y39E4B.12c.1; WBGene00001630. [Q95ZJ1-3]
EnsemblMetazoa; Y39E4B.12c.2; Y39E4B.12c.2; WBGene00001630. [Q95ZJ1-3]
EnsemblMetazoa; Y39E4B.12c.3; Y39E4B.12c.3; WBGene00001630. [Q95ZJ1-3]
GeneID; 176736; -.
KEGG; cel:CELE_Y39E4B.12; -.
UCSC; Y39E4B.12c; c. elegans. [Q95ZJ1-1]
CTD; 176736; -.
WormBase; Y39E4B.12a; CE24240; WBGene00001630; gly-5. [Q95ZJ1-1]
WormBase; Y39E4B.12b; CE28119; WBGene00001630; gly-5. [Q95ZJ1-2]
WormBase; Y39E4B.12c; CE28120; WBGene00001630; gly-5. [Q95ZJ1-3]
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
InParanoid; Q95ZJ1; -.
KO; K00710; -.
OMA; ERWNPLC; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q95ZJ1; -.
Reactome; R-CEL-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
PRO; PR:Q95ZJ1; -.
Proteomes; UP000001940; Chromosome III.
Bgee; WBGene00001630; 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; 1.
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 1 626 Polypeptide N-
acetylgalactosaminyltransferase 5.
/FTId=PRO_0000059148.
TOPO_DOM 1 11 Cytoplasmic. {ECO:0000255}.
TRANSMEM 12 31 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 32 626 Lumenal. {ECO:0000255}.
DOMAIN 488 610 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 174 284 Catalytic subdomain A.
REGION 345 407 Catalytic subdomain B.
METAL 268 268 Manganese. {ECO:0000250}.
METAL 270 270 Manganese. {ECO:0000250}.
METAL 404 404 Manganese. {ECO:0000250}.
BINDING 215 215 Substrate. {ECO:0000250}.
BINDING 245 245 Substrate. {ECO:0000250}.
BINDING 269 269 Substrate. {ECO:0000250}.
BINDING 376 376 Substrate. {ECO:0000250}.
BINDING 407 407 Substrate. {ECO:0000250}.
BINDING 412 412 Substrate. {ECO:0000250}.
CARBOHYD 32 32 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 338 338 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 165 399 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 390 466 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 502 521 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 544 557 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 583 598 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 492 523 VRNSAVQPARCLDCMVGRHEKNRPVGTYQCHG -> MRNAG
GKNRQCIDYKPSGGKTVGMYQCHN (in isoform b).
{ECO:0000303|PubMed:9525933}.
/FTId=VSP_011238.
VAR_SEQ 492 523 VRNSAVQPARCLDCMVGRHEKNRPVGTYQCHG -> LRNAQ
TSQCLDSAVGEEVENKAITPYPCHE (in isoform c).
{ECO:0000303|PubMed:9525933}.
/FTId=VSP_011239.
CONFLICT 361 361 K -> E (in Ref. 1; AAC13671/AAC13672/
AAC13673). {ECO:0000305}.
SEQUENCE 626 AA; 71382 MW; 561BD0576514B983 CRC64;
MIIFKKKAIL KVLLLVPVFW ICSLIFFAAT SNDSSQIGSN NDLANKIAEA NFHPKAAKQD
VIQGFGPPIE PEPVVENNKV EEEEQPGGNL AKPKFMVDPN DPIYKKGDAA QAGELGKAVV
VDKTKLSTEE KAKYDKGMLN NAFNQYASDM ISVHRTLPTN IDAECKTEKY NENLPRTSVI
ICFHNEAWSV LLRTVHSVLE RTPDHLLEEV VLVDDFSDMD HTKRPLEEYM SQFGGKVKIL
RMEKREGLIR ARLRGAAVAT GEVLTYLDSH CECMEGWMEP LLDRIKRDPT TVVCPVIDVI
DDNTFEYHHS KAYFTSVGGF DWGLQFNWHS IPERDRKNRT RPIDPVRSPT MAGGLFSIDK
KYFEKLGTYD PGFDIWGGEN LELSFKIWMC GGTLEIVPCS HVGHVFRKRS PYKWRTGVNV
LKRNSIRLAE VWLDDYKTYY YERINNQLGD FGDISSRKKL REDLGCKSFK WYLDNIYPEL
FVPGESVAKG EVRNSAVQPA RCLDCMVGRH EKNRPVGTYQ CHGQGGNQYW MLSKDGEIRR
DESCVDYAGS DVMVFPCHGM KGNQEWRYNH DTGRLQHAVS QKCLGMTKDG AKLEMVACQY
DDPYQHWKFK EYNEAKAIEH GAKPPS


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