GLTL6_HUMAN
ID GLTL6_HUMAN Reviewed; 601 AA.
AC Q49A17; Q2L4S6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase-like 6;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 17;
DE Short=GalNAc-T17;
DE Short=pp-GaNTase 17;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase 17;
DE AltName: Full=Putative polypeptide N-acetylgalactosaminyltransferase 17;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 17;
GN Name=GALNTL6; Synonyms=GALNT17;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Bennett E.P.;
RT "The GalNAc-transferase gene family.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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. {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q49A17-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q49A17-2; Sequence=VSP_032402;
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; AJ626725; CAF25036.1; -; mRNA.
DR EMBL; AC024706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025561; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC025821; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093803; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC095045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC095063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC097496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC109520; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC110776; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131952; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047551; AAH47551.1; -; mRNA.
DR CCDS; CCDS34104.1; -. [Q49A17-1]
DR RefSeq; NP_001030017.2; NM_001034845.2. [Q49A17-1]
DR AlphaFoldDB; Q49A17; -.
DR SMR; Q49A17; -.
DR BioGRID; 138023; 2.
DR STRING; 9606.ENSP00000423313; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR GlyGen; Q49A17; 2 sites.
DR iPTMnet; Q49A17; -.
DR PhosphoSitePlus; Q49A17; -.
DR BioMuta; GALNTL6; -.
DR DMDM; 296434516; -.
DR EPD; Q49A17; -.
DR jPOST; Q49A17; -.
DR MassIVE; Q49A17; -.
DR MaxQB; Q49A17; -.
DR PaxDb; Q49A17; -.
DR PeptideAtlas; Q49A17; -.
DR PRIDE; Q49A17; -.
DR ProteomicsDB; 62014; -. [Q49A17-1]
DR ProteomicsDB; 62015; -. [Q49A17-2]
DR Antibodypedia; 28511; 31 antibodies from 12 providers.
DR DNASU; 442117; -.
DR Ensembl; ENST00000506823.6; ENSP00000423313.1; ENSG00000174473.16. [Q49A17-1]
DR Ensembl; ENST00000508122.5; ENSP00000423827.1; ENSG00000174473.16. [Q49A17-2]
DR GeneID; 442117; -.
DR KEGG; hsa:442117; -.
DR MANE-Select; ENST00000506823.6; ENSP00000423313.1; NM_001034845.3; NP_001030017.2.
DR UCSC; uc003isv.4; human. [Q49A17-1]
DR CTD; 442117; -.
DR DisGeNET; 442117; -.
DR GeneCards; GALNTL6; -.
DR HGNC; HGNC:33844; GALNTL6.
DR HPA; ENSG00000174473; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 615138; gene.
DR neXtProt; NX_Q49A17; -.
DR OpenTargets; ENSG00000174473; -.
DR PharmGKB; PA164720162; -.
DR VEuPathDB; HostDB:ENSG00000174473; -.
DR eggNOG; KOG3736; Eukaryota.
DR GeneTree; ENSGT00940000155038; -.
DR InParanoid; Q49A17; -.
DR OMA; FGFVNHT; -.
DR PhylomeDB; Q49A17; -.
DR TreeFam; TF313267; -.
DR PathwayCommons; Q49A17; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 442117; 11 hits in 1069 CRISPR screens.
DR ChiTaRS; GALNTL6; human.
DR GenomeRNAi; 442117; -.
DR Pharos; Q49A17; Tbio.
DR PRO; PR:Q49A17; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q49A17; protein.
DR Bgee; ENSG00000174473; Expressed in prefrontal cortex and 89 other tissues.
DR ExpressionAtlas; Q49A17; baseline and differential.
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; IDA:UniProtKB.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
DR GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA:UniProtKB.
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 Alternative splicing; Disulfide bond; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..601
FT /note="Polypeptide N-acetylgalactosaminyltransferase-like
FT 6"
FT /id="PRO_0000325774"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..601
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 453..585
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 139..248
FT /note="Catalytic subdomain A"
FT REGION 306..368
FT /note="Catalytic subdomain B"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 365
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 368
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 141
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 588
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 130..360
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 351..427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 466..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 518..533
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 558..573
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 1..45
FT /note="MKRKQKRFLQMTLLFTVALIFLPNVGLWSLYKDKHLVKSAEPGEQ -> MRA
FT KFRAGAGHQRNPSISADHGVHELVY (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_032402"
FT CONFLICT 83
FT /note="G -> R (in Ref. 3; AAH47551)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="A -> P (in Ref. 3; AAH47551)"
FT /evidence="ECO:0000305"
FT CONFLICT 563
FT /note="P -> H (in Ref. 3; AAH47551)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 601 AA; 69788 MW; DEFBE2E41DD2FC1D CRC64;
MKRKQKRFLQ MTLLFTVALI FLPNVGLWSL YKDKHLVKSA EPGEQQTFPL GLGDGQFYSW
TDGLRRKDWH DYESIQKEAM RSGKGEHGKP YPLTEEDHDD SAYRENGFNI FVSNNIALER
SLPDIRHANC KHKMYLERLP NTSIIIPFHN EGWTSLLRTI HSIINRTPGS LIAEIILVDD
FSEREHLKDK LEEYMARFSK VRIVRTKKRE GLIRTRLLGA SMARGEVLTF LDSHCEVNVN
WLPPLLNQIA LNHKTIVCPM IDVIDHNHFG YEAQAGDAMR GAFDWEMYYK RIPIPPELQR
ADPSDPFESP VMAGGLFAVD RKWFWELGGY DPGLEIWGGE QYEISFKVWM CGGEMFDVPC
SRVGHIYRKY VPYKVPSGTS LARNLKRVAE TWMDEFAEYI YQRRPEYRHL STGDISAQKE
LRKQLKCKDF KWFMAAVAWD VPKYYPPVEP PPAAWGEIRN VAANLCVDSK HGATGTELRL
DICVKDGSER TWSHEQLFTF GWREDIRPGE PLHTRKFCFD AISHNSPVTL YDCHGMKGNQ
LWGYRKDRTL FHPVSNSCMD CNPAEKKIFM ARCDPLSETQ QWIFEHINMT VLEKFNHHAN
S
