GLT16_HUMAN
ID GLT16_HUMAN Reviewed; 558 AA.
AC Q8N428; Q4KMG3; Q58A55; Q9ULT9;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 16;
DE EC=2.4.1.41;
DE AltName: Full=Polypeptide GalNAc transferase 16;
DE Short=GalNAc-T16;
DE AltName: Full=Polypeptide GalNAc transferase-like protein 1;
DE Short=GalNAc-T-like protein 1;
DE Short=pp-GaNTase-like protein 1;
DE AltName: Full=Polypeptide N-acetylgalactosaminyltransferase-like protein 1;
DE AltName: Full=Protein-UDP acetylgalactosaminyltransferase-like protein 1;
DE AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 1;
GN Name=GALNT16; Synonyms=GALNTL1, KIAA1130;
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fetal brain;
RA Guo J., Zhang Y., Chen L., Narimatsu H.;
RT "Cloning and Characterization of New Member of Human UDP-N-acetyl-alpha-D-
RT galactosamine:polypeptide N-acetylgalactosaminyltransferase, Designated
RT GalNAc-T16.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-201.
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-201.
RC TISSUE=Brain, and Chondrosarcoma;
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).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22186971; DOI=10.1093/glycob/cwr183;
RA Raman J., Guan Y., Perrine C.L., Gerken T.A., Tabak L.A.;
RT "UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-
RT acetylgalactosaminyltransferases: completion of the family tree.";
RL Glycobiology 22:768-777(2012).
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.
CC {ECO:0000269|PubMed:22186971}.
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:22186971};
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:22186971};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=251 uM for Muc5AC {ECO:0000269|PubMed:22186971};
CC KM=310 uM for Muc5AC-3 {ECO:0000269|PubMed:22186971};
CC KM=390 uM for Muc5AC-13 {ECO:0000269|PubMed:22186971};
CC KM=332 uM for EA2 {ECO:0000269|PubMed:22186971};
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=Q8N428-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N428-2; Sequence=VSP_011231;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86444.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Putative
CC polypeptide N-acetylgalactosaminyltransferase-like protein 1;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_499";
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DR EMBL; AB032956; BAA86444.1; ALT_INIT; mRNA.
DR EMBL; AB078143; BAD93178.1; -; mRNA.
DR EMBL; AK289745; BAF82434.1; -; mRNA.
DR EMBL; CH471061; EAW80987.1; -; Genomic_DNA.
DR EMBL; BC036812; AAH36812.2; -; mRNA.
DR EMBL; BC098578; AAH98578.1; -; mRNA.
DR CCDS; CCDS32107.1; -. [Q8N428-1]
DR RefSeq; NP_001161840.1; NM_001168368.1. [Q8N428-1]
DR RefSeq; NP_065743.2; NM_020692.2. [Q8N428-1]
DR RefSeq; XP_011535307.1; XM_011537005.1. [Q8N428-1]
DR RefSeq; XP_011535308.1; XM_011537006.2. [Q8N428-1]
DR RefSeq; XP_016876987.1; XM_017021498.1. [Q8N428-1]
DR AlphaFoldDB; Q8N428; -.
DR SMR; Q8N428; -.
DR BioGRID; 121524; 19.
DR IntAct; Q8N428; 9.
DR STRING; 9606.ENSP00000336729; -.
DR CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR CAZy; GT27; Glycosyltransferase Family 27.
DR iPTMnet; Q8N428; -.
DR PhosphoSitePlus; Q8N428; -.
DR BioMuta; GALNT16; -.
DR DMDM; 51316024; -.
DR EPD; Q8N428; -.
DR jPOST; Q8N428; -.
DR MassIVE; Q8N428; -.
DR MaxQB; Q8N428; -.
DR PaxDb; Q8N428; -.
DR PeptideAtlas; Q8N428; -.
DR PRIDE; Q8N428; -.
DR ProteomicsDB; 71869; -. [Q8N428-1]
DR ProteomicsDB; 71870; -. [Q8N428-2]
DR Antibodypedia; 25033; 69 antibodies from 17 providers.
DR DNASU; 57452; -.
DR Ensembl; ENST00000337827.8; ENSP00000336729.4; ENSG00000100626.17. [Q8N428-1]
DR Ensembl; ENST00000448469.8; ENSP00000402970.3; ENSG00000100626.17. [Q8N428-1]
DR Ensembl; ENST00000553471.6; ENSP00000451420.1; ENSG00000100626.17. [Q8N428-2]
DR Ensembl; ENST00000553669.1; ENSP00000451200.1; ENSG00000100626.17. [Q8N428-2]
DR GeneID; 57452; -.
DR KEGG; hsa:57452; -.
DR MANE-Select; ENST00000448469.8; ENSP00000402970.3; NM_001168368.2; NP_001161840.1.
DR UCSC; uc001xla.3; human. [Q8N428-1]
DR CTD; 57452; -.
DR DisGeNET; 57452; -.
DR GeneCards; GALNT16; -.
DR HGNC; HGNC:23233; GALNT16.
DR HPA; ENSG00000100626; Tissue enhanced (brain, heart muscle).
DR MIM; 615132; gene.
DR neXtProt; NX_Q8N428; -.
DR OpenTargets; ENSG00000100626; -.
DR PharmGKB; PA134991608; -.
DR VEuPathDB; HostDB:ENSG00000100626; -.
DR eggNOG; KOG3738; Eukaryota.
DR GeneTree; ENSGT00940000158846; -.
DR HOGENOM; CLU_013477_0_2_1; -.
DR InParanoid; Q8N428; -.
DR OMA; VCNPREG; -.
DR PhylomeDB; Q8N428; -.
DR TreeFam; TF313267; -.
DR PathwayCommons; Q8N428; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SABIO-RK; Q8N428; -.
DR SignaLink; Q8N428; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 57452; 12 hits in 1057 CRISPR screens.
DR ChiTaRS; GALNT16; human.
DR GenomeRNAi; 57452; -.
DR Pharos; Q8N428; Tbio.
DR PRO; PR:Q8N428; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8N428; protein.
DR Bgee; ENSG00000100626; Expressed in endothelial cell and 144 other tissues.
DR ExpressionAtlas; Q8N428; baseline and differential.
DR Genevisible; Q8N428; HS.
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:0018242; P:protein O-linked glycosylation via serine; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Alternative splicing; Disulfide bond; Glycosyltransferase; Golgi apparatus;
KW Lectin; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..558
FT /note="Polypeptide N-acetylgalactosaminyltransferase 16"
FT /id="PRO_0000059135"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..558
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 428..555
FT /note="Ricin B-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REGION 33..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..227
FT /note="Catalytic subdomain A"
FT REGION 286..348
FT /note="Catalytic subdomain B"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 317
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 345
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 348
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT DISULFID 113..340
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 331..409
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 441..460
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 486..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT DISULFID 530..543
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT VAR_SEQ 514..558
FT /note="KWRRKGSFIQHSVSGLCLETKPAQLVTSKCQADAQAQQWQLLPHT -> VSL
FT LASGPEAQQPEGPCLRVADLGRRAPD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10574461, ECO:0000303|Ref.2"
FT /id="VSP_011231"
FT VARIANT 201
FT /note="V -> M (in dbSNP:rs12879377)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_055848"
FT VARIANT 497
FT /note="P -> S (in dbSNP:rs59840366)"
FT /id="VAR_061195"
SQ SEQUENCE 558 AA; 63074 MW; FF35C5606B5291B8 CRC64;
MRKIRANAIA ILTVAWILGT FYYLWQDNRA HAASSGGRGA QRAGRRSEQL REDRTIPLIV
TGTPSKGFDE KAYLSAKQLK AGEDPYRQHA FNQLESDKLS PDRPIRDTRH YSCPSVSYSS
DLPATSVIIT FHNEARSTLL RTVKSVLNRT PANLIQEIIL VDDFSSDPED CLLLTRIPKV
KCLRNDRREG LIRSRVRGAD VAAATVLTFL DSHCEVNTEW LPPMLQRVKE DHTRVVSPII
DVISLDNFAY LAASADLRGG FDWSLHFKWE QIPLEQKMTR TDPTRPIRTP VIAGGIFVID
KSWFNHLGKY DAQMDIWGGE NFELSFRVWM CGGSLEIVPC SRVGHVFRKR HPYNFPEGNA
LTYIRNTKRT AEVWMDEYKQ YYYEARPSAI GKAFGSVATR IEQRKKMNCK SFRWYLENVY
PELTVPVKEA LPGIIKQGVN CLESQGQNTA GDFLLGMGIC RGSAKNPQPA QAWLFSDHLI
QQQGKCLAAT STLMSSPGSP VILQMCNPRE GKQKWRRKGS FIQHSVSGLC LETKPAQLVT
SKCQADAQAQ QWQLLPHT
