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   27-MAR-2024, entry version 168.
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.
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; 22.
DR   IntAct; Q8N428; 9.
DR   STRING; 9606.ENSP00000336729; -.
DR   CAZy; CBM13; Carbohydrate-Binding Module Family 13.
DR   CAZy; GT27; Glycosyltransferase Family 27.
DR   GlyGen; Q8N428; 4 sites, 1 O-linked glycan (4 sites).
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; 9606-ENSP00000336729; -.
DR   PeptideAtlas; Q8N428; -.
DR   ProteomicsDB; 71869; -. [Q8N428-1]
DR   ProteomicsDB; 71870; -. [Q8N428-2]
DR   Pumba; Q8N428; -.
DR   Antibodypedia; 25033; 84 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   AGR; HGNC:23233; -.
DR   CTD; 57452; -.
DR   DisGeNET; 57452; -.
DR   GeneCards; GALNT16; -.
DR   HGNC; HGNC:23233; GALNT16.
DR   HPA; ENSG00000100626; Tissue enhanced (heart).
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; VKMELCN; -.
DR   OrthoDB; 202750at2759; -.
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; 14 hits in 1133 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 146 other cell types or tissues.
DR   ExpressionAtlas; Q8N428; 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: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; 2.80.10.50; -; 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   PANTHER; PTHR11675; N-ACETYLGALACTOSAMINYLTRANSFERASE; 1.
DR   PANTHER; PTHR11675:SF3; POLYPEPTIDE N-ACETYLGALACTOSAMINYLTRANSFERASE 16; 1.
DR   Pfam; PF00535; Glycos_transf_2; 1.
DR   Pfam; PF00652; Ricin_B_lectin; 1.
DR   SMART; SM00458; RICIN; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   SUPFAM; SSF50370; Ricin B-like lectins; 1.
DR   PROSITE; PS50231; RICIN_B_LECTIN; 1.
DR   Genevisible; Q8N428; HS.
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
//