ID   B4GN3_HUMAN             Reviewed;         998 AA.
AC   Q6L9W6; Q6ZNC1; Q8N7T6;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   24-JAN-2024, entry version 146.
DE   RecName: Full=Beta-1,4-N-acetylgalactosaminyltransferase 3;
DE            Short=B4GalNAcT3;
DE            Short=Beta4GalNAc-T3;
DE            Short=Beta4GalNAcT3;
DE            EC=2.4.1.244;
DE   AltName: Full=Beta-1,4-N-acetylgalactosaminyltransferase III;
DE   AltName: Full=N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 2;
DE            Short=NGalNAc-T2;
GN   Name=B4GALNT3;
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], CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND
RP   VARIANT ARG-411.
RX   PubMed=12966086; DOI=10.1074/jbc.m308857200;
RA   Sato T., Gotoh M., Kiyohara K., Kameyama A., Kubota T., Kikuchi N.,
RA   Ishizuka Y., Iwasaki H., Togayachi A., Kudo T., Ohkura T., Nakanishi H.,
RA   Narimatsu H.;
RT   "Molecular cloning and characterization of a novel human beta 1,4-N-
RT   acetylgalactosaminyltransferase, beta 4GalNAc-T3, responsible for the
RT   synthesis of N,N'-diacetyllactosediamine, galNAc beta 1-4GlcNAc.";
RL   J. Biol. Chem. 278:47534-47544(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 540-998.
RC   TISSUE=Testis, and Tongue;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [4]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16728562; DOI=10.1093/glycob/cwl005;
RA   Ikehara Y., Sato T., Niwa T., Nakamura S., Gotoh M., Ikehara S.K.,
RA   Kiyohara K., Aoki C., Iwai T., Nakanishi H., Hirabayashi J., Tatematsu M.,
RA   Narimatsu H.;
RT   "Apical Golgi localization of N,N'-diacetyllactosediamine synthase,
RT   beta4GalNAc-T3, is responsible for LacdiNAc expression on gastric mucosa.";
RL   Glycobiology 16:777-785(2006).
CC   -!- FUNCTION: Transfers N-acetylgalactosamine (GalNAc) from UDP-GalNAc to
CC       N-acetylglucosamine-beta-benzyl with a beta-1,4-linkage to form N,N'-
CC       diacetyllactosediamine, GalNAc-beta-1,4-GlcNAc structures in N-linked
CC       glycans and probably O-linked glycans. Mediates the N,N'-
CC       diacetyllactosediamine formation on gastric mucosa.
CC       {ECO:0000269|PubMed:16728562}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetyl-beta-D-glucosaminyl derivative + UDP-N-acetyl-
CC         alpha-D-galactosamine = an N-acetyl-beta-D-galactosaminyl-(1->4)-N-
CC         acetyl-beta-D-glucosaminyl derivative + H(+) + UDP;
CC         Xref=Rhea:RHEA:20493, ChEBI:CHEBI:15378, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:61631, ChEBI:CHEBI:67138, ChEBI:CHEBI:138027;
CC         EC=2.4.1.244; Evidence={ECO:0000269|PubMed:12966086};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000269|PubMed:16728562}; Single-pass type II membrane protein
CC       {ECO:0000269|PubMed:16728562}. Note=Localizes to apical Golgi.
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis, colon and stomach.
CC       Weakly expressed in other tissues. {ECO:0000269|PubMed:12966086}.
CC   -!- SIMILARITY: Belongs to the chondroitin N-
CC       acetylgalactosaminyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC05141.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAD18454.1; Type=Miscellaneous discrepancy; Note=Probable intron retention.; Evidence={ECO:0000305};
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DR   EMBL; AB089940; BAD02449.1; -; mRNA.
DR   EMBL; AK097681; BAC05141.1; ALT_INIT; mRNA.
DR   EMBL; AK131277; BAD18454.1; ALT_SEQ; mRNA.
DR   EMBL; AC005844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC006205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS8504.1; -.
DR   RefSeq; NP_775864.3; NM_173593.3.
DR   AlphaFoldDB; Q6L9W6; -.
DR   SMR; Q6L9W6; -.
DR   BioGRID; 129537; 24.
DR   IntAct; Q6L9W6; 3.
DR   STRING; 9606.ENSP00000266383; -.
DR   CAZy; GT7; Glycosyltransferase Family 7.
DR   GlyGen; Q6L9W6; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q6L9W6; -.
DR   PhosphoSitePlus; Q6L9W6; -.
DR   BioMuta; B4GALNT3; -.
DR   DMDM; 161789024; -.
DR   jPOST; Q6L9W6; -.
DR   MassIVE; Q6L9W6; -.
DR   PaxDb; 9606-ENSP00000266383; -.
DR   PeptideAtlas; Q6L9W6; -.
DR   ProteomicsDB; 66562; -.
DR   Antibodypedia; 2483; 86 antibodies from 16 providers.
DR   DNASU; 283358; -.
DR   Ensembl; ENST00000266383.10; ENSP00000266383.5; ENSG00000139044.12.
DR   GeneID; 283358; -.
DR   KEGG; hsa:283358; -.
DR   MANE-Select; ENST00000266383.10; ENSP00000266383.5; NM_173593.4; NP_775864.3.
DR   UCSC; uc001qii.2; human.
DR   AGR; HGNC:24137; -.
DR   CTD; 283358; -.
DR   DisGeNET; 283358; -.
DR   GeneCards; B4GALNT3; -.
DR   HGNC; HGNC:24137; B4GALNT3.
DR   HPA; ENSG00000139044; Tissue enhanced (stomach).
DR   MIM; 612220; gene.
DR   neXtProt; NX_Q6L9W6; -.
DR   OpenTargets; ENSG00000139044; -.
DR   PharmGKB; PA142672564; -.
DR   VEuPathDB; HostDB:ENSG00000139044; -.
DR   eggNOG; KOG3588; Eukaryota.
DR   GeneTree; ENSGT01050000244857; -.
DR   HOGENOM; CLU_011195_0_0_1; -.
DR   InParanoid; Q6L9W6; -.
DR   OMA; VDPHLQF; -.
DR   OrthoDB; 2907318at2759; -.
DR   PhylomeDB; Q6L9W6; -.
DR   TreeFam; TF318303; -.
DR   BRENDA; 2.4.1.244; 2681.
DR   PathwayCommons; Q6L9W6; -.
DR   SignaLink; Q6L9W6; -.
DR   BioGRID-ORCS; 283358; 13 hits in 1141 CRISPR screens.
DR   ChiTaRS; B4GALNT3; human.
DR   GenomeRNAi; 283358; -.
DR   Pharos; Q6L9W6; Tbio.
DR   PRO; PR:Q6L9W6; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q6L9W6; Protein.
DR   Bgee; ENSG00000139044; Expressed in apex of heart and 149 other cell types or tissues.
DR   ExpressionAtlas; Q6L9W6; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0008376; F:acetylgalactosaminyltransferase activity; IDA:HGNC-UCL.
DR   GO; GO:0033842; F:N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR008428; Chond_GalNAc.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   InterPro; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   PANTHER; PTHR12369:SF15; BETA-1,4-N-ACETYLGALACTOSAMINYLTRANSFERASE 3; 1.
DR   PANTHER; PTHR12369; CHONDROITIN SYNTHASE; 1.
DR   Pfam; PF05679; CHGN; 1.
DR   Pfam; PF07691; PA14; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
DR   PROSITE; PS51820; PA14; 1.
DR   Genevisible; Q6L9W6; HS.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome;
KW   Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..998
FT                   /note="Beta-1,4-N-acetylgalactosaminyltransferase 3"
FT                   /id="PRO_0000252368"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        46..998
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          117..278
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   REGION          302..326
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..562
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         59
FT                   /note="G -> S (in dbSNP:rs2075033)"
FT                   /id="VAR_027842"
FT   VARIANT         265
FT                   /note="R -> Q (in dbSNP:rs11063529)"
FT                   /id="VAR_027843"
FT   VARIANT         411
FT                   /note="K -> R (in dbSNP:rs7298766)"
FT                   /evidence="ECO:0000269|PubMed:12966086"
FT                   /id="VAR_027844"
FT   VARIANT         768
FT                   /note="R -> Q (in dbSNP:rs11063570)"
FT                   /id="VAR_048717"
FT   VARIANT         992
FT                   /note="R -> H (in dbSNP:rs36078145)"
FT                   /id="VAR_048718"
SQ   SEQUENCE   998 AA;  114975 MW;  1FDA8490C8FA1D0B CRC64;
     MGSPRAARPP LLLRPVKLLR RRFRLLLALA VVSVGLWTLY LELVASAQVG GNPLNRRYGS
     WRELAKALAS RNIPAVDPHL QFYHPQRLSL EDHDIDQGVS SNSSYLKWNK PVPWLSEFRG
     RANLHVFEDW CGSSIQQLRR NLHFPLYPHI RTTLRKLAVS PKWTNYGLRI FGYLHPFTDG
     KIQFAIAADD NAEFWLSLDD QVSGLQLLAS VGKTGKEWTA PGEFGKFRSQ ISKPVSLSAS
     HRYYFEVLHK QNEEGTDHVE VAWRRNDPGA KFTIIDSLSL SLFTNETFLQ MDEVGHIPQT
     AASHVDSSNA LPRDEQPPAD MLRPDPRDTL YRVPLIPKSH LRHVLPDCPY KPSYLVDGLP
     LQRYQGLRFV HLSFVYPNDY TRLSHMETHN KCFYQENAYY QDRFSFQEYI KIDQPEKQGL
     EQPGFEENLL EESQYGEVAE ETPASNNQNA RMLEGRQTPA STLEQDATDY RLRSLRKLLA
     QPREGLLAPF SKRNSTASFP GRTSHIPVQQ PEKRKQKPSP EPSQDSPHSD KWPPGHPVKN
     LPQMRGPRPR PAGDSPRKTQ WLNQVESYIA EQRRGDRMRP QAPGRGWHGE EEVVAAAGQE
     GQVEGEEEGE EEEEEEDMSE VFEYVPVFDP VVNWDQTFSA RNLDFQALRT DWIDLSCNTS
     GNLLLPEQEA LEVTRVFLKK LNQRSRGRYQ LQRIVNVEKR QDQLRGGRYL LELELLEQGQ
     RVVRLSEYVS ARGWQGIDPA GGEEVEARNL QGLVWDPHNR RRQVLNTRAQ EPKLCWPQGF
     SWSHRAVVHF VVPVKNQARW VQQFIKDMEN LFQVTGDPHF NIVITDYSSE DMDVEMALKR
     SKLRSYQYVK LSGNFERSAG LQAGIDLVKD PHSIIFLCDL HIHFPAGVID AIRKHCVEGK
     MAFAPMVMRL HCGATPQWPE GYWEVNGFGL LGIYKSDLDR IGGMNTKEFR DRWGGEDWEL
     LDRILQAGLD VERLSLRNFF HHFHSKRGMW SRRQMKTL
//