B4GN3_HUMAN
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 03-AUG-2022, entry version 139.
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 iPTMnet; Q6L9W6; -.
DR PhosphoSitePlus; Q6L9W6; -.
DR BioMuta; B4GALNT3; -.
DR DMDM; 161789024; -.
DR jPOST; Q6L9W6; -.
DR MassIVE; Q6L9W6; -.
DR PaxDb; Q6L9W6; -.
DR PeptideAtlas; Q6L9W6; -.
DR PRIDE; Q6L9W6; -.
DR Antibodypedia; 2483; 82 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 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; 339331at2759; -.
DR PhylomeDB; Q6L9W6; -.
DR TreeFam; TF318303; -.
DR BRENDA; 2.4.1.244; 2681.
DR PathwayCommons; Q6L9W6; -.
DR SignaLink; Q6L9W6; -.
DR BioGRID-ORCS; 283358; 9 hits in 1060 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 147 other tissues.
DR ExpressionAtlas; Q6L9W6; baseline and differential.
DR Genevisible; Q6L9W6; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR008428; Chond_GalNAc.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR037524; PA14/GLEYA.
DR InterPro; IPR011658; PA14_dom.
DR Pfam; PF05679; CHGN; 1.
DR Pfam; PF07691; PA14; 1.
DR SMART; SM00758; PA14; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS51820; PA14; 1.
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
