ID   B4GN4_HUMAN             Reviewed;        1039 AA.
AC   Q76KP1; Q96LV2;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   23-FEB-2022, entry version 135.
DE   RecName: Full=N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-acetylgalactosaminyltransferase 1;
DE            Short=NGalNAc-T1;
DE            EC=2.4.1.244;
DE   AltName: Full=Beta-1,4-N-acetylgalactosaminyltransferase IV;
DE            Short=Beta4GalNAc-T4;
DE            Short=Beta4GalNAcT4;
GN   Name=B4GALNT4;
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, AND TISSUE SPECIFICITY.
RX   PubMed=15044014; DOI=10.1016/s0014-5793(04)00219-4;
RA   Gotoh M., Sato T., Kiyohara K., Kameyama A., Kikuchi N., Kwon Y.-D.,
RA   Ishizuka Y., Iwai T., Nakanishi H., Narimatsu H.;
RT   "Molecular cloning and characterization of beta1,4-N-
RT   acetylgalactosaminyltransferases IV synthesizing N,N'-
RT   diacetyllactosediamine.";
RL   FEBS Lett. 562:134-140(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 707-1039.
RC   TISSUE=Cerebellum;
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).
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.
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:15044014};
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC       {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in ovary, adult and fetal brain.
CC       Also expressed in fetal kidney and lung. {ECO:0000269|PubMed:15044014}.
CC   -!- SIMILARITY: Belongs to the chondroitin N-
CC       acetylgalactosaminyltransferase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB71566.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB089939; BAD06471.1; -; mRNA.
DR   EMBL; AK057774; BAB71566.1; ALT_INIT; mRNA.
DR   CCDS; CCDS7694.1; -.
DR   RefSeq; NP_848632.2; NM_178537.4.
DR   SMR; Q76KP1; -.
DR   BioGRID; 130784; 7.
DR   IntAct; Q76KP1; 7.
DR   STRING; 9606.ENSP00000328277; -.
DR   CAZy; GT7; Glycosyltransferase Family 7.
DR   GlyGen; Q76KP1; 1 site.
DR   iPTMnet; Q76KP1; -.
DR   PhosphoSitePlus; Q76KP1; -.
DR   BioMuta; B4GALNT4; -.
DR   DMDM; 74712926; -.
DR   EPD; Q76KP1; -.
DR   jPOST; Q76KP1; -.
DR   MassIVE; Q76KP1; -.
DR   PaxDb; Q76KP1; -.
DR   PeptideAtlas; Q76KP1; -.
DR   PRIDE; Q76KP1; -.
DR   ProteomicsDB; 68677; -.
DR   Antibodypedia; 64249; 5 antibodies from 5 providers.
DR   DNASU; 338707; -.
DR   Ensembl; ENST00000329962; ENSP00000328277; ENSG00000182272.
DR   GeneID; 338707; -.
DR   KEGG; hsa:338707; -.
DR   MANE-Select; ENST00000329962.11; ENSP00000328277.6; NM_178537.5; NP_848632.2.
DR   UCSC; uc001lpb.4; human.
DR   CTD; 338707; -.
DR   DisGeNET; 338707; -.
DR   GeneCards; B4GALNT4; -.
DR   HGNC; HGNC:26315; B4GALNT4.
DR   HPA; ENSG00000182272; Tissue enhanced (brain, ovary).
DR   MIM; 618560; gene.
DR   neXtProt; NX_Q76KP1; -.
DR   OpenTargets; ENSG00000182272; -.
DR   PharmGKB; PA142672565; -.
DR   VEuPathDB; HostDB:ENSG00000182272; -.
DR   eggNOG; KOG3588; Eukaryota.
DR   GeneTree; ENSGT01030000234702; -.
DR   HOGENOM; CLU_011195_0_0_1; -.
DR   InParanoid; Q76KP1; -.
DR   OMA; LEPCTYA; -.
DR   OrthoDB; 339331at2759; -.
DR   PhylomeDB; Q76KP1; -.
DR   TreeFam; TF318303; -.
DR   BRENDA; 2.4.1.244; 2681.
DR   BRENDA; 2.4.1.92; 2681.
DR   PathwayCommons; Q76KP1; -.
DR   SignaLink; Q76KP1; -.
DR   BioGRID-ORCS; 338707; 10 hits in 1043 CRISPR screens.
DR   ChiTaRS; B4GALNT4; human.
DR   GenomeRNAi; 338707; -.
DR   Pharos; Q76KP1; Tdark.
DR   PRO; PR:Q76KP1; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q76KP1; protein.
DR   Bgee; ENSG00000182272; Expressed in right hemisphere of cerebellum and 115 other tissues.
DR   ExpressionAtlas; Q76KP1; baseline and differential.
DR   Genevisible; Q76KP1; HS.
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: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   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
DR   PROSITE; PS51820; PA14; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Golgi apparatus; Membrane; Reference proteome; Signal-anchor;
KW   Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..1039
FT                   /note="N-acetyl-beta-glucosaminyl-glycoprotein 4-beta-N-
FT                   acetylgalactosaminyltransferase 1"
FT                   /id="PRO_0000252370"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..1039
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          108..278
FT                   /note="PA14"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01164"
FT   REGION          51..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          298..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..493
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          531..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          562..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..89
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..484
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..576
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        641..664
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         67
FT                   /note="A -> V (in dbSNP:rs34063493)"
FT                   /id="VAR_061096"
FT   VARIANT         88
FT                   /note="G -> V (in dbSNP:rs11822725)"
FT                   /id="VAR_061097"
FT   CONFLICT        942
FT                   /note="V -> M (in Ref. 2; BAB71566)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1039 AA;  116513 MW;  1D8D9E07AFC8DF70 CRC64;
     MPRLPVKKIR KQMKLLLLLL LLSCAAWLTY VHLGLVRQGR ALRQRLGYGR DGEKLTSETD
     GRGVHAAPST QRAEDSSESR EEEQAPEGRD LDMLFPGGAG RLPLNFTHQT PPWREEYKGQ
     VNLHVFEDWC GGAVGHLRRN LHFPLFPHTR TTVKKLAVSP KWKNYGLRIF GFIHPARDGD
     VQFSVASDDN SEFWLSLDES PAAAQLVAFV GKTGSEWTAP GEFTKFSSQV SKPRRLMASR
     RYYFELLHKQ DDRGSDHVEV GWRAFLPGLK FEVISSAHIS LYTDESALKM DHVAHVPQSP
     ASHVGGRPPQ EETSADMLRP DPRDTFFLTP RMESSSLENV LEPCAYAPTY VVKDFPIARY
     QGLQFVYLSF VYPNDYTRLT HMETDNKCFY RESPLYLERF GFYKYMKMDK EEGDEDEEDE
     VQRRAFLFLN PDDFLDDEDE GELLDSLEPT EAAPPRSGPQ SPAPAAPAQP GATLAPPTPP
     RPRDGGTPRH SRALSWAARA ARPLPLFLGR APPPRPAVEQ PPPKVYVTRV RPGQRASPRA
     PAPRAPWPPF PGVFLHPRPL PRVQLRAPPR PPRPHGRRTG GPQATQPRPP ARAQATQGGR
     EGQARTLGPA APTVDSNLSS EARPVTSFLS LSQVSGPQLP GEGEEEEEGE DDGAPGDEAA
     SEDSEEAAGP ALGRWREDAI DWQRTFSVGA VDFELLRSDW NDLRCNVSGN LQLPEAEAVD
     VTAQYMERLN ARHGGRFALL RIVNVEKRRD SARGSRFLLE LELQERGGGR LRLSEYVFLR
     LPGARVGDAD GESPEPAPAA SVRPDGRPEL CRPLRLAWRQ DVMVHFIVPV KNQARWVAQF
     LADMAALHAR TGDSRFSVVL VDFESEDMDV ERALRAARLP RYQYLRRTGN FERSAGLQAG
     VDAVEDASSI VFLCDLHIHF PPNILDGIRK HCVEGRLAFA PVVMRLSCGS SPRDPHGYWE
     VNGFGLFGIY KSDFDRVGGM NTEEFRDQWG GEDWELLDRV LQAGLEVERL RLRNFYHHYH
     SKRGMWSVRS RKGSRTGAS
//