EOGT_HUMAN
ID EOGT_HUMAN Reviewed; 527 AA.
AC Q5NDL2; A8K2U1; B4DFH5; L7X1M5; Q6MZY0; Q6P985; Q6ZTV0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=EGF domain-specific O-linked N-acetylglucosamine transferase;
DE EC=2.4.1.255 {ECO:0000250|UniProtKB:Q8BYW9};
DE AltName: Full=Extracellular O-linked N-acetylglucosamine transferase;
DE Flags: Precursor;
GN Name=EOGT; Synonyms=AER61, C3orf64, EOGT1;
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] (ISOFORM 1), FUNCTION, AND MUTAGENESIS OF
RP 295-ASP--ASP-297.
RC TISSUE=Embryonic kidney;
RX PubMed=23671640; DOI=10.1371/journal.pone.0062835;
RA Muller R., Jenny A., Stanley P.;
RT "The EGF repeat-specific O-GlcNAc-transferase Eogt interacts with Notch
RT signaling and pyrimidine metabolism pathways in Drosophila.";
RL PLoS ONE 8:E62835-E62835(2013).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Kiefer-Meyer M.C., Pagny S., Durambure G., Faye L., Gomord V.,
RA Mollicone R., Oriol R.;
RT "Phylogeny of xylosyltransferases.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain cortex, Thymus, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 102-527.
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 69-527 (ISOFORM 1).
RC TISSUE=Esophageal carcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP VARIANTS AOS4 SER-207 AND GLN-377.
RX PubMed=23522784; DOI=10.1016/j.ajhg.2013.02.012;
RA Shaheen R., Aglan M., Keppler-Noreuil K., Faqeih E., Ansari S., Horton K.,
RA Ashour A., Zaki M.S., Al-Zahrani F., Cueto-Gonzalez A.M., Abdel-Salam G.,
RA Temtamy S., Alkuraya F.S.;
RT "Mutations in EOGT confirm the genetic heterogeneity of autosomal-recessive
RT Adams-Oliver syndrome.";
RL Am. J. Hum. Genet. 92:598-604(2013).
CC -!- FUNCTION: Catalyzes the transfer of a single N-acetylglucosamine from
CC UDP-GlcNAc to a serine or threonine residue in extracellular proteins
CC resulting in their modification with a beta-linked N-acetylglucosamine
CC (O-GlcNAc). Specifically glycosylates the Thr residue located between
CC the fifth and sixth conserved cysteines of folded EGF-like domains.
CC {ECO:0000269|PubMed:23671640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-
CC acetyl-beta-D-glucosaminyl)-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:48904, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:12251,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:90838; EC=2.4.1.255;
CC Evidence={ECO:0000250|UniProtKB:Q8BYW9};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-
CC (N-acetyl-beta-D-glucosaminyl)-L-threonyl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:48908, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:12252,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:90840; EC=2.4.1.255;
CC Evidence={ECO:0000250|UniProtKB:Q8BYW9};
CC -!- INTERACTION:
CC Q5NDL2-3; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-13052900, EBI-18304435;
CC Q5NDL2-3; Q9UKG4: SLC13A4; NbExp=3; IntAct=EBI-13052900, EBI-12808018;
CC Q5NDL2-3; Q8TBB6: SLC7A14; NbExp=3; IntAct=EBI-13052900, EBI-5235586;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5NDL2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5NDL2-2; Sequence=VSP_027897, VSP_027898;
CC Name=3;
CC IsoId=Q5NDL2-3; Sequence=VSP_027899;
CC -!- DISEASE: Adams-Oliver syndrome 4 (AOS4) [MIM:615297]: A form of Adams-
CC Oliver syndrome, a disorder characterized by the congenital absence of
CC skin (aplasia cutis congenita) in combination with transverse limb
CC defects. Aplasia cutis congenita can be located anywhere on the body,
CC but in the vast majority of the cases, it is present on the posterior
CC parietal region where it is often associated with an underlying defect
CC of the parietal bones. Limb abnormalities are typically limb truncation
CC defects affecting the distal phalanges or entire digits (true
CC ectrodactyly). Only rarely, metatarsals/metacarpals or more proximal
CC limb structures are also affected. Apart from transverse limb defects,
CC syndactyly, most commonly of second and third toes, can also be
CC observed. The clinical features are highly variable and can also
CC include cardiovascular malformations, brain abnormalities and vascular
CC defects such as cutis marmorata and dilated scalp veins.
CC {ECO:0000269|PubMed:23522784}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 61 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF83045.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAG57436.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; KC347596; AGC92970.1; -; mRNA.
DR EMBL; AJ868234; CAI30569.1; -; mRNA.
DR EMBL; AK126187; BAC86479.1; -; mRNA.
DR EMBL; AK290356; BAF83045.1; ALT_INIT; mRNA.
DR EMBL; AK294101; BAG57436.1; ALT_INIT; mRNA.
DR EMBL; AC109587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC060887; AAH60887.1; -; mRNA.
DR EMBL; BX640821; CAE45897.2; -; mRNA.
DR CCDS; CCDS2908.1; -. [Q5NDL2-3]
DR CCDS; CCDS63684.1; -. [Q5NDL2-1]
DR RefSeq; NP_001265618.1; NM_001278689.1. [Q5NDL2-1]
DR RefSeq; NP_775925.1; NM_173654.2. [Q5NDL2-3]
DR RefSeq; XP_005264800.1; XM_005264743.2. [Q5NDL2-1]
DR RefSeq; XP_016861694.1; XM_017006205.1. [Q5NDL2-1]
DR RefSeq; XP_016861695.1; XM_017006206.1. [Q5NDL2-1]
DR AlphaFoldDB; Q5NDL2; -.
DR SMR; Q5NDL2; -.
DR BioGRID; 130045; 77.
DR IntAct; Q5NDL2; 23.
DR STRING; 9606.ENSP00000373206; -.
DR CAZy; GT61; Glycosyltransferase Family 61.
DR GlyGen; Q5NDL2; 1 site.
DR iPTMnet; Q5NDL2; -.
DR PhosphoSitePlus; Q5NDL2; -.
DR BioMuta; EOGT; -.
DR DMDM; 74708096; -.
DR EPD; Q5NDL2; -.
DR jPOST; Q5NDL2; -.
DR MassIVE; Q5NDL2; -.
DR MaxQB; Q5NDL2; -.
DR PaxDb; Q5NDL2; -.
DR PeptideAtlas; Q5NDL2; -.
DR PRIDE; Q5NDL2; -.
DR ProteomicsDB; 1853; -.
DR ProteomicsDB; 63594; -. [Q5NDL2-1]
DR ProteomicsDB; 63595; -. [Q5NDL2-2]
DR ProteomicsDB; 63596; -. [Q5NDL2-3]
DR Antibodypedia; 15479; 49 antibodies from 17 providers.
DR DNASU; 285203; -.
DR Ensembl; ENST00000295571.9; ENSP00000295571.5; ENSG00000163378.14. [Q5NDL2-3]
DR Ensembl; ENST00000383701.8; ENSP00000373206.3; ENSG00000163378.14. [Q5NDL2-1]
DR Ensembl; ENST00000540764.5; ENSP00000443780.2; ENSG00000163378.14. [Q5NDL2-1]
DR Ensembl; ENST00000540955.5; ENSP00000444264.2; ENSG00000163378.14. [Q5NDL2-3]
DR GeneID; 285203; -.
DR KEGG; hsa:285203; -.
DR MANE-Select; ENST00000383701.8; ENSP00000373206.3; NM_001278689.2; NP_001265618.1.
DR UCSC; uc003dnk.5; human. [Q5NDL2-1]
DR CTD; 285203; -.
DR DisGeNET; 285203; -.
DR GeneCards; EOGT; -.
DR GeneReviews; EOGT; -.
DR HGNC; HGNC:28526; EOGT.
DR HPA; ENSG00000163378; Low tissue specificity.
DR MalaCards; EOGT; -.
DR MIM; 614789; gene.
DR MIM; 615297; phenotype.
DR neXtProt; NX_Q5NDL2; -.
DR OpenTargets; ENSG00000163378; -.
DR Orphanet; 974; Adams-Oliver syndrome.
DR PharmGKB; PA143485338; -.
DR VEuPathDB; HostDB:ENSG00000163378; -.
DR eggNOG; KOG4698; Eukaryota.
DR GeneTree; ENSGT00940000156493; -.
DR HOGENOM; CLU_039300_0_0_1; -.
DR InParanoid; Q5NDL2; -.
DR OMA; RFQTPQC; -.
DR OrthoDB; 567582at2759; -.
DR PhylomeDB; Q5NDL2; -.
DR TreeFam; TF313716; -.
DR BRENDA; 2.4.1.255; 2681.
DR PathwayCommons; Q5NDL2; -.
DR SignaLink; Q5NDL2; -.
DR BioGRID-ORCS; 285203; 7 hits in 1076 CRISPR screens.
DR ChiTaRS; EOGT; human.
DR GenomeRNAi; 285203; -.
DR Pharos; Q5NDL2; Tbio.
DR PRO; PR:Q5NDL2; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q5NDL2; protein.
DR Bgee; ENSG00000163378; Expressed in blood vessel layer and 183 other tissues.
DR ExpressionAtlas; Q5NDL2; baseline and differential.
DR Genevisible; Q5NDL2; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IBA:GO_Central.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016262; F:protein N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0097363; F:protein O-GlcNAc transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0097370; P:protein O-GlcNAcylation via threonine; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB.
DR InterPro; IPR007657; Glycosyltransferase_61.
DR PANTHER; PTHR20961; PTHR20961; 1.
DR Pfam; PF04577; Glyco_transf_61; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Reference proteome; Signal; Transferase.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..527
FT /note="EGF domain-specific O-linked N-acetylglucosamine
FT transferase"
FT /id="PRO_0000301970"
FT MOTIF 295..297
FT /note="Required for optimal activity"
FT MOTIF 524..527
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 208
FT /note="F -> C (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027897"
FT VAR_SEQ 209..527
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_027898"
FT VAR_SEQ 278..361
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027899"
FT VARIANT 207
FT /note="W -> S (in AOS4; dbSNP:rs587776993)"
FT /evidence="ECO:0000269|PubMed:23522784"
FT /id="VAR_070090"
FT VARIANT 377
FT /note="R -> Q (in AOS4; dbSNP:rs587776995)"
FT /evidence="ECO:0000269|PubMed:23522784"
FT /id="VAR_070091"
FT MUTAGEN 295..297
FT /note="DYD->AYA: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:23671640"
FT CONFLICT 199
FT /note="Q -> R (in Ref. 3; BAC86479)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="Y -> C (in Ref. 6; CAE45897)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="S -> F (in Ref. 3; BAG57436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 62011 MW; C34D267187BFDDA9 CRC64;
MLMLFVFGVL LHEVSLSGQN EAPPNTHSIP GEPLYNYASI RLPEEHIPFF LHNNRHIATV
CRKDSLCPYK KHLEKLKYCW GYEKSCKPEF RFGYPVCSYV DMGWTDTLES AEDIFWKQAD
FGYARERLEE MHVLCQPKET SDSSLVCSRY LQYCRATNLY LDLRNIKRNH DRFKEDFFQS
GEIGGHCKLD IRTLTSEGQR KSPLQSWFAE LQSYTQLNFR PIEDAKCDIV IEKPTYFMKL
DAGVNMYHHF CDFINLYITQ HVNNSFSTDV YIVMWDTSSY GYGDLFSDTW NAFTDYDVIH
LKTYDSKRVC FKEAVFSLLP RMRYGLFYNT PLISGCQNTG LFRAFAQHVL HRLNITQEGP
KDGKIRVTIL ARSTEYRKIL NQNELVNALK TVSTFEVQIV DYKYRELGFL DQLRITHNTD
IFIGMHGAGL THLLFLPDWA AVFELYNCED ERCYLDLARL RGVHYITWRR QNKVFPQDKG
HHPTLGEHPK FTNYSFDVEE FMYLVLQAAD HVLQHPKWPF KKKHDEL
