PLGT2_DANRE
ID PLGT2_DANRE Reviewed; 500 AA.
AC Q7ZVE6; B0CM11; Q5RI39;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein O-glucosyltransferase 2 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q6UW63};
DE AltName: Full=KDEL motif-containing protein 1;
DE AltName: Full=Protein O-xylosyltransferase POGLUT2 {ECO:0000305};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:Q6UW63};
DE Flags: Precursor;
GN Name=poglut2; Synonyms=kdelc1; ORFNames=si:dkey-22a1.1, zgc:56065;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=18296487; DOI=10.1101/gr.7187808;
RA Bushell K.M., Soellner C., Schuster-Boeckler B., Bateman A., Wright G.J.;
RT "Large-scale screening for novel low-affinity extracellular protein
RT interactions.";
RL Genome Res. 18:622-630(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Protein glucosyltransferase that catalyzes the transfer of
CC glucose from UDP-glucose to a serine residue within the consensus
CC sequence peptide C-X-N-T-X-G-S-F-X-C. Can also catalyze the transfer of
CC xylose from UDP-xylose but less efficiently.
CC {ECO:0000250|UniProtKB:Q6UW63}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[EGF-like domain protein] + UDP-alpha-D-glucose = 3-O-
CC (beta-D-glucosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:58116, Rhea:RHEA-COMP:14610, Rhea:RHEA-COMP:16010,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:140576;
CC Evidence={ECO:0000250|UniProtKB:Q6UW63};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[EGF-like domain protein] + UDP-alpha-D-xylose = 3-O-
CC (beta-D-xylosyl)-L-seryl-[EGF-like domain protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:62016, Rhea:RHEA-COMP:16010, Rhea:RHEA-COMP:16011,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57632,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:132085;
CC Evidence={ECO:0000250|UniProtKB:Q6UW63};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q6UW63}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the KDELC family. {ECO:0000305}.
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DR EMBL; CU638807; CAP71956.1; -; mRNA.
DR EMBL; BX322637; CAI20990.1; -; Genomic_DNA.
DR EMBL; BC045893; AAH45893.1; -; mRNA.
DR RefSeq; NP_957225.1; NM_200931.1.
DR AlphaFoldDB; Q7ZVE6; -.
DR SMR; Q7ZVE6; -.
DR STRING; 7955.ENSDARP00000042296; -.
DR CAZy; GT90; Glycosyltransferase Family 90.
DR PaxDb; Q7ZVE6; -.
DR PRIDE; Q7ZVE6; -.
DR GeneID; 393905; -.
DR KEGG; dre:393905; -.
DR CTD; 79070; -.
DR ZFIN; ZDB-GENE-040426-878; poglut2.
DR eggNOG; KOG2458; Eukaryota.
DR InParanoid; Q7ZVE6; -.
DR OrthoDB; 547457at2759; -.
DR PhylomeDB; Q7ZVE6; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q7ZVE6; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0140561; F:EGF-domain serine glucosyltransferase activity; IEA:RHEA.
DR GO; GO:0140562; F:EGF-domain serine xylosyltransferase activity; IEA:RHEA.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR006598; CAP10.
DR InterPro; IPR017868; Filamin/ABP280_repeat-like.
DR InterPro; IPR001298; Filamin/ABP280_rpt.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR Pfam; PF00630; Filamin; 1.
DR Pfam; PF05686; Glyco_transf_90; 1.
DR SMART; SM00672; CAP10; 1.
DR SMART; SM00557; IG_FLMN; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
DR PROSITE; PS50194; FILAMIN_REPEAT; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Reference proteome; Signal; Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..500
FT /note="Protein O-glucosyltransferase 2"
FT /id="PRO_0000247165"
FT REPEAT 23..128
FT /note="Filamin"
FT MOTIF 497..500
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 26
FT /note="A -> P (in Ref. 1; CAP71956)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="T -> I (in Ref. 1; CAP71956)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="E -> V (in Ref. 1; CAP71956)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="Q -> K (in Ref. 1; CAP71956)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="I -> V (in Ref. 1; CAP71956)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="R -> K (in Ref. 2; CAI20990)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="Y -> C (in Ref. 1; CAP71956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 57802 MW; AD1C93F7F5A8D23E CRC64;
MLRKLLLLLM SCIIFLTRRS KAAAAASASK TLVWGPGLET NAVLPARFFF IQTVDTTGTN
FTTSPGENTF EVKITSPTEP YARIWIQILD RNDGSFLVRY RMYASYTDLH VEVLLKDKLV
GKSPYVLRGA VYHESCDCPE PDGALWEKNM HCPASFSQIE SDLSIFQSVD PDRNAHEIIQ
RFGKSHSLCH YTIKNNQVYI KTHGEHVGFR IFMDAFLLSL TRKVKLPDIE FFVNLGDWPL
EKRRASQNPS PVFSWCGSND TRDIVMPTYD LTESVLETMG RVSLDMMSVQ GHTGPVWEKK
INKGFWRGRD SRKERLELVK LARANTAMLD AALTNFFFFK HDESLYGPLV KHVSFFDFFK
YKYQINVDGT VAAYRLPYLL AGDSVVFKHD SIYYEHFYNE LQPWVHYIPF RSDLSDLLEK
IQWAKDHDEE AKKIALAGQQ FARTHLMGDS VFCYYHKLFQ KYAELQVTKP KVRDGMELVE
QPKDDLFPCY CARKKVRDEL
