GT643_ARATH
ID GT643_ARATH Reviewed; 329 AA.
AC Q9C975; F4HS52; Q8LG66;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Glycosyltransferase family protein 64 C3 {ECO:0000303|PubMed:24905498};
DE Short=GT64 C3 {ECO:0000303|PubMed:24905498};
DE EC=2.4.1.- {ECO:0000305};
DE Flags: Precursor;
GN OrderedLocusNames=At1g80290 {ECO:0000312|Araport:AT1G80290};
GN ORFNames=F5I6.4 {ECO:0000312|EMBL:AAG52433.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|Proteomes:UP000006548};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP GENE FAMILY.
RX PubMed=16045474; DOI=10.1111/j.1365-313x.2005.02455.x;
RA Singh S.K., Eland C., Harholt J., Scheller H.V., Marchant A.;
RT "Cell adhesion in Arabidopsis thaliana is mediated by ECTOPICALLY PARTING
RT CELLS 1--a glycosyltransferase (GT64) related to the animal exostosins.";
RL Plant J. 43:384-397(2005).
RN [7]
RP WEB RESOURCE, AND GENE FAMILY.
RC STRAIN=cv. Columbia;
RX PubMed=24905498; DOI=10.1111/tpj.12577;
RA Lao J., Oikawa A., Bromley J.R., McInerney P., Suttangkakul A.,
RA Smith-Moritz A.M., Plahar H., Chiu T.-Y., Gonzalez Fernandez-Nino S.M.G.,
RA Ebert B., Yang F., Christiansen K.M., Hansen S.F., Stonebloom S.,
RA Adams P.D., Ronald P.C., Hillson N.J., Hadi M.Z., Vega-Sanchez M.E.,
RA Loque D., Scheller H.V., Heazlewood J.L.;
RT "The plant glycosyltransferase clone collection for functional genomics.";
RL Plant J. 79:517-529(2014).
CC -!- FUNCTION: Probable glycosyltransferase. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9ES89};
CC -!- PATHWAY: Protein modification; protein glycosylation. {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C975-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C975-2; Sequence=VSP_057105;
CC -!- SIMILARITY: Belongs to the glycosyltransferase 64 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=JBEI Glycosyltransferase (GT) Collection;
CC URL="http://gt.jbei.org/arabidopsis.html";
CC -!- WEB RESOURCE: Name=CAZY, the Carbohydrate Active enZYmes database;
CC URL="http://www.cazy.org/GT64_all.html";
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DR EMBL; AC018848; AAG52433.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36383.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE36384.1; -; Genomic_DNA.
DR EMBL; AK317465; BAH20131.1; -; mRNA.
DR EMBL; BT024721; ABD59059.1; -; mRNA.
DR EMBL; AY084439; AAM61012.1; -; mRNA.
DR PIR; D96834; D96834.
DR RefSeq; NP_001077854.1; NM_001084385.1. [Q9C975-2]
DR RefSeq; NP_565236.1; NM_106678.3. [Q9C975-1]
DR AlphaFoldDB; Q9C975; -.
DR SMR; Q9C975; -.
DR STRING; 3702.AT1G80290.2; -.
DR CAZy; GT64; Glycosyltransferase Family 64.
DR PaxDb; Q9C975; -.
DR PRIDE; Q9C975; -.
DR ProteomicsDB; 247204; -. [Q9C975-1]
DR EnsemblPlants; AT1G80290.1; AT1G80290.1; AT1G80290. [Q9C975-1]
DR EnsemblPlants; AT1G80290.2; AT1G80290.2; AT1G80290. [Q9C975-2]
DR GeneID; 844369; -.
DR Gramene; AT1G80290.1; AT1G80290.1; AT1G80290. [Q9C975-1]
DR Gramene; AT1G80290.2; AT1G80290.2; AT1G80290. [Q9C975-2]
DR KEGG; ath:AT1G80290; -.
DR Araport; AT1G80290; -.
DR TAIR; locus:2034225; AT1G80290.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_060636_0_0_1; -.
DR OrthoDB; 750735at2759; -.
DR PhylomeDB; Q9C975; -.
DR BioCyc; ARA:AT1G80290-MON; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:Q9C975; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C975; baseline and differential.
DR Genevisible; Q9C975; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR015338; GT64.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF09258; Glyco_transf_64; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Disulfide bond; Glycoprotein; Manganese;
KW Metal-binding; Reference proteome; Signal; Transferase.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..329
FT /note="Glycosyltransferase family protein 64 C3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430882"
FT REGION 268..284
FT /note="Substrate binding"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT ACT_SITE 230
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 118..123
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 139..141
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 141
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 226..230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT BINDING 271..284
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT CARBOHYD 99
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 228..287
FT /evidence="ECO:0000250|UniProtKB:Q9ES89"
FT VAR_SEQ 1
FT /note="M -> MPSASEADM (in isoform 2)"
FT /id="VSP_057105"
FT CONFLICT 87
FT /note="S -> R (in Ref. 5; AAM61012)"
SQ SEQUENCE 329 AA; 37703 MW; 60FED6ABA9F83B76 CRC64;
MGVKSVRFSI WFLFVVTDLV FCRTLSGDPD PCDATNQREF QKLRSDQITV LINGYSEYRI
PLLQTIVASY SSSSIVSSIL VLWGNPSTPD QLLDQLYQNL TQYSPGSASI SLIQQSSSSL
NARFLPRSSV DTRAVLICDD DVEIDQRSLE FAFSVWKSNP DRLVGTFVRS HGFDLQGKEW
IYTVHPDKYS IVLTKFMMMK QDYLFEYSCK GGVEMEEMRM IVDQMRNCED ILMNFVAADR
LRAGPIMVGA ERVRDWGDAR NEEVEERVRD VGLSSRRVEH RKRRGNCIRE FHRVMGKMPL
MYSYGKVVNS VGEQGLCRKA GKLVFCDRD
