GT14_ARATH
ID GT14_ARATH Reviewed; 521 AA.
AC Q84R16; O23260;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 116.
DE RecName: Full=Probable xyloglucan galactosyltransferase GT14 {ECO:0000305};
DE EC=2.4.1.- {ECO:0000305};
DE AltName: Full=Glycosyltransferase 14 {ECO:0000303|PubMed:15020758};
DE Short=AtGT14 {ECO:0000303|PubMed:15020758};
GN Name=GT14 {ECO:0000303|PubMed:15020758};
GN OrderedLocusNames=At4g13990 {ECO:0000312|Araport:AT4G13990};
GN ORFNames=dl3035w {ECO:0000312|EMBL:CAB10178.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9461215; DOI=10.1038/35140;
RA Bevan M., Bancroft I., Bent E., Love K., Goodman H.M., Dean C.,
RA Bergkamp R., Dirkse W., van Staveren M., Stiekema W., Drost L., Ridley P.,
RA Hudson S.-A., Patel K., Murphy G., Piffanelli P., Wedler H., Wedler E.,
RA Wambutt R., Weitzenegger T., Pohl T., Terryn N., Gielen J., Villarroel R.,
RA De Clercq R., van Montagu M., Lecharny A., Aubourg S., Gy I., Kreis M.,
RA Lao N., Kavanagh T., Hempel S., Kotter P., Entian K.-D., Rieger M.,
RA Schaefer M., Funk B., Mueller-Auer S., Silvey M., James R., Monfort A.,
RA Pons A., Puigdomenech P., Douka A., Voukelatou E., Milioni D.,
RA Hatzopoulos P., Piravandi E., Obermaier B., Hilbert H., Duesterhoeft A.,
RA Moores T., Jones J.D.G., Eneva T., Palme K., Benes V., Rechmann S.,
RA Ansorge W., Cooke R., Berger C., Delseny M., Voet M., Volckaert G.,
RA Mewes H.-W., Klosterman S., Schueller C., Chalwatzis N.;
RT "Analysis of 1.9 Mb of contiguous sequence from chromosome 4 of Arabidopsis
RT thaliana.";
RL Nature 391:485-488(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=15020758; DOI=10.1104/pp.103.036285;
RA Li X., Cordero I., Caplan J., Moelhoej M., Reiter W.D.;
RT "Molecular analysis of 10 coding regions from Arabidopsis that are
RT homologous to the MUR3 xyloglucan galactosyltransferase.";
RL Plant Physiol. 134:940-950(2004).
CC -!- FUNCTION: Functions in xyloglucan synthesis by adding side chains to
CC the xylosylated glucan backbone. Involved in the galactosylation of
CC hemicellulose xyloglucan. {ECO:0000250|UniProtKB:F4K6F1}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q7XJ98}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q7XJ98}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, hypocotyls, cotyledons, leaves,
CC stems, stamens and carpels. {ECO:0000269|PubMed:15020758}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 47 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB10178.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78441.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KJ138760; AHL38700.1; -; mRNA.
DR EMBL; Z97335; CAB10178.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161537; CAB78441.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE83357.1; -; Genomic_DNA.
DR EMBL; CP002687; ANM67227.1; -; Genomic_DNA.
DR EMBL; BT006172; AAP04155.1; -; mRNA.
DR PIR; H71400; H71400.
DR RefSeq; NP_001319928.1; NM_001340898.1.
DR RefSeq; NP_193135.2; NM_117474.3.
DR AlphaFoldDB; Q84R16; -.
DR STRING; 3702.AT4G13990.1; -.
DR CAZy; GT47; Glycosyltransferase Family 47.
DR PaxDb; Q84R16; -.
DR PRIDE; Q84R16; -.
DR ProteomicsDB; 247300; -.
DR EnsemblPlants; AT4G13990.1; AT4G13990.1; AT4G13990.
DR EnsemblPlants; AT4G13990.2; AT4G13990.2; AT4G13990.
DR GeneID; 827035; -.
DR Gramene; AT4G13990.1; AT4G13990.1; AT4G13990.
DR Gramene; AT4G13990.2; AT4G13990.2; AT4G13990.
DR KEGG; ath:AT4G13990; -.
DR Araport; AT4G13990; -.
DR TAIR; locus:2129281; AT4G13990.
DR eggNOG; KOG1021; Eukaryota.
DR HOGENOM; CLU_012659_2_1_1; -.
DR InParanoid; Q84R16; -.
DR OMA; VLLCFDY; -.
DR OrthoDB; 789556at2759; -.
DR PhylomeDB; Q84R16; -.
DR PRO; PR:Q84R16; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q84R16; baseline and differential.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR004263; Exostosin.
DR InterPro; IPR040911; Exostosin_GT47.
DR PANTHER; PTHR11062; PTHR11062; 1.
DR Pfam; PF03016; Exostosin; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..521
FT /note="Probable xyloglucan galactosyltransferase GT14"
FT /id="PRO_0000435996"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 31..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..521
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT REGION 72..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 81
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 411
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 521 AA; 60991 MW; 609410A9DEFE337D CRC64;
MRPKNYSQME KPISITTGKF RTNNNNNHNN VWFVVPLFFI LCFVLLCFDY SALFTDTDET
AFSIPDVTQK STSSEFTKDD NFSRFPDDPS PDSSCSGRYI YVHELPYRFN GDLLDNCFKI
TRGTEKDICP YIENYGFGPV IKNYENVLLK QSWFTTNQFM LEVIFHNKMI NYRCLTNDSS
LASAVFVPFY AGLDMSRYLW GFNITVRDSS SHELMDWLVV QKEWGRMSGR DHFLVSGRIA
WDFRRQTDNE SDWGSKLRFL PESRNMSMLS IESSSWKNDY AIPYPTCFHP RSVDEIVEWQ
ELMRSRKREY LFTFAGAPRP EYKDSVRGKI IDECLESKKQ CYLLDCNYGN VNCDNPVNVM
KVFRNSVFCL QPPGDSYTRR SMFDSILAGC IPVFFHPGTA YAQYKWHLPK NHSSYSVYLP
VKDVKEWNIK IKERLIEIPE ERVVRLREEV IRLIPKVVYA DPKYGSDGSE DAFELAVKGM
LERIEEVREM MRQGKDGSDG FDDRDDYKYT FSPYEEPQVL A