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GAUTE_ARATH
ID   GAUTE_ARATH             Reviewed;         532 AA.
AC   Q8GWT1; Q9LF35;
DT   23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Probable galacturonosyltransferase 14;
DE            EC=2.4.1.-;
GN   Name=GAUT14; OrderedLocusNames=At5g15470; ORFNames=T20K14.80;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(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].
RC   STRAIN=cv. Columbia;
RX   PubMed=11910074; DOI=10.1126/science.1071006;
RA   Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA   Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA   Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA   Shinagawa A., Shinozaki K.;
RT   "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL   Science 296:141-145(2002).
RN   [4]
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   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=16540543; DOI=10.1073/pnas.0600120103;
RA   Sterling J.D., Atmodjo M.A., Inwood S.E., Kumar Kolli V.S., Quigley H.F.,
RA   Hahn M.G., Mohnen D.;
RT   "Functional identification of an Arabidopsis pectin biosynthetic
RT   homogalacturonan galacturonosyltransferase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5236-5241(2006).
RN   [6]
RP   TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=19825675; DOI=10.1093/mp/ssp062;
RA   Caffall K.H., Pattathil S., Phillips S.E., Hahn M.G., Mohnen D.;
RT   "Arabidopsis thaliana T-DNA mutants implicate GAUT genes in the
RT   biosynthesis of pectin and xylan in cell walls and seed testa.";
RL   Mol. Plant 2:1000-1014(2009).
CC   -!- FUNCTION: May be involved in pectin and/or xylans biosynthesis in cell
CC       walls. {ECO:0000250}.
CC   -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC       pass type II membrane protein {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, inflorescences, siliques,
CC       leaves and stems. {ECO:0000269|PubMed:19825675}.
CC   -!- DISRUPTION PHENOTYPE: No obvious phenotype. Increased galacturonic acid
CC       and Gal content in cell wall, but reduced xylose and rhamnose content.
CC       {ECO:0000269|PubMed:19825675}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC01746.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AL391143; CAC01746.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED92165.1; -; Genomic_DNA.
DR   EMBL; AK118651; BAC43247.1; -; mRNA.
DR   EMBL; BT005899; AAO64834.1; -; mRNA.
DR   PIR; T51525; T51525.
DR   RefSeq; NP_197051.2; NM_121551.4.
DR   AlphaFoldDB; Q8GWT1; -.
DR   STRING; 3702.AT5G15470.1; -.
DR   CAZy; GT8; Glycosyltransferase Family 8.
DR   PaxDb; Q8GWT1; -.
DR   PRIDE; Q8GWT1; -.
DR   ProteomicsDB; 222164; -.
DR   EnsemblPlants; AT5G15470.1; AT5G15470.1; AT5G15470.
DR   GeneID; 831400; -.
DR   Gramene; AT5G15470.1; AT5G15470.1; AT5G15470.
DR   KEGG; ath:AT5G15470; -.
DR   Araport; AT5G15470; -.
DR   TAIR; locus:2180947; AT5G15470.
DR   eggNOG; ENOG502QQKV; Eukaryota.
DR   HOGENOM; CLU_010770_5_1_1; -.
DR   InParanoid; Q8GWT1; -.
DR   OMA; TSIRETY; -.
DR   OrthoDB; 414752at2759; -.
DR   PhylomeDB; Q8GWT1; -.
DR   UniPathway; UPA00845; -.
DR   PRO; PR:Q8GWT1; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q8GWT1; baseline and differential.
DR   Genevisible; Q8GWT1; AT.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
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:0090406; C:pollen tube; IDA:TAIR.
DR   GO; GO:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; ISS:TAIR.
DR   GO; GO:0052325; P:cell wall pectin biosynthetic process; IGI:TAIR.
DR   GO; GO:0048358; P:mucilage pectin biosynthetic process; IMP:TAIR.
DR   GO; GO:0009555; P:pollen development; IGI:TAIR.
DR   GO; GO:0009860; P:pollen tube growth; IGI:TAIR.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029993; GAUT.
DR   InterPro; IPR002495; Glyco_trans_8.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   PANTHER; PTHR32116; PTHR32116; 1.
DR   Pfam; PF01501; Glyco_transf_8; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   2: Evidence at transcript level;
KW   Cell wall biogenesis/degradation; Glycoprotein; Glycosyltransferase;
KW   Golgi apparatus; Membrane; Reference proteome; Signal-anchor; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..532
FT                   /note="Probable galacturonosyltransferase 14"
FT                   /id="PRO_0000392564"
FT   TOPO_DOM        1..40
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        41..61
FT                   /note="Helical; Signal-anchor for type II membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        62..532
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        395
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        444
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        519
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   532 AA;  60823 MW;  861B689D5E772C62 CRC64;
     MQLHISPSMR SITISSSNEF IDLMKIKVAA RHISYRTLFH TILILAFLLP FVFILTAVVT
     LEGVNKCSSI DCLGRRIGPR LLGRVDDSER LARDFYKILN EVSTQEIPDG LKLPNSFSQL
     VSDMKNNHYD AKTFALVLRA MMEKFERDMR ESKFAELMNK HFAASSIPKG IHCLSLRLTD
     EYSSNAHARR QLPSPEFLPV LSDNAYHHFI LSTDNILAAS VVVSSAVQSS SKPEKIVFHI
     ITDKKTYAGM HSWFALNSVA PAIVEVKGVH QFDWLTRENV PVLEAVESHN GVRDYYHGNH
     VAGANLTETT PRTFASKLQS RSPKYISLLN HLRIYIPELF PNLDKVVFLD DDIVVQGDLT
     PLWDVDLGGK VNGAVETCRG EDEWVMSKRL RNYFNFSHPL IAKHLDPEEC AWAYGMNIFD
     LQAWRKTNIR ETYHSWLREN LKSNLTMWKL GTLPPALIAF KGHVHIIDSS WHMLGLGYQS
     KTNIENVKKA AVIHYNGQSK PWLEIGFEHL RPFWTKYVNY SNDFIKNCHI LE
 
 
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