GATL1_ARATH
ID GATL1_ARATH Reviewed; 351 AA.
AC Q9LN68; Q8L5Z6; Q8LF94;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Probable galacturonosyltransferase-like 1;
DE EC=2.4.1.-;
DE AltName: Full=Protein GAOLAOZHUANGREN 1;
DE AltName: Full=Protein PARVUS;
GN Name=GATL1; Synonyms=GLZ1, PARVUS; OrderedLocusNames=At1g19300;
GN ORFNames=F18O14.2;
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], FUNCTION, INDUCTION, TISSUE SPECIFICITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15010604; DOI=10.1023/b:plan.0000019074.60542.6c;
RA Lao N.T., Long D., Kiang S., Coupland G., Shoue D.A., Carpita N.C.,
RA Kavanagh T.A.;
RT "Mutation of a family 8 glycosyltransferase gene alters cell wall
RT carbohydrate composition and causes a humidity-sensitive semi-sterile dwarf
RT phenotype in Arabidopsis.";
RL Plant Mol. Biol. 53:687-701(2003).
RN [2]
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 [3]
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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=15564529; DOI=10.1093/pcp/pch168;
RA Shao M., Zheng H., Hu Y., Liu D., Jang J.C., Ma H., Huang H.;
RT "The GAOLAOZHUANGREN1 gene encodes a putative glycosyltransferase that is
RT critical for normal development and carbohydrate metabolism.";
RL Plant Cell Physiol. 45:1453-1460(2004).
RN [8]
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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=17991630; DOI=10.1093/pcp/pcm155;
RA Lee C., Zhong R., Richardson E.A., Himmelsbach D.S., McPhail B.T., Ye Z.H.;
RT "The PARVUS gene is expressed in cells undergoing secondary wall thickening
RT and is essential for glucuronoxylan biosynthesis.";
RL Plant Cell Physiol. 48:1659-1672(2007).
CC -!- FUNCTION: Required for the biosynthesis of the tetrasaccharide primer
CC sequence, beta-D-Xyl-(1,3)-alpha-l-Rha-(1,2)-alpha-D-GalA-(1,4)-D-Xyl,
CC located at the reducing end of glucuronoxylan. Might catalyze the
CC transfer of the reducing Xyl residue onto a protein acceptor in the
CC endoplasmic reticulum, which is then transported to the Golgi where the
CC subsequent additions of sugar residues take place.
CC {ECO:0000269|PubMed:15010604, ECO:0000269|PubMed:15564529,
CC ECO:0000269|PubMed:17991630}.
CC -!- PATHWAY: Glycan metabolism; pectin biosynthesis.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17991630}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:17991630}.
CC -!- TISSUE SPECIFICITY: Expressed in stems, leaves, flowers, siliques and
CC roots. Detected in fibers and xylem cells undergoing secondary wall
CC thickening. {ECO:0000269|PubMed:15010604, ECO:0000269|PubMed:15564529,
CC ECO:0000269|PubMed:17991630}.
CC -!- INDUCTION: By light. {ECO:0000269|PubMed:15010604}.
CC -!- DISRUPTION PHENOTYPE: Dwarf phenotype. Severe reduction in the
CC mechanical strength of stems and collapsed vessels. Reduced fertility.
CC {ECO:0000269|PubMed:15010604, ECO:0000269|PubMed:15564529,
CC ECO:0000269|PubMed:17991630}.
CC -!- MISCELLANEOUS: The name gaolaozhuangren came from a group of small
CC people in a modern Chinese novel.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 8 family. {ECO:0000305}.
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DR EMBL; AC025808; AAF79456.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE29827.1; -; Genomic_DNA.
DR EMBL; AF424600; AAL11594.1; -; mRNA.
DR EMBL; AY099796; AAM20647.1; -; mRNA.
DR EMBL; AY084974; AAM61534.1; -; mRNA.
DR EMBL; BT025257; ABF19010.1; -; mRNA.
DR RefSeq; NP_564077.1; NM_101787.3.
DR AlphaFoldDB; Q9LN68; -.
DR SMR; Q9LN68; -.
DR BioGRID; 23751; 1.
DR IntAct; Q9LN68; 1.
DR STRING; 3702.AT1G19300.1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR SwissPalm; Q9LN68; -.
DR PaxDb; Q9LN68; -.
DR PRIDE; Q9LN68; -.
DR ProteomicsDB; 248561; -.
DR EnsemblPlants; AT1G19300.1; AT1G19300.1; AT1G19300.
DR GeneID; 838512; -.
DR Gramene; AT1G19300.1; AT1G19300.1; AT1G19300.
DR KEGG; ath:AT1G19300; -.
DR Araport; AT1G19300; -.
DR TAIR; locus:2016432; AT1G19300.
DR eggNOG; ENOG502QTN8; Eukaryota.
DR HOGENOM; CLU_034713_0_0_1; -.
DR InParanoid; Q9LN68; -.
DR OMA; INPMWHI; -.
DR OrthoDB; 1520602at2759; -.
DR PhylomeDB; Q9LN68; -.
DR UniPathway; UPA00845; -.
DR PRO; PR:Q9LN68; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LN68; baseline and differential.
DR Genevisible; Q9LN68; AT.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047262; F:polygalacturonate 4-alpha-galacturonosyltransferase activity; ISS:TAIR.
DR GO; GO:0052386; P:cell wall thickening; IMP:TAIR.
DR GO; GO:0010417; P:glucuronoxylan biosynthetic process; IMP:TAIR.
DR GO; GO:0048366; P:leaf development; IMP:TAIR.
DR GO; GO:0032504; P:multicellular organism reproduction; IMP:TAIR.
DR GO; GO:0045489; P:pectin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0010051; P:xylem and phloem pattern formation; IMP:TAIR.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002495; Glyco_trans_8.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01501; Glyco_transf_8; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Glycoprotein;
KW Glycosyltransferase; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="Probable galacturonosyltransferase-like 1"
FT /id="PRO_0000392603"
FT TOPO_DOM 1..5
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 6..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..351
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 204
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 67
FT /note="V -> M (in Ref. 6; AAM61534)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="A -> T (in Ref. 4; AAM20647)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="V -> I (in Ref. 6; AAM61534)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 39020 MW; 51E6E533EAF9183E CRC64;
MSQHLLLLIL LSLLLLHKPI SATTIIQKFK EAPQFYNSAD CPLIDDSESD DDVVAKPIFC
SRRAVHVAMT LDAAYIRGSV AAVLSVLQHS SCPENIVFHF VASASADASS LRATISSSFP
YLDFTVYVFN VSSVSRLISS SIRSALDCPL NYARSYLADL LPPCVRRVVY LDSDLILVDD
IAKLAATDLG RDSVLAAPEY CNANFTSYFT STFWSNPTLS LTFADRKACY FNTGVMVIDL
SRWREGAYTS RIEEWMAMQK RMRIYELGSL PPFLLVFAGL IKPVNHRWNQ HGLGGDNFRG
LCRDLHPGPV SLLHWSGKGK PWARLDAGRP CPLDALWAPY DLLQTPFALD S
