SRGT1_ARATH
ID SRGT1_ARATH Reviewed; 802 AA.
AC Q8VYF9; Q9S7Y6;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Peptidyl serine alpha-galactosyltransferase {ECO:0000303|PubMed:24914209};
DE Short=AtSGT1 {ECO:0000303|PubMed:24914209};
DE EC=2.4.1.- {ECO:0000305};
DE Flags: Precursor;
GN Name=SERGT1 {ECO:0000303|PubMed:25944827};
GN Synonyms=SGT1 {ECO:0000303|PubMed:24914209};
GN OrderedLocusNames=At3g01720 {ECO:0000312|Araport:AT3G01720};
GN ORFNames=F28J7.5 {ECO:0000312|EMBL:AAF03428.1},
GN F4P13.27 {ECO:0000312|EMBL:AAF01555.1};
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|EMBL:AAL59929.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=24914209; DOI=10.1074/jbc.m114.553933;
RA Saito F., Suyama A., Oka T., Yoko-o T., Matsuoka K., Jigami Y., Shimma Y.;
RT "Identification of a novel peptidyl serine alpha-galactosyltransferase gene
RT family in plants.";
RL J. Biol. Chem. 289:20405-20420(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 DISRUPTION PHENOTYPE.
RX PubMed=25944827; DOI=10.1104/pp.114.255521;
RA Velasquez S.M., Marzol E., Borassi C., Pol-Fachin L., Ricardi M.M.,
RA Mangano S., Juarez S.P., Salter J.D., Dorosz J.G., Marcus S.E., Knox J.P.,
RA Dinneny J.R., Iusem N.D., Verli H., Estevez J.M.;
RT "Low sugar is not always good: impact of specific o-glycan defects on tip
RT growth in Arabidopsis.";
RL Plant Physiol. 168:808-813(2015).
CC -!- FUNCTION: Glycosyltransferase involved in the O-galactosylation of
CC several proteins including extensins. Catalyzes the transfer of alpha-
CC galactosyl to Ser residues. Hydroxylation of proline residues adjacent
CC to the serine acceptor is required for activity.
CC {ECO:0000269|PubMed:24914209}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:24914209}; Single-pass type I membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Reduced root hair length (PubMed:25944827).
CC Longer roots and larger leaves (PubMed:24914209).
CC {ECO:0000269|PubMed:24914209, ECO:0000269|PubMed:25944827}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF01555.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF03428.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB617523; BAL63044.1; -; mRNA.
DR EMBL; AC009325; AAF01555.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC010797; AAF03428.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE73707.1; -; Genomic_DNA.
DR EMBL; AY072107; AAL59929.1; -; mRNA.
DR EMBL; AY096685; AAM20319.1; -; mRNA.
DR RefSeq; NP_566148.2; NM_111038.4.
DR AlphaFoldDB; Q8VYF9; -.
DR STRING; 3702.AT3G01720.1; -.
DR iPTMnet; Q8VYF9; -.
DR PaxDb; Q8VYF9; -.
DR PRIDE; Q8VYF9; -.
DR ProteomicsDB; 226711; -.
DR EnsemblPlants; AT3G01720.1; AT3G01720.1; AT3G01720.
DR GeneID; 821091; -.
DR Gramene; AT3G01720.1; AT3G01720.1; AT3G01720.
DR KEGG; ath:AT3G01720; -.
DR Araport; AT3G01720; -.
DR TAIR; locus:2082314; AT3G01720.
DR eggNOG; ENOG502QQG8; Eukaryota.
DR HOGENOM; CLU_018998_1_0_1; -.
DR InParanoid; Q8VYF9; -.
DR OMA; NLECINT; -.
DR OrthoDB; 198312at2759; -.
DR PhylomeDB; Q8VYF9; -.
DR PRO; PR:Q8VYF9; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8VYF9; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR044845; HPAT/SRGT1-like.
DR PANTHER; PTHR31485; PTHR31485; 1.
PE 2: Evidence at transcript level;
KW Endoplasmic reticulum; Glycoprotein; Glycosyltransferase; Membrane;
KW Reference proteome; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..802
FT /note="Peptidyl serine alpha-galactosyltransferase"
FT /id="PRO_5007714630"
FT TOPO_DOM 20..750
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 751..771
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 772..802
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 699..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 777..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 706..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 802 AA; 91449 MW; 5E69351814493B89 CRC64;
MRWDLITAIV AALVVSVLAD ESGQMAPYRI HTLFSVECQN YFDWQTVGLM HSFLKSGQPG
PITRLLSCTD DQKKTYRGMN LAPTFEVPSW SRHPKTGDWY PAINKPVGVL YWLQHSEEAK
HVDWVVILDA DMIIRGPIIP WELGAERGRP FAAHYGYLVG CDNLLVRLHT KHPELCDKVG
GLLAMHIDDL RVLAPLWLSK TEDVRQDTAH WTTNLTGDIY GKGWISEMYG YSFGAAEAGL
KHKINDDLMI YPGYVPREGV EPVLMHYGLP FSIGNWSFTK LDHHEDNIVY DCNRLFPEPP
YPREVKIMEP DPSKRRGLIL SLECMNTLNE GLILRHAENG CPKPKWTKYL SFLKSKTFME
LTRPKLLAPG SVHILPDQHE PPPIDEFKGT YPKIHTLFST ECTTYFDWQT VGFMHSFRQS
GQPGNITRLL SCTDEALKNY KGHDLAPTHY VPSMSRHPLT GDWYPAINKP AAVVHWLHHT
NIDAEYVVIL DADMILRGPI TPWEFKAARG RPVSTPYDYL IGCDNDLARL HTRNPEACDK
VGGVIIMHIE DLRKFAMYWL LKTQEVRADK EHYGKELTGD IYESGWISEM YGYSFGAAEL
NLRHSINKEI MIYPGYVPEP GADYRVFHYG LEFKVGNWSF DKANWRNTDL INKCWAKFPD
PPSPSAVHQT DNDLRQRDLL SIECGQKLNE ALFLHHKRRN CPEPGSESTE KISVSRKVGN
IETKQTQGSD ETKESSGSSE SEGRFSTLKL WVIALWLISG VGFLVVMLLV FSTRRGRGTT
RGKGYRNKRR TSYSNTGFLD TK
