STL1_ARATH
ID STL1_ARATH Reviewed; 771 AA.
AC O22943;
DT 05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable glycosyltransferase STELLO1 {ECO:0000303|PubMed:27277162};
DE EC=2.4.-.- {ECO:0000305};
GN Name=STL1 {ECO:0000303|PubMed:27277162};
GN OrderedLocusNames=At2g41770 {ECO:0000312|Araport:AT2G41770};
GN ORFNames=T11A7.13 {ECO:0000312|EMBL:AAC02770.1};
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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=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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF 205-ASP--ASP-206; ARG-260; 296-ASP--ASP-298 AND
RP 591-ASP--ASP-592, INTERACTION WITH STL2; CESA1; CESA3; CESA4; CESA6; CESA7
RP AND CESA8, LACK OF INTERACTION WITH GOT1, AND SUBUNIT.
RX PubMed=27277162; DOI=10.1038/ncomms11656;
RA Zhang Y., Nikolovski N., Sorieul M., Vellosillo T., McFarlane H.E.,
RA Dupree R., Kesten C., Schneider R., Driemeier C., Lathe R., Lampugnani E.,
RA Yu X., Ivakov A., Doblin M.S., Mortimer J.C., Brown S.P., Persson S.,
RA Dupree P.;
RT "Golgi-localized STELLO proteins regulate the assembly and trafficking of
RT cellulose synthase complexes in Arabidopsis.";
RL Nat. Commun. 7:11656-11656(2016).
CC -!- FUNCTION: Probable glycosyltransferase regulating the assembly and
CC trafficking of cellulose synthase complexes.
CC {ECO:0000269|PubMed:27277162}.
CC -!- SUBUNIT: Homo- and heterodimer with STL2 (PubMed:27277162). Interacts
CC with CESA1, CESA3, CESA4, CESA6, CESA7 and CESA8, but not with GOT1
CC (PubMed:27277162). {ECO:0000269|PubMed:27277162}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:27277162}; Single-pass type II membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in cells that are expanding or producing
CC secondary cell walls. {ECO:0000269|PubMed:27277162}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC STL2. Stl1 and stl2 double mutants are impaired in cellulose production
CC and exhibit a stunted growth. {ECO:0000269|PubMed:27277162}.
CC -!- MISCELLANEOUS: In classical Greek, STELLO mean 'to set in order,
CC arrange, send'. {ECO:0000305|PubMed:27277162}.
CC -!- SIMILARITY: Belongs to the STELLO family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC002339; AAC02770.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10030.1; -; Genomic_DNA.
DR EMBL; AY056269; AAL07118.1; -; mRNA.
DR PIR; H84845; H84845.
DR RefSeq; NP_565960.1; NM_129741.1.
DR AlphaFoldDB; O22943; -.
DR STRING; 3702.AT2G41770.1; -.
DR PaxDb; O22943; -.
DR PRIDE; O22943; -.
DR ProteomicsDB; 228422; -.
DR EnsemblPlants; AT2G41770.1; AT2G41770.1; AT2G41770.
DR GeneID; 818776; -.
DR Gramene; AT2G41770.1; AT2G41770.1; AT2G41770.
DR KEGG; ath:AT2G41770; -.
DR Araport; AT2G41770; -.
DR TAIR; locus:2054371; AT2G41770.
DR eggNOG; ENOG502QTAG; Eukaryota.
DR HOGENOM; CLU_011678_0_0_1; -.
DR InParanoid; O22943; -.
DR OMA; HEVFYTE; -.
DR OrthoDB; 703174at2759; -.
DR PhylomeDB; O22943; -.
DR PRO; PR:O22943; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22943; baseline and differential.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
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:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0052324; P:plant-type cell wall cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:2001009; P:regulation of plant-type cell wall cellulose biosynthetic process; IMP:UniProtKB.
DR InterPro; IPR005049; STL-like.
DR PANTHER; PTHR31362; PTHR31362; 1.
DR Pfam; PF03385; STELLO; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Reference proteome; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..771
FT /note="Probable glycosyltransferase STELLO1"
FT /id="PRO_0000437204"
FT TOPO_DOM 1..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:27277162"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 72..771
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:27277162"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 729
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT MUTAGEN 205..206
FT /note="DD->AA: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27277162"
FT MUTAGEN 260
FT /note="R->A: No effect."
FT /evidence="ECO:0000269|PubMed:27277162"
FT MUTAGEN 296..298
FT /note="DVD->AVA: Loss of activity."
FT /evidence="ECO:0000269|PubMed:27277162"
FT MUTAGEN 591..592
FT /note="DD->AA: No effect."
FT /evidence="ECO:0000269|PubMed:27277162"
SQ SEQUENCE 771 AA; 88063 MW; AC827D75B1D83A1D CRC64;
MLVQDRAAPS PAKPPKSQIR ELPTHQQIRR RFSEPKNLDF STWFSENLSR IAVFSLLIVT
IVAFFFLYNT TDTASLLCFQ SQSTQFLQSL SRPQIKWNSI PVVPDKTSPY ANFQTEKWIV
VSVTKYPTEE LKSLVKIRGW QVLAIGNSAT PKDWSLKGSI FLSLDAQAEL GYRVLDHLPY
DSFVRKSVGY LFAIQHGAKK IYDADDRGEV IDGDLGKHFD VELVGLDSKQ EPILQYSHEN
PNRTVVNPYI HFGQRSVWPR GLPLENVGEI NHEEYYTEVF GGKQFIQQGI SNGLPDVDSV
FYFTRKTTLE AFDIRFDEHS PKVALPQGVM VPVNSFNTLY HSSAFWGLML PVSVSSMASD
VLRGYWGQRL LWELGGYVAV YPPTAHRFDR IEAYPFVEEK DLHVNVGRLI KFLLAWRSEK
HSFFETVLDL SFAMAEEGFW TEQDLKFTAA WLQDLIAVGY QQPRLMSLEL DRPRASIGHG
DRKEFVPRKL PSVHLGVEET GTVSTEIGNL IRWRKNFGNV VLVMFCNGPV ERTALEWRLL
YGRIFKTVVI LSSQKNSDLY VEEAKLDHIY KHLPKIFDRY SSAEGFLFVE DDTVLNYWNL
LQADKSKIWT TDKVSKSWTS VKPTGNSDWF SVQAELVKKT VSTMPAHFQV NYKDATKNNH
ETLTVCSSEV FYVPKRLVTD FIDLVDLVGD MDLHYKVAVP MFFLSMDSPQ NFDPVLGSMV
YKRKSASFNT SSSLYSAKAP AVHPWSISSE QDFIKLVQQM AEGDPLLMEL V
