ID   STL2_ARATH              Reviewed;         765 AA.
AC   Q9SCN0;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Probable glycosyltransferase STELLO2 {ECO:0000303|PubMed:27277162};
DE            EC=2.4.-.- {ECO:0000305};
GN   Name=STL2 {ECO:0000303|PubMed:27277162};
GN   OrderedLocusNames=At3g57420 {ECO:0000312|Araport:AT3G57420};
GN   ORFNames=T8H10.20 {ECO:0000312|EMBL:CAB66099.1};
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=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   [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].
RA   Shinn P., Chen H., Cheuk R., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, INTERACTION WITH
RP   STL2; CESA1; CESA3; CESA4; CESA6; CESA7 AND CESA8, LACK OF INTERACTION WITH
RP   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 STL1 (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:0000305|PubMed:27277162}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype, due to the redundancy with
CC       STL1. 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}.
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DR   EMBL; AL133248; CAB66099.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE79653.1; -; Genomic_DNA.
DR   EMBL; BT015820; AAU94383.1; -; mRNA.
DR   EMBL; BT021114; AAX12884.1; -; mRNA.
DR   EMBL; AK229605; BAF01451.1; -; mRNA.
DR   PIR; T46178; T46178.
DR   RefSeq; NP_191301.1; NM_115602.4.
DR   AlphaFoldDB; Q9SCN0; -.
DR   STRING; 3702.AT3G57420.1; -.
DR   PaxDb; Q9SCN0; -.
DR   PRIDE; Q9SCN0; -.
DR   ProteomicsDB; 228265; -.
DR   EnsemblPlants; AT3G57420.1; AT3G57420.1; AT3G57420.
DR   GeneID; 824909; -.
DR   Gramene; AT3G57420.1; AT3G57420.1; AT3G57420.
DR   KEGG; ath:AT3G57420; -.
DR   Araport; AT3G57420; -.
DR   TAIR; locus:2103473; AT3G57420.
DR   eggNOG; ENOG502QTAG; Eukaryota.
DR   HOGENOM; CLU_011678_0_0_1; -.
DR   InParanoid; Q9SCN0; -.
DR   OMA; DKVTESW; -.
DR   OrthoDB; 703174at2759; -.
DR   PhylomeDB; Q9SCN0; -.
DR   PRO; PR:Q9SCN0; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9SCN0; baseline and differential.
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: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..765
FT                   /note="Probable glycosyltransferase STELLO2"
FT                   /id="PRO_0000437205"
FT   TOPO_DOM        1..43
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000269|PubMed:27277162"
FT   TRANSMEM        44..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        65..765
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:27277162"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        723
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   765 AA;  87660 MW;  420870946C923BC5 CRC64;
     MLVQDRVAPK PPKSRIRELP SRDRFAEPKI LDFSSWVSDN VYRIVIIFLF IVTVAAFFFL
     YNTTDTASLL CFQSQSTQSL QSLTRPQINW NSIQIVSDKT SPYASFRTEK WIVVSVTKHP
     TEELKGLVKI KGWQVLAIGN SLTPKDWNLK GAIFLSLDAQ AELNYRILDH LPYDSFVRKS
     VGYLFAIQHG AKKIFDADDR GEVIDGDLGK HFDVELVGED ARQEPILQYS HENPNRTVVN
     PYIHFGQRSV WPRGLPLENV GEINHEEYYT EVFGGKQFIQ QGISNGLPDV DSVYYSTRKT
     TFEPFDIRFD EHSPKVALPQ GMMVPVNSFN TLYHSSAFWG LMLPVSVSSM ASDVIRGYWG
     QRLLWELGGY VAVYPPTVHR YDRVEAYPFS DEKDLHINVG RLIKFLLAWR SNKHRFFETI
     LDLSFVMAEQ GFWTELDVKF TAAWLQDLLM VGYQQPRLMS LELDRPRATI GHGDRKEFVP
     RKLPSVHLGV EEIGTVSSEI GNLIKWRKNF GNVVLIMFCN GPVERTALEW RLLYGRIFKT
     VVILSSRKNS DLYVQEAKLD HIYKRLPKIF DRYSSADGFV FVEDDTVLNY WNLLQADKTK
     LWTTDKVTES WTTVRPAGNS DWYSVQAELV KKIVSTMPVH FQVNYKEATK NSDGTSLTMC
     SSEVFYVPKR FVSDFTDLVN LVGDMDLHYK VAVPMFFLSM DSPQNFDPVL GSMVYKSEPA
     SLNSSLSLYS AEAPAVHPWS ISNEQDFIKL VREMAEGDPL LMELV