CSLD2_ARATH
ID CSLD2_ARATH Reviewed; 1145 AA.
AC Q9LFL0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Cellulose synthase-like protein D2;
DE Short=AtCslD2;
DE EC=2.4.1.-;
GN Name=CSLD2; OrderedLocusNames=At5g16910; ORFNames=F2K13.60;
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 GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11027699; DOI=10.1104/pp.124.2.495;
RA Richmond T.A., Somerville C.R.;
RT "The cellulose synthase superfamily.";
RL Plant Physiol. 124:495-498(2000).
CC -!- FUNCTION: Thought to be a Golgi-localized beta-glycan synthase that
CC polymerize the backbones of noncellulosic polysaccharides
CC (hemicelluloses) of plant cell wall.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Multi-
CC pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like D subfamily. {ECO:0000305}.
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DR EMBL; AL391141; CAC01704.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92357.1; -; Genomic_DNA.
DR PIR; T51546; T51546.
DR RefSeq; NP_001318575.1; NM_001343473.1.
DR AlphaFoldDB; Q9LFL0; -.
DR SMR; Q9LFL0; -.
DR STRING; 3702.AT5G16910.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR TCDB; 4.D.3.1.9; the glycan glucosyl transferase (opgh) family.
DR iPTMnet; Q9LFL0; -.
DR PaxDb; Q9LFL0; -.
DR PRIDE; Q9LFL0; -.
DR ProteomicsDB; 222664; -.
DR EnsemblPlants; AT5G16910.1; AT5G16910.1; AT5G16910.
DR GeneID; 831554; -.
DR Gramene; AT5G16910.1; AT5G16910.1; AT5G16910.
DR KEGG; ath:AT5G16910; -.
DR Araport; AT5G16910; -.
DR TAIR; locus:2148171; AT5G16910.
DR eggNOG; ENOG502QU14; Eukaryota.
DR HOGENOM; CLU_001418_1_0_1; -.
DR InParanoid; Q9LFL0; -.
DR OMA; THAHLMD; -.
DR OrthoDB; 679241at2759; -.
DR PhylomeDB; Q9LFL0; -.
DR BioCyc; ARA:AT5G16910-MON; -.
DR PRO; PR:Q9LFL0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9LFL0; baseline and differential.
DR Genevisible; Q9LFL0; AT.
DR GO; GO:0005768; C:endosome; HDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0030173; C:integral component of Golgi membrane; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005802; C:trans-Golgi network; HDA:TAIR.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:InterPro.
DR GO; GO:0051753; F:mannan synthase activity; IDA:TAIR.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030244; P:cellulose biosynthetic process; IEA:InterPro.
DR GO; GO:0009833; P:plant-type primary cell wall biogenesis; IBA:GO_Central.
DR GO; GO:0009409; P:response to cold; IEP:TAIR.
DR GO; GO:0048767; P:root hair elongation; IMP:TAIR.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR005150; Cellulose_synth.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF03552; Cellulose_synt; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1145
FT /note="Cellulose synthase-like protein D2"
FT /id="PRO_0000319347"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 930..950
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 956..976
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1002..1022
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1046..1066
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1079..1099
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1109..1129
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 422
FT /evidence="ECO:0000255"
FT ACT_SITE 848
FT /evidence="ECO:0000255"
SQ SEQUENCE 1145 AA; 128360 MW; 21A37FD050DC26BC CRC64;
MASNKHFDKS RSNLSNNSDI QEPGRPPAGH SVKFAQRTSS GRYINYSRDD LDSELGGQDF
MSYTVHIPPT PDNQPMDPSI SQKVEEQYVA NSMFTGGFKS NTRAHLMHKV IETEPNHPQM
AGSKGSSCAI PGCDAKVMSD ERGQDLLPCE CDFKICRDCF IDAVKTGGGI CPGCKEPYKN
THLTDQVDEN GQQRPMLPGG GGSKMERRLS MVKSTNKSAL MRSQTGDFDH NRWLFETTGT
YGYGNAFWTK DGDFGSGKDG DGDGDGMGME AQDLMSRPWR PLTRKLKIPA GVISPYRLLI
FIRIVVLALF LTWRVKHQNP DAVWLWGMSV VCELWFALSW LLDQLPKLCP INRATDLQVL
KEKFETPTAS NPTGKSDLPG FDVFVSTADP EKEPPLVTAN TILSILAAEY PVEKLSCYVS
DDGGALLTFE AMAEAASFAN IWVPFCRKHA IEPRNPDSYF SLKRDPYKNK VKSDFVKDRR
RVKREFDEFK VRVNSLPDSI RRRSDAYHAR EEIKAMKMQR QNRDDEPMEP VKIPKATWMA
DGTHWPGTWL TSASDHAKGD HAGIIQVMLK PPSDEPLHGV SEGFLDLTDV DIRLPLLVYV
SREKRPGYDH NKKAGAMNAL VRASAIMSNG PFILNLDCDH YIYNSEALRE GMCFMMDRGG
DRLCYVQFPQ RFEGIDPSDR YANHNTVFFD VNMRALDGLM GPVYVGTGCL FRRIALYGFN
PPRSKDFSPS CWSCCFPRSK KKNIPEENRA LRMSDYDDEE MNLSLVPKKF GNSTFLIDSI
PVAEFQGRPL ADHPAVKNGR PPGALTIPRE LLDASTVAEA IAVISCWYED KTEWGSRIGW
IYGSVTEDVV TGYRMHNRGW KSVYCVTKRD AFRGTAPINL TDRLHQVLRW ATGSVEIFFS
RNNALLASSK MKILQRIAYL NVGIYPFTSI FLIVYCFLPA LSLFSGQFIV QTLNVTFLVY
LLIISITLCL LALLEIKWSG ISLEEWWRNE QFWLIGGTSA HLAAVLQGLL KVVAGVEISF
TLTSKSGGDD IDDEFADLYM VKWTSLMIPP ITIIMVNLIA IAVGFSRTIY SVVPQWSKLI
GGVFFSFWVL AHLYPFAKGL MGRRGRTPTI VYVWSGLVAI TISLLWVAIN PPAGNTEIGG
NFSFP
