CSLD5_ARATH
ID CSLD5_ARATH Reviewed; 1181 AA.
AC Q9SRW9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Cellulose synthase-like protein D5;
DE Short=AtCslD5;
DE EC=2.4.1.-;
GN Name=CSLD5; OrderedLocusNames=At1g02730; ORFNames=F22D16.26;
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=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 [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;
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 [4]
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).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=17892446; DOI=10.1111/j.1365-313x.2007.03281.x;
RA Bernal A.J., Jensen J.K., Harholt J., Soerensen S., Moller I., Blaukopf C.,
RA Johansen B., de Lotto R., Pauly M., Scheller H.V., Willats W.G.T.;
RT "Disruption of ATCSLD5 results in reduced growth, reduced xylan and
RT homogalacturonan synthase activity and altered xylan occurrence in
RT Arabidopsis.";
RL Plant J. 52:791-802(2007).
CC -!- FUNCTION: Involved in stem and root growth. Possesses xylan and
CC homogalacturonan synthase activity. {ECO:0000269|PubMed:17892446}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000305|PubMed:17892446}; Multi-pass membrane protein
CC {ECO:0000305|PubMed:17892446}.
CC -!- TISSUE SPECIFICITY: Expressed in vascular tissues.
CC {ECO:0000269|PubMed:17892446}.
CC -!- DEVELOPMENTAL STAGE: Expressed at its highest level between 21 and 25
CC days, during the inflorescence stem elongation phase.
CC {ECO:0000269|PubMed:17892446}.
CC -!- DISRUPTION PHENOTYPE: Significant reduction of root and stem growth,
CC xylan reduction in stem and increased susceptibility to the cellulose
CC synthase inhibitor isoxaben. {ECO:0000269|PubMed:17892446}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC cellulose synthase-like D subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AK226870; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC009525; AAF02892.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27464.1; -; Genomic_DNA.
DR EMBL; AK226870; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; D86157; D86157.
DR RefSeq; NP_171773.1; NM_100153.4.
DR AlphaFoldDB; Q9SRW9; -.
DR SMR; Q9SRW9; -.
DR STRING; 3702.AT1G02730.1; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR iPTMnet; Q9SRW9; -.
DR PaxDb; Q9SRW9; -.
DR PRIDE; Q9SRW9; -.
DR ProteomicsDB; 224514; -.
DR EnsemblPlants; AT1G02730.1; AT1G02730.1; AT1G02730.
DR GeneID; 839467; -.
DR Gramene; AT1G02730.1; AT1G02730.1; AT1G02730.
DR KEGG; ath:AT1G02730; -.
DR Araport; AT1G02730; -.
DR TAIR; locus:2024745; AT1G02730.
DR eggNOG; ENOG502QQG2; Eukaryota.
DR HOGENOM; CLU_001418_1_0_1; -.
DR InParanoid; Q9SRW9; -.
DR OMA; ATEHRGW; -.
DR OrthoDB; 679241at2759; -.
DR PhylomeDB; Q9SRW9; -.
DR BioCyc; ARA:AT1G02730-MON; -.
DR BRENDA; 2.4.2.24; 399.
DR PRO; PR:Q9SRW9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9SRW9; baseline and differential.
DR Genevisible; Q9SRW9; AT.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
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:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016760; F:cellulose synthase (UDP-forming) activity; IEA:InterPro.
DR GO; GO:0046527; F:glucosyltransferase activity; NAS:TAIR.
DR GO; GO:0051753; F:mannan synthase activity; IDA:TAIR.
DR GO; GO:0000919; P:cell plate assembly; IMP:TAIR.
DR GO; GO:0042546; P:cell wall biogenesis; NAS: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:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0009651; P:response to salt stress; IMP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
DR GO; GO:0048367; P:shoot system development; 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 2: Evidence at transcript level;
KW Cell wall biogenesis/degradation; Coiled coil; Glycosyltransferase;
KW Golgi apparatus; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..1181
FT /note="Cellulose synthase-like protein D5"
FT /id="PRO_0000319350"
FT TRANSMEM 312..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 966..986
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 991..1011
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1038..1058
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1082..1102
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1116..1136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1146..1166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 497..542
FT /evidence="ECO:0000255"
FT COMPBIAS 1..21
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 443
FT /evidence="ECO:0000255"
FT ACT_SITE 884
FT /evidence="ECO:0000255"
FT CONFLICT 1046
FT /note="L -> P (in Ref. 3; AK226870)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1181 AA; 132587 MW; B7D0C72FF5D20A5D CRC64;
MVKSAASQSP SPVTITVTPC KGSGDRSLGL TSPIPRASVI TNQNSPLSSR ATRRTSISSG
NRRSNGDEGR YCSMSVEDLT AETTNSECVL SYTVHIPPTP DHQTVFASQE SEEDEMLKGN
SNQKSFLSGT IFTGGFKSVT RGHVIDCSMD RADPEKKSGQ ICWLKGCDEK VVHGRCECGF
RICRDCYFDC ITSGGGNCPG CKEPYRDIND DPETEEEDEE DEAKPLPQMG ESKLDKRLSV
VKSFKAQNQA GDFDHTRWLF ETKGTYGYGN AVWPKDGYGI GSGGGGNGYE TPPEFGERSK
RPLTRKVSVS AAIISPYRLL IALRLVALGL FLTWRVRHPN REAMWLWGMS TTCELWFALS
WLLDQLPKLC PVNRLTDLGV LKERFESPNL RNPKGRSDLP GIDVFVSTAD PEKEPPLVTA
NTILSILAVD YPVEKLACYL SDDGGALLTF EALAQTASFA STWVPFCRKH NIEPRNPEAY
FGQKRNFLKN KVRLDFVRER RRVKREYDEF KVRINSLPEA IRRRSDAYNV HEELRAKKKQ
MEMMMGNNPQ ETVIVPKATW MSDGSHWPGT WSSGETDNSR GDHAGIIQAM LAPPNAEPVY
GAEADAENLI DTTDVDIRLP MLVYVSREKR PGYDHNKKAG AMNALVRTSA IMSNGPFILN
LDCDHYIYNS MALREGMCFM LDRGGDRICY VQFPQRFEGI DPNDRYANHN TVFFDVSMRA
LDGLQGPMYV GTGCIFRRTA LYGFSPPRAT EHHGWLGRRK VKISLRRPKA MMKKDDEVSL
PINGEYNEEE NDDGDIESLL LPKRFGNSNS FVASIPVAEY QGRLIQDLQG KGKNSRPAGS
LAVPREPLDA ATVAEAISVI SCFYEDKTEW GKRVGWIYGS VTEDVVTGYR MHNRGWRSIY
CVTKRDAFRG TAPINLTDRL HQVLRWATGS VEIFFSRNNA IFATRRMKFL QRVAYFNVGM
YPFTSLFLIV YCILPAISLF SGQFIVQSLD ITFLIYLLSI TLTLCMLSLL EIKWSGITLH
EWWRNEQFWV IGGTSAHPAA VLQGLLKVIA GVDISFTLTS KSSAPEDGDD EFADLYVVKW
SFLMVPPLTI MMVNMIAIAV GLARTLYSPF PQWSKLVGGV FFSFWVLCHL YPFAKGLMGR
RGRVPTIVFV WSGLLSIIVS LLWVYINPPS GKQDYMQFQF P
