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CSLD3_ARATH
ID   CSLD3_ARATH             Reviewed;        1145 AA.
AC   Q9M9M4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Cellulose synthase-like protein D3;
DE            Short=AtCslD3;
DE            EC=2.4.1.-;
DE   AltName: Full=Protein KOJAK;
GN   Name=CSLD3; Synonyms=KJK; OrderedLocusNames=At3g03050; ORFNames=T17B22.26;
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 [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MUTAGENESIS OF GLU-829.
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=11156607; DOI=10.1101/gad.188801;
RA   Favery B., Ryan E., Foreman J., Linstead P., Boudonck K., Steer M.,
RA   Shaw P., Dolan L.;
RT   "KOJAK encodes a cellulose synthase-like protein required for root hair
RT   cell morphogenesis in Arabidopsis.";
RL   Genes Dev. 15:79-89(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia;
RX   PubMed=11402188; DOI=10.1104/pp.126.2.575;
RA   Wang X., Cnops G., Vanderhaeghen R., de Block S., van Montagu M.,
RA   van Lijsebettens M.;
RT   "AtCSLD3, a cellulose synthase-like gene important for root hair growth in
RT   arabidopsis.";
RL   Plant Physiol. 126:575-586(2001).
RN   [3]
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   [4]
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   [5]
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   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. La-0;
RX   PubMed=14506206; DOI=10.1074/mcp.t300006-mcp200;
RA   Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT   "Large-scale analysis of in vivo phosphorylated membrane proteins by
RT   immobilized metal ion affinity chromatography and mass spectrometry.";
RL   Mol. Cell. Proteomics 2:1234-1243(2003).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15308754; DOI=10.1105/tpc.104.023150;
RA   Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.;
RT   "Phosphoproteomics of the Arabidopsis plasma membrane and a new
RT   phosphorylation site database.";
RL   Plant Cell 16:2394-2405(2004).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-755, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=cv. Columbia;
RX   PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA   Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA   Rathjen J.P., Peck S.C.;
RT   "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT   thaliana.";
RL   J. Proteomics 72:439-451(2009).
RN   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19376835; DOI=10.1104/pp.109.138677;
RA   Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA   Grossmann J., Gruissem W., Baginsky S.;
RT   "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT   chloroplast kinase substrates and phosphorylation networks.";
RL   Plant Physiol. 150:889-903(2009).
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. Required for synthesis of a cell
CC       wall polysaccharide essential for root hair elongation, but not
CC       initiation. May be the functional ortholog of rice CSLD1.
CC       {ECO:0000269|PubMed:11402188}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC       {ECO:0000305|PubMed:11156607}; Multi-pass membrane protein
CC       {ECO:0000305|PubMed:11156607}.
CC   -!- TISSUE SPECIFICITY: Preferentially expressed in root hair cells.
CC       Expressed in roots, leaves, stems, flowers and siliques.
CC       {ECO:0000269|PubMed:11156607, ECO:0000269|PubMed:11402188}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. Plant
CC       cellulose synthase-like D subfamily. {ECO:0000305}.
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DR   EMBL; AF232907; AAG60543.1; -; mRNA.
DR   EMBL; AJ297948; CAC82909.1; -; Genomic_DNA.
DR   EMBL; AC012328; AAF26119.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE73896.1; -; Genomic_DNA.
DR   EMBL; AF360180; AAK25890.1; -; mRNA.
DR   EMBL; AY039996; AAK64073.1; -; mRNA.
DR   RefSeq; NP_186955.1; NM_111175.3.
DR   AlphaFoldDB; Q9M9M4; -.
DR   SMR; Q9M9M4; -.
DR   BioGRID; 6481; 2.
DR   IntAct; Q9M9M4; 2.
DR   STRING; 3702.AT3G03050.1; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   iPTMnet; Q9M9M4; -.
DR   PaxDb; Q9M9M4; -.
DR   PRIDE; Q9M9M4; -.
DR   ProteomicsDB; 220366; -.
DR   EnsemblPlants; AT3G03050.1; AT3G03050.1; AT3G03050.
DR   GeneID; 821148; -.
DR   Gramene; AT3G03050.1; AT3G03050.1; AT3G03050.
DR   KEGG; ath:AT3G03050; -.
DR   Araport; AT3G03050; -.
DR   TAIR; locus:2097700; AT3G03050.
DR   eggNOG; ENOG502QU14; Eukaryota.
DR   HOGENOM; CLU_001418_0_2_1; -.
DR   InParanoid; Q9M9M4; -.
DR   OMA; MWRIKHK; -.
DR   OrthoDB; 679241at2759; -.
DR   PhylomeDB; Q9M9M4; -.
DR   BioCyc; ARA:AT3G03050-MON; -.
DR   BRENDA; 2.4.1.12; 399.
DR   PRO; PR:Q9M9M4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9M9M4; baseline and differential.
DR   Genevisible; Q9M9M4; AT.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR   GO; GO:0005768; C:endosome; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA: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; HDA:TAIR.
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   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.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Glycosyltransferase; Golgi apparatus;
KW   Membrane; Phosphoprotein; Reference proteome; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..1145
FT                   /note="Cellulose synthase-like protein D3"
FT                   /id="PRO_0000319348"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
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        1045..1065
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..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        419
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        848
FT                   /evidence="ECO:0000255"
FT   MOD_RES         755
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:14506206,
FT                   ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:19245862"
FT   MUTAGEN         829
FT                   /note="E->K: In kjk-3; reduction of root hair growth."
FT                   /evidence="ECO:0000269|PubMed:11156607"
SQ   SEQUENCE   1145 AA;  128589 MW;  F5763EF66124E33D CRC64;
     MASNNHFMNS RSNLSTNSDA AEAERHQQPV SNSVTFARRT PSGRYVNYSR DDLDSELGSV
     DLTGYSVHIP PTPDNQPMDP SISQKVEEQY VSNSLFTGGF NSVTRAHLME KVIDTETSHP
     QMAGAKGSSC AVPGCDVKVM SDERGQDLLP CECDFKICRD CFMDAVKTGG MCPGCKEPYR
     NTDLADFADN NKQQRPMLPP PAGGSKMDRR LSLMKSTKSG LMRSQTGDFD HNRWLFETSG
     TYGFGNAFWT KDGNFGSDKD GNGHGMGPQD LMSRPWRPLT RKLQIPAAVI SPYRLLILIR
     IVVLALFLMW RIKHKNPDAI WLWGMSVVCE LWFALSWLLD QLPKLCPINR ATDLNVLKEK
     FETPTPSNPT GKSDLPGLDM FVSTADPEKE PPLVTSNTIL SILAADYPVE KLACYVSDDG
     GALLTFEAMA EAASFANMWV PFCRKHNIEP RNPDSYFSLK RDPYKNKVKA DFVKDRRRVK
     REYDEFKVRI NSLPDSIRRR SDAYHAREEI KAMKLQRQNR DEEIVEPVKI PKATWMADGT
     HWPGTWINSG PDHSRSDHAG IIQVMLKPPS DEPLHGVSEG FLDLTDVDIR LPLLVYVSRE
     KRPGYDHNKK AGAMNALVRA SAIMSNGPFI LNLDCDHYIY NSQALREGMC FMMDRGGDRL
     CYVQFPQRFE GIDPSDRYAN HNTVFFDVNM RALDGLMGPV YVGTGCLFRR IALYGFDPPR
     AKEHHPGFCS CCFSRKKKKS RVPEENRSLR MGGDSDDDEE MNLSLVPKKF GNSTFLIDSI
     PVAEFQGRPL ADHPAVQNGR PPGALTIPRE LLDASTVAEA IAVISCWYED KTEWGSRIGW
     IYGSVTEDVV TGYRMHNRGW KSVYCVTKRD AFRGTAPINL TDRLHQVLRW ATGSVEIFFS
     RNNAFFASPR MKILQRIAYL NVGIYPFTSF FLIVYCFLPA LSLFSGQFIV QTLNVTFLVY
     LLIISITLCL LALLEIKWSG ISLEEWWRNE QFWLIGGTSA HLAAVIQGLL KVVAGIEISF
     TLTSKSGGED VDDEFADLYI VKWTSLMIPP ITIMMVNLIA IAVGFSRTIY SVIPQWSKLI
     GGVFFSFWVL AHLYPFAKGL MGRRGRTPTI VYVWSGLVAI TISLLWVAIN PPAGSTQIGG
     SFTFP
 
 
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