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Protein

Probable cinnamyl alcohol dehydrogenase 9

Gene

CAD9

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in lignin biosynthesis. May catalyze the final step specific for the production of lignin monomers, like coniferyl alcohol, sinapyl alcohol and 4-coumaryl alcohol.1 Publication

Catalytic activityi

Cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH.

Cofactori

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Pathwayi: phenylpropanoid biosynthesis

This protein is involved in the pathway phenylpropanoid biosynthesis, which is part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the pathway phenylpropanoid biosynthesis and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Zinc 1; catalyticBy similarity
Binding sitei52 – 521NADPBy similarity
Metal bindingi72 – 721Zinc 1; catalyticBy similarity
Metal bindingi73 – 731Zinc 1; catalyticBy similarity
Metal bindingi103 – 1031Zinc 2By similarity
Metal bindingi106 – 1061Zinc 2By similarity
Metal bindingi109 – 1091Zinc 2By similarity
Metal bindingi117 – 1171Zinc 2By similarity
Metal bindingi166 – 1661Zinc 1; catalyticBy similarity
Binding sitei170 – 1701NADPBy similarity
Binding sitei254 – 2541NADPBy similarity
Binding sitei278 – 2781NADP; via carbonyl oxygenBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi191 – 1966NADPBy similarity
Nucleotide bindingi214 – 2196NADPBy similarity
Nucleotide bindingi301 – 3033NADPBy similarity

GO - Molecular functioni

  • cinnamyl-alcohol dehydrogenase activity Source: UniProtKB
  • sinapyl alcohol dehydrogenase activity Source: UniProtKB-EC
  • zinc ion binding Source: InterPro

GO - Biological processi

  • lignin biosynthetic process Source: UniProtKB
  • response to cytokinin Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Lignin biosynthesis

Keywords - Ligandi

Metal-binding, NADP, Zinc

Enzyme and pathway databases

BioCyciARA:AT4G39330-MONOMER.
ARA:GQT-120-MONOMER.
UniPathwayiUPA00711.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable cinnamyl alcohol dehydrogenase 9 (EC:1.1.1.195)
Short name:
AtCAD9
Gene namesi
Name:CAD9
Synonyms:CAD1
Ordered Locus Names:At4g39330
ORF Names:T22F8.230
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G39330.

Subcellular locationi

GO - Cellular componenti

  • apoplast Source: TAIR
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Probable cinnamyl alcohol dehydrogenase 9PRO_0000160810Add
BLAST

Proteomic databases

PaxDbiP42734.
PRIDEiP42734.

Expressioni

Tissue specificityi

Expressed in the vasculature of the primary root and elongation regions. Expressed in the hypocotyl, cotyledon veins, vasculature of the first rosette leaves, and hydathodes. In stems, expressed in the vascular cambium, interfascicular cambium, developing xylem, and phloem. Expressed in the entire floral organs at late developing stage, and in the abscission, style and stigmatic regions of siliques and seed funicules.2 Publications

Gene expression databases

GenevisibleiP42734. AT.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi15368. 1 interaction.
IntActiP42734. 1 interaction.
STRINGi3702.AT4G39330.1.

Structurei

3D structure databases

ProteinModelPortaliP42734.
SMRiP42734. Positions 4-358.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0023. Eukaryota.
COG1064. LUCA.
HOGENOMiHOG000294667.
InParanoidiP42734.
KOiK00083.
OMAiACKRSHE.
PhylomeDBiP42734.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P42734-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAKSPETEHP NKVFGWGARD KSGVLSPFHF SRRDNGENDV TVKILFCGVC
60 70 80 90 100
HTDLHTIKND WGYSYYPVVP GHEIVGIATK VGKNVTKFKE GDRVGVGVIS
110 120 130 140 150
GSCQSCESCD QDLENYCPQM SFTYNAIGSD GTKNYGGYSE NIVVDQRFVL
160 170 180 190 200
RFPENLPSDS GAPLLCAGIT VYSPMKYYGM TEAGKHLGVA GLGGLGHVAV
210 220 230 240 250
KIGKAFGLKV TVISSSSTKA EEAINHLGAD SFLVTTDPQK MKAAIGTMDY
260 270 280 290 300
IIDTISAVHA LYPLLGLLKV NGKLIALGLP EKPLELPMFP LVLGRKMVGG
310 320 330 340 350
SDVGGMKETQ EMLDFCAKHN ITADIELIKM DEINTAMERL AKSDVRYRFV
360
IDVANSLSPP
Length:360
Mass (Da):38,934
Last modified:May 29, 2007 - v2
Checksum:i0E4F3B0581785759
GO
Isoform 2 (identifier: P42734-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     302-311: DVGGMKETQE → LLSLMLGTGS
     312-360: Missing.

Note: No experimental confirmation available.
Show »
Length:311
Mass (Da):33,253
Checksum:i539EE3E5D40C94CE
GO

Sequence cautioni

The sequence BAH56862.1 differs from that shown. Reason: Frameshift at position 300. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti202 – 2021I → S in AAA99511 (PubMed:7630954).Curated
Sequence conflicti352 – 3521D → N in AAM64913 (PubMed:19423640).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei302 – 31110DVGGMKETQE → LLSLMLGTGS in isoform 2. 1 PublicationVSP_037894
Alternative sequencei312 – 36049Missing in isoform 2. 1 PublicationVSP_037895Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37883 Genomic DNA. Translation: AAA99511.1.
L37884 mRNA. Translation: AAA74746.1.
AY302076 mRNA. Translation: AAP59429.1.
AL050351 Genomic DNA. Translation: CAB43648.1.
AL161595 Genomic DNA. Translation: CAB80596.1.
CP002687 Genomic DNA. Translation: AEE87056.1.
CP002687 Genomic DNA. Translation: AEE87057.1.
AF370498 mRNA. Translation: AAK43875.1.
AY064669 mRNA. Translation: AAL47376.1.
AK317632 mRNA. Translation: BAH20294.1.
AK318747 mRNA. Translation: BAH56862.1. Frameshift.
AY087363 mRNA. Translation: AAM64913.1.
PIRiS71179.
T08581.
RefSeqiNP_001031812.1. NM_001036735.1. [P42734-2]
NP_195643.1. NM_120093.4. [P42734-1]
UniGeneiAt.24772.
At.67820.
At.75608.

Genome annotation databases

EnsemblPlantsiAT4G39330.1; AT4G39330.1; AT4G39330. [P42734-1]
GeneIDi830088.
KEGGiath:AT4G39330.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37883 Genomic DNA. Translation: AAA99511.1.
L37884 mRNA. Translation: AAA74746.1.
AY302076 mRNA. Translation: AAP59429.1.
AL050351 Genomic DNA. Translation: CAB43648.1.
AL161595 Genomic DNA. Translation: CAB80596.1.
CP002687 Genomic DNA. Translation: AEE87056.1.
CP002687 Genomic DNA. Translation: AEE87057.1.
AF370498 mRNA. Translation: AAK43875.1.
AY064669 mRNA. Translation: AAL47376.1.
AK317632 mRNA. Translation: BAH20294.1.
AK318747 mRNA. Translation: BAH56862.1. Frameshift.
AY087363 mRNA. Translation: AAM64913.1.
PIRiS71179.
T08581.
RefSeqiNP_001031812.1. NM_001036735.1. [P42734-2]
NP_195643.1. NM_120093.4. [P42734-1]
UniGeneiAt.24772.
At.67820.
At.75608.

3D structure databases

ProteinModelPortaliP42734.
SMRiP42734. Positions 4-358.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi15368. 1 interaction.
IntActiP42734. 1 interaction.
STRINGi3702.AT4G39330.1.

Proteomic databases

PaxDbiP42734.
PRIDEiP42734.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G39330.1; AT4G39330.1; AT4G39330. [P42734-1]
GeneIDi830088.
KEGGiath:AT4G39330.

Organism-specific databases

TAIRiAT4G39330.

Phylogenomic databases

eggNOGiKOG0023. Eukaryota.
COG1064. LUCA.
HOGENOMiHOG000294667.
InParanoidiP42734.
KOiK00083.
OMAiACKRSHE.
PhylomeDBiP42734.

Enzyme and pathway databases

UniPathwayiUPA00711.
BioCyciARA:AT4G39330-MONOMER.
ARA:GQT-120-MONOMER.

Miscellaneous databases

PROiP42734.

Gene expression databases

GenevisibleiP42734. AT.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProiIPR013149. ADH_C.
IPR013154. ADH_N.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
IPR020843. PKS_ER.
[Graphical view]
PANTHERiPTHR11695. PTHR11695. 1 hit.
PfamiPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SMARTiSM00829. PKS_ER. 1 hit.
[Graphical view]
SUPFAMiSSF50129. SSF50129. 1 hit.
SSF51735. SSF51735. 1 hit.
PROSITEiPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A gene encoding a cinnamyl alcohol dehydrogenase homolog in Arabidopsis thaliana."
    Somers D.A., Nourse J.P., Manners J.M., Abrahams S.L., Watson J.M.
    Plant Physiol. 108:1309-1310(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  2. "Functional reclassification of the putative cinnamyl alcohol dehydrogenase multigene family in Arabidopsis."
    Kim S.-J., Kim M.-R., Bedgar D.L., Moinuddin S.G.A., Cardenas C.L., Davin L.B., Kang C., Lewis N.G.
    Proc. Natl. Acad. Sci. U.S.A. 101:1455-1460(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], GENE FAMILY, NOMENCLATURE.
  3. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  6. "Analysis of multiple occurrences of alternative splicing events in Arabidopsis thaliana using novel sequenced full-length cDNAs."
    Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M., Shinozaki K.
    DNA Res. 16:155-164(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: cv. Columbia.
  7. "Full-length cDNA from Arabidopsis thaliana."
    Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  8. "Evidence for a role of AtCAD 1 in lignification of elongating stems of Arabidopsis thaliana."
    Eudes A., Pollet B., Sibout R., Do C.-T., Seguin A., Lapierre C., Jouanin L.
    Planta 225:23-39(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  9. "Expression of cinnamyl alcohol dehydrogenases and their putative homologues during Arabidopsis thaliana growth and development: lessons for database annotations?"
    Kim S.-J., Kim K.-W., Cho M.-H., Franceschi V.R., Davin L.B., Lewis N.G.
    Phytochemistry 68:1957-1974(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiCADH9_ARATH
AccessioniPrimary (citable) accession number: P42734
Secondary accession number(s): B9DHS7
, C0Z2D3, Q8LB84, Q94K02
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 29, 2007
Last modified: May 11, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.