P42734 (CADH9_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable cinnamyl alcohol dehydrogenase 9
Short name=AtCAD9
EC=1.1.1.195

Gene names

Name:	CAD9
Synonyms:	CAD1
Ordered Locus Names:	At4g39330
ORF Names:	T22F8.230

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	360 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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. Ref.8
Catalytic activity	Cinnamyl alcohol + NADP+ = cinnamaldehyde + NADPH.
Cofactor	Binds 2 zinc ions per subunit By similarity.
Pathway	Aromatic compound metabolism; phenylpropanoid biosynthesis.
Subunit structure	Homodimer By similarity.
Tissue specificity	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. Ref.8 Ref.9
Sequence similarities	Belongs to the zinc-containing alcohol dehydrogenase family.
Sequence caution	The sequence BAH56862.1 differs from that shown. Reason: Frameshift at position 300.

Ontologies

Keywords
Biological process	Lignin biosynthesis
Coding sequence diversity	Alternative splicing
Ligand	Metal-binding NADP Zinc
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	lignin biosynthetic process Inferred from mutant phenotype Ref.8. Source: UniProtKB
Cellular component	apoplast Inferred from direct assay. Source: TAIR
Molecular function	cinnamyl-alcohol dehydrogenase activity Inferred from mutant phenotype Ref.8. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro sinapyl alcohol dehydrogenase activity Inferred from electronic annotation. Source: EC zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P42734-1)

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.

Isoform 2 (identifier: P42734-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 360	360	Probable cinnamyl alcohol dehydrogenase 9		PRO_0000160810
Regions
	Nucleotide binding	191 – 196	6	NADP By similarity
	Nucleotide binding	214 – 219	6	NADP By similarity
	Nucleotide binding	301 – 303	3	NADP By similarity
Sites
	Metal binding	50	1	Zinc 1; catalytic By similarity
	Metal binding	72	1	Zinc 1; catalytic By similarity
	Metal binding	73	1	Zinc 1; catalytic By similarity
	Metal binding	103	1	Zinc 2 By similarity
	Metal binding	106	1	Zinc 2 By similarity
	Metal binding	109	1	Zinc 2 By similarity
	Metal binding	117	1	Zinc 2 By similarity
	Metal binding	166	1	Zinc 1; catalytic By similarity
	Binding site	52	1	NADP By similarity
	Binding site	170	1	NADP By similarity
	Binding site	254	1	NADP By similarity
	Binding site	278	1	NADP; via carbonyl oxygen By similarity
Natural variations
	Alternative sequence	302 – 311	10	DVGGMKETQE → LLSLMLGTGS in isoform 2.		VSP_037894
	Alternative sequence	312 – 360	49	Missing in isoform 2.		VSP_037895
Experimental info
	Sequence conflict	202	1	I → S in AAA99511. Ref.1
	Sequence conflict	352	1	D → N in AAM64913. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: 0E4F3B0581785759	FASTA	360	38,934
	10 20 30 40 50 60 MAKSPETEHP NKVFGWGARD KSGVLSPFHF SRRDNGENDV TVKILFCGVC HTDLHTIKND 70 80 90 100 110 120 WGYSYYPVVP GHEIVGIATK VGKNVTKFKE GDRVGVGVIS GSCQSCESCD QDLENYCPQM 130 140 150 160 170 180 SFTYNAIGSD GTKNYGGYSE NIVVDQRFVL RFPENLPSDS GAPLLCAGIT VYSPMKYYGM 190 200 210 220 230 240 TEAGKHLGVA GLGGLGHVAV KIGKAFGLKV TVISSSSTKA EEAINHLGAD SFLVTTDPQK 250 260 270 280 290 300 MKAAIGTMDY IIDTISAVHA LYPLLGLLKV NGKLIALGLP EKPLELPMFP LVLGRKMVGG 310 320 330 340 350 360 SDVGGMKETQ EMLDFCAKHN ITADIELIKM DEINTAMERL AKSDVRYRFV IDVANSLSPP
	Isoform 2 [UniParc]. Checksum: 539EE3E5D40C94CE	FASTA	311	33,253
	10 20 30 40 50 60 MAKSPETEHP NKVFGWGARD KSGVLSPFHF SRRDNGENDV TVKILFCGVC HTDLHTIKND 70 80 90 100 110 120 WGYSYYPVVP GHEIVGIATK VGKNVTKFKE GDRVGVGVIS GSCQSCESCD QDLENYCPQM 130 140 150 160 170 180 SFTYNAIGSD GTKNYGGYSE NIVVDQRFVL RFPENLPSDS GAPLLCAGIT VYSPMKYYGM 190 200 210 220 230 240 TEAGKHLGVA GLGGLGHVAV KIGKAFGLKV TVISSSSTKA EEAINHLGAD SFLVTTDPQK 250 260 270 280 290 300 MKAAIGTMDY IIDTISAVHA LYPLLGLLKV NGKLIALGLP EKPLELPMFP LVLGRKMVGG 310 SLLSLMLGTG S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 7630954] [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: 14745009] [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: 10617198] [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: 14593172] [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: 19423640] [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: 16832689] [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: 17467016] [Abstract] Cited for: TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00538689. IPI00540521.
PIR	S71179. T08581.
RefSeq	NP_001031812.1. NM_001036735.1. NP_195643.1. NM_120093.4.
UniGene	At.24772. At.67820.
3D structure databases
ProteinModelPortal	P42734.
SMR	P42734. Positions 4-358.
ModBase	Search...
Protein-protein interaction databases
IntAct	P42734. 1 interaction.
STRING	P42734.
Proteomic databases
PRIDE	P42734.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G39330.1; AT4G39330.1; AT4G39330.
GeneID	830088.
GenomeReviews	Gene locus AT4G39330 in contig CT486007_GR.
KEGG	ath:AT4G39330.
NMPDR	fig|3702.1.peg.22068.
Organism-specific databases
TAIR	At4g39330.
Phylogenomic databases
eggNOG	KOG0023.
HOGENOM	HBG753318.
InParanoid	P42734.
OMA	KSPETEH.
PhylomeDB	P42734.
ProtClustDB	PLN02586.
Gene expression databases
Genevestigator	P42734.
Family and domain databases
InterPro	IPR013149. ADH_C. IPR013154. ADH_GroES-like. IPR002085. ADH_SF_Zn-type. IPR002328. ADH_Zn_CS. IPR011032. GroES-like. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHER	PTHR11695. ADH_Sf_Zn. 1 hit.
Pfam	PF08240. ADH_N. 1 hit. PF00107. ADH_zinc_N. 1 hit. [Graphical view]
SUPFAM	SSF50129. GroES_like. 1 hit.
PROSITE	PS00059. ADH_ZINC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CADH9_ARATH

Accession

Primary (citable) accession number: P42734
Secondary accession number(s): B9DHS7 , C0Z2D3, Q8LB84, Q94K02

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	May 29, 2007
Last modified:	December 14, 2011
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program