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Reviewed, UniProtKB/Swiss-Prot P27450 (CX32_ARATH)

Last modified June 16, 2009. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable serine/threonine-protein kinase Cx32, chloroplastic
    EC=2.7.11.1
Gene names
Ordered Locus Names: At4g35600
ORF Names: F8D20.110
OrganismArabidopsis thaliana (Mouse-ear cress) [Complete proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidseurosids IIBrassicalesBrassicaceaeArabidopsis

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + a protein = ADP + a phosphoprotein.

Subcellular location

Plastidchloroplast Potential.

Sequence similarities

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.

Contains 1 protein kinase domain.

Caution

Was originally (Ref.1) reported to be a connexin and to contain transmembrane domains. Ref.4 authors have assigned that this is not a connexin, but rather a protein kinase.

Sequence caution

The sequence AAA32850.1 differs from that shown. Reason: Frameshift at several positions.

The sequence AAA32850.1 differs from that shown. Reason: Miscellaneous discrepancy. Sequencing errors.

The sequence CAA20030.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB80276.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4242Chloroplast Potential
Chain43 – 419377Probable serine/threonine-protein kinase Cx32, chloroplastic
PRO_0000024321

Regions

Domain86 – 368283Protein kinase
Nucleotide binding92 – 1009ATP By similarity
Compositional bias9 – 146Poly-Ser

Sites

Active site2181Proton acceptor By similarity
Binding site1241ATP By similarity

Amino acid modifications

Modified residue1171Phosphoserine Ref.5 Ref.6

Sequences

Sequence LengthMass (Da)Tools
P27450-1 [UniParc].

Last modified June 21, 2004. Version 2.
Checksum: 7C85AB6C38925145

FASTA41946,340
        10         20         30         40         50         60 
MGACISFFSS SSPSKTGLHS HATTNNHSNG TEFSSTTGAT TNSSVGQQSQ FSDISTGIIS 

        70         80         90        100        110        120 
DSGKLLESPN LKVYNFLDLK TATKNFKPDS MLGQGGFGKV YRGWVDATTL APSRVGSGMI 

       130        140        150        160        170        180 
VAIKRLNSES VQGFAEWRSE VNFLGMLSHR NLVKLLGYCR EDKELLLVYE FMPKGSLESH 

       190        200        210        220        230        240 
LFRRNDPFPW DLRIKIVIGA ARGLAFLHSL QREVIYRDFK ASNILLDSNY DAKLSDFGLA 

       250        260        270        280        290        300 
KLGPADEKSH VTTRIMGTYG YAAPEYMATG HLYVKSDVFA FGVVLLEIMT GLTAHNTKRP 

       310        320        330        340        350        360 
RGQESLVDWL RPELSNKHRV KQIMDKGIKG QYTTKVATEM ARITLSCIEP DPKNRPHMKE 

       370        380        390        400        410 
VVEVLEHIQG LNVVPNRSST KQAVANSSRS SPHHYRYKAG ALGAERKRAT PGRFGSVEK 

« Hide

References

« Hide 'large scale' references
[1]"Gap junction protein homologue from Arabidopsis thaliana: evidence for connexins in plants."
Meiners S., Xu A., Schindler M.
Proc. Natl. Acad. Sci. U.S.A. 88:4119-4122(1991) [PubMed: 1851993] [Abstract]
Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
[2]"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. expand/collapse author list , 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.
[3]"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. expand/collapse author list , 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].
Strain: cv. Columbia.
[4]"The proposed plant connexin is a protein kinase-like protein."
Mushegian A.R., Koonin E.V.
Plant Cell 5:998-999(1993) [PubMed: 8400879] [Abstract]
Cited for: DISCUSSION OF SEQUENCE.
[5]"Phosphoproteomics of the Arabidopsis plasma membrane and a new phosphorylation site database."
Nuehse T.S., Stensballe A., Jensen O.N., Peck S.C.
Plant Cell 16:2394-2405(2004) [PubMed: 15308754] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, MASS SPECTROMETRY.
[6]"Temporal analysis of sucrose-induced phosphorylation changes in plasma membrane proteins of Arabidopsis."
Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.
Mol. Cell. Proteomics 6:1711-1726(2007) [PubMed: 17586839] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, MASS SPECTROMETRY.

Cross-references

Sequence databases

M63234 mRNA. Translation: AAA32850.1. Sequence problems.
AL031135 Genomic DNA. Translation: CAA20030.1. Sequence problems.
AL161587 Genomic DNA. Translation: CAB80276.1. Sequence problems.
AY065403 mRNA. Translation: AAL38844.1.
AY096501 mRNA. Translation: AAM20151.1.
IPIIPI00549060.
PIRA39357.
C85420.
T04665.
RefSeqNP_195285.3.
UniGeneAt.57035

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActP27450. 8 interactions.

Protein family/group databases

TCDB1.A.26.1.1. plant plasmodesmata (PPD) family.

Proteomic databases

ProMEXP27450.

Genome annotation databases

GeneID829712.
GenomeReviewsGene locus AT4G35600 in contig CT486007_GR.
KEGGath:AT4G35600.
NMPDRfig|3702.1.peg.21645.

Organism-specific databases

GeneFarm1725. 129.
TAIRAt4g35600.

Phylogenomic databases

OMAP27450. NCASAID.

Enzyme and pathway databases

BRENDA2.7.11.1. 302.

Gene expression databases

ArrayExpressP27450.
GermOnlineAT4G35600. Arabidopsis thaliana.

Family and domain databases

InterProIPR000719. Prot_kinase_core.
IPR017441. Protein_kinase_ATP_BS.
IPR017442. Se/Thr_pkinase-rel.
IPR008271. Ser_thr_pkin_AS.
[Graphical view]
PfamPF00069. Pkinase. 1 hit.
[Graphical view]
ProDomPD000001. Prot_kinase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCX32_ARATH
AccessionPrimary (citable) accession number: P27450
Secondary accession number(s): O81792, Q8VZ07, Q9M068
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 21, 2004
Last modified: June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents