CST_ARATH
ID CST_ARATH Reviewed; 419 AA.
AC P27450; O81792; Q8VZ07; Q9M068;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Probable serine/threonine-protein kinase CST {ECO:0000305};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein CAST AWAY {ECO:0000303|PubMed:21628627};
GN Name=CST {ECO:0000303|PubMed:21628627};
GN Synonyms=CX32 {ECO:0000303|PubMed:8400879},
GN KIN4 {ECO:0000303|PubMed:21219905}; OrderedLocusNames=At4g35600;
GN ORFNames=F8D20.110;
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 PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1851993; DOI=10.1073/pnas.88.10.4119;
RA Meiners S., Xu A., Schindler M.;
RT "Gap junction protein homologue from Arabidopsis thaliana: evidence for
RT connexins in plants.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4119-4122(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
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 [4]
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 [5]
RP DISCUSSION OF SEQUENCE.
RX PubMed=8400879; DOI=10.2307/3869621;
RA Mushegian A.R., Koonin E.V.;
RT "The proposed plant connexin is a protein kinase-like protein.";
RL Plant Cell 5:998-999(1993).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Seedling;
RX PubMed=17586839; DOI=10.1074/mcp.m700164-mcp200;
RA Niittylae T., Fuglsang A.T., Palmgren M.G., Frommer W.B., Schulze W.X.;
RT "Temporal analysis of sucrose-induced phosphorylation changes in plasma
RT membrane proteins of Arabidopsis.";
RL Mol. Cell. Proteomics 6:1711-1726(2007).
RN [9]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-2, AND MYRISTOYLATION AT GLY-2.
RX PubMed=21219905; DOI=10.1016/j.febslet.2011.01.001;
RA Stael S., Bayer R.G., Mehlmer N., Teige M.;
RT "Protein N-acylation overrides differing targeting signals.";
RL FEBS Lett. 585:517-522(2011).
RN [10]
RP FUNCTION, INTERACTION WITH SOBIR1/EVR AND RLK5/HAE, SUBCELLULAR LOCATION,
RP AUTOPHOSPHORYLATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLY-2; CYS-4;
RP LYS-124 AND GLY-157, PALMITOYLATION AT CYS-4, AND MYRISTOYLATION AT GLY-2.
RX PubMed=21628627; DOI=10.1104/pp.111.175224;
RA Burr C.A., Leslie M.E., Orlowski S.K., Chen I., Wright C.E., Daniels M.J.,
RA Liljegren S.J.;
RT "CAST AWAY, a membrane-associated receptor-like kinase, inhibits organ
RT abscission in Arabidopsis.";
RL Plant Physiol. 156:1837-1850(2011).
CC -!- FUNCTION: Acts as a spatial inhibitor of signaling that modulates
CC abscission zone cell adhesion and expansion. Acts both directly and
CC indirectly by physically interacting with RLK5/HAE and SOBIR1/EVR at
CC the cell surface. {ECO:0000269|PubMed:21628627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000305};
CC -!- SUBUNIT: Interacts with SOBIR1/EVR and RLK5/HAE.
CC {ECO:0000269|PubMed:21628627}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21219905,
CC ECO:0000269|PubMed:21628627}; Lipid-anchor
CC {ECO:0000269|PubMed:21628627, ECO:0000305|PubMed:21219905}. Nucleus
CC {ECO:0000269|PubMed:21219905}. Note=Predominantly localized at the
CC plasma membrane. {ECO:0000269|PubMed:21219905}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=P27450-1; Sequence=Displayed;
CC -!- PTM: Autophosphorylated on serine, threonine and tyrosine residues.
CC {ECO:0000269|PubMed:21628627}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- CAUTION: Was originally (PubMed:1851993) reported to be a connexin and
CC to contain transmembrane domains. PubMed:8400879 authors have assigned
CC that this is not a connexin, but rather a protein kinase.
CC {ECO:0000305|PubMed:1851993}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA32850.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAA32850.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
CC Sequence=CAA20030.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80276.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M63234; AAA32850.1; ALT_SEQ; mRNA.
DR EMBL; AL031135; CAA20030.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161587; CAB80276.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86538.1; -; Genomic_DNA.
DR EMBL; AY065403; AAL38844.1; -; mRNA.
DR EMBL; AY096501; AAM20151.1; -; mRNA.
DR PIR; A39357; A39357.
DR PIR; C85420; C85420.
DR PIR; T04665; T04665.
DR RefSeq; NP_195285.3; NM_119725.5. [P27450-1]
DR AlphaFoldDB; P27450; -.
DR SMR; P27450; -.
DR BioGRID; 14994; 12.
DR IntAct; P27450; 8.
DR STRING; 3702.AT4G35600.2; -.
DR iPTMnet; P27450; -.
DR PaxDb; P27450; -.
DR PRIDE; P27450; -.
DR ProteomicsDB; 222631; -. [P27450-1]
DR EnsemblPlants; AT4G35600.1; AT4G35600.1; AT4G35600. [P27450-1]
DR GeneID; 829712; -.
DR Gramene; AT4G35600.1; AT4G35600.1; AT4G35600. [P27450-1]
DR KEGG; ath:AT4G35600; -.
DR Araport; AT4G35600; -.
DR eggNOG; KOG1187; Eukaryota.
DR HOGENOM; CLU_000288_21_2_1; -.
DR InParanoid; P27450; -.
DR PhylomeDB; P27450; -.
DR PRO; PR:P27450; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P27450; baseline and differential.
DR Genevisible; P27450; AT.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0060862; P:negative regulation of floral organ abscission; IMP:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell membrane; Kinase; Lipoprotein;
KW Membrane; Myristate; Nucleotide-binding; Nucleus; Palmitate;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:21219905,
FT ECO:0000305|PubMed:21628627"
FT CHAIN 2..419
FT /note="Probable serine/threonine-protein kinase CST"
FT /id="PRO_0000024321"
FT DOMAIN 86..368
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 8..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 218
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 92..100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:14506206,
FT ECO:0007744|PubMed:15308754, ECO:0007744|PubMed:17586839"
FT MOD_RES 169
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 253
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 258
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT MOD_RES 266
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O48814"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000305|PubMed:21219905,
FT ECO:0000305|PubMed:21628627"
FT LIPID 4
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:21628627"
FT MUTAGEN 2
FT /note="G->A: Drastic reduction of plasma membrane
FT localization and strong increase of nuclear localization.
FT Partial redistribution from the plasma membrane to the
FT cytoplasm."
FT /evidence="ECO:0000269|PubMed:21219905,
FT ECO:0000269|PubMed:21628627"
FT MUTAGEN 4
FT /note="C->S: Partial redistribution from the plasma
FT membrane to the cytoplasm."
FT /evidence="ECO:0000269|PubMed:21628627"
FT MUTAGEN 124
FT /note="K->A: Abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:21628627"
FT MUTAGEN 157
FT /note="G->R: In cst-1; abolishes kinase activity."
FT /evidence="ECO:0000269|PubMed:21628627"
SQ SEQUENCE 419 AA; 46340 MW; 7C85AB6C38925145 CRC64;
MGACISFFSS SSPSKTGLHS HATTNNHSNG TEFSSTTGAT TNSSVGQQSQ FSDISTGIIS
DSGKLLESPN LKVYNFLDLK TATKNFKPDS MLGQGGFGKV YRGWVDATTL APSRVGSGMI
VAIKRLNSES VQGFAEWRSE VNFLGMLSHR NLVKLLGYCR EDKELLLVYE FMPKGSLESH
LFRRNDPFPW DLRIKIVIGA ARGLAFLHSL QREVIYRDFK ASNILLDSNY DAKLSDFGLA
KLGPADEKSH VTTRIMGTYG YAAPEYMATG HLYVKSDVFA FGVVLLEIMT GLTAHNTKRP
RGQESLVDWL RPELSNKHRV KQIMDKGIKG QYTTKVATEM ARITLSCIEP DPKNRPHMKE
VVEVLEHIQG LNVVPNRSST KQAVANSSRS SPHHYRYKAG ALGAERKRAT PGRFGSVEK
