ZAR1_ARATH
ID ZAR1_ARATH Reviewed; 716 AA.
AC Q9ZU46;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Receptor protein kinase-like protein ZAR1 {ECO:0000303|PubMed:27014878};
DE EC=2.7.11.1 {ECO:0000305};
DE AltName: Full=Protein ZYGOTIC ARREST 1 {ECO:0000303|PubMed:27014878};
DE Flags: Precursor;
GN Name=ZAR1 {ECO:0000303|PubMed:27014878};
GN OrderedLocusNames=At2g01210 {ECO:0000312|Araport:AT2G01210};
GN ORFNames=F10A8.9 {ECO:0000312|EMBL:AAD14521.1};
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].
RX PubMed=20064227; DOI=10.1186/1471-2164-11-19;
RA Gou X., He K., Yang H., Yuan T., Lin H., Clouse S.D., Li J.;
RT "Genome-wide cloning and sequence analysis of leucine-rich repeat receptor-
RT like protein kinase genes in Arabidopsis thaliana.";
RL BMC Genomics 11:19-19(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 FUNCTION, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP MUTAGENESIS OF LYS-534; 358-GLU--LYS-373 AND 557-GLN--GLN-584, INTERACTION
RP WITH CAM1; CML8 AND GB1, DOMAIN, AND AUTOPHOSPHORYLATION.
RX PubMed=27014878; DOI=10.1371/journal.pgen.1005933;
RA Yu T.Y., Shi D.Q., Jia P.F., Tang J., Li H.J., Liu J., Yang W.C.;
RT "The Arabidopsis receptor kinase ZAR1 is required for zygote asymmetric
RT division and its daughter cell fate.";
RL PLoS Genet. 12:E1005933-E1005933(2016).
CC -!- FUNCTION: Receptor protein kinase acting as an integrator for
CC intracellular calcium and heterotrimeric G protein signaling with
CC extracellular signals during early zygote development. Involved in
CC modulating the asymmetric division of zygote and the cell fate
CC determination of its daughter cells. {ECO:0000269|PubMed:27014878}.
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: Part of an in vivo complex containing ZAR1, CAM1 and GB1.
CC Interacts (via CaMBD domain) with calmodulins CAM1 and CML8 in a
CC calcium independent manner. Interacts (via GBeta-binding domain) with
CC GB1. {ECO:0000269|PubMed:27014878}.
CC -!- INTERACTION:
CC Q9ZU46; A0A1I9LQ53: At3g50230; NbExp=3; IntAct=EBI-16954860, EBI-20654045;
CC Q9ZU46; Q9LVI6: RLK902; NbExp=4; IntAct=EBI-16954860, EBI-1626936;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27014878};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed at the micropylar nuclei of the embryo
CC sac at eight-nucleate stage before cellularization, but not in chalazal
CC nuclei. After cellularization, expressed in central cell and synergids
CC in mature embryo sac. After fertilization, detected specifically in
CC zygote, endosperm precursor cell, and later in endosperm. In addition,
CC also present in sperm and the vegetative cells in both pollen and
CC pollen tube. Expressed at high level in the egg cell, the central cell,
CC the endosperm, and at low level in the zygote.
CC {ECO:0000269|PubMed:27014878}.
CC -!- DOMAIN: The CaMBD domain (358-373) is required for calmodulin binding.
CC {ECO:0000269|PubMed:27014878}.
CC -!- DOMAIN: The GBeta-binding domain (577-584) is required for GB1 binding.
CC {ECO:0000269|PubMed:27014878}.
CC -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC inactive. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC -!- PTM: Autophosphorylated. The kinase activity is activated by the
CC binding of CAM1 and/or GB1. {ECO:0000269|PubMed:27014878}.
CC -!- DISRUPTION PHENOTYPE: Embryo lethal when homozygous.
CC {ECO:0000269|PubMed:27014878}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; FJ708685; ACN59280.1; -; mRNA.
DR EMBL; AC006200; AAD14521.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05416.1; -; Genomic_DNA.
DR PIR; H84421; H84421.
DR RefSeq; NP_178230.1; NM_126182.4.
DR AlphaFoldDB; Q9ZU46; -.
DR SMR; Q9ZU46; -.
DR IntAct; Q9ZU46; 31.
DR STRING; 3702.AT2G01210.1; -.
DR iPTMnet; Q9ZU46; -.
DR PaxDb; Q9ZU46; -.
DR PRIDE; Q9ZU46; -.
DR ProteomicsDB; 232313; -.
DR EnsemblPlants; AT2G01210.1; AT2G01210.1; AT2G01210.
DR GeneID; 814649; -.
DR Gramene; AT2G01210.1; AT2G01210.1; AT2G01210.
DR KEGG; ath:AT2G01210; -.
DR Araport; AT2G01210; -.
DR TAIR; locus:2038706; AT2G01210.
DR eggNOG; ENOG502QT84; Eukaryota.
DR HOGENOM; CLU_000288_92_6_1; -.
DR OMA; AADPCAW; -.
DR OrthoDB; 826997at2759; -.
DR PhylomeDB; Q9ZU46; -.
DR PRO; PR:Q9ZU46; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU46; baseline and differential.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0090406; C:pollen tube; IDA:TAIR.
DR GO; GO:0099503; C:secretory vesicle; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:TAIR.
DR GO; GO:0010070; P:zygote asymmetric cell division; IMP:UniProtKB.
DR GO; GO:0010069; P:zygote asymmetric cytokinesis in embryo sac; IMP:TAIR.
DR Gene3D; 3.80.10.10; -; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR013210; LRR_N_plant-typ.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF08263; LRRNT_2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00369; LRR_TYP; 3.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Kinase; Leucine-rich repeat; Membrane; Phosphoprotein;
KW Receptor; Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..716
FT /note="Receptor protein kinase-like protein ZAR1"
FT /evidence="ECO:0000255"
FT /id="PRO_5006753639"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 87..111
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 113..135
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 136..159
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 160..183
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT REPEAT 185..208
FT /note="LRR 5"
FT /evidence="ECO:0000255"
FT REPEAT 210..233
FT /note="LRR 6"
FT /evidence="ECO:0000255"
FT REPEAT 234..258
FT /note="LRR 7"
FT /evidence="ECO:0000255"
FT DOMAIN 404..711
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 358..373
FT /note="CaMBD"
FT /evidence="ECO:0000269|PubMed:27014878"
FT REGION 557..584
FT /note="GBeta-binding"
FT /evidence="ECO:0000269|PubMed:27014878"
FT REGION 575..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94F62"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q94AG2"
FT MUTAGEN 358..373
FT /note="Missing: Loss of interaction with CAM1 or CML8."
FT /evidence="ECO:0000269|PubMed:27014878"
FT MUTAGEN 534
FT /note="K->A: Loss of kinase activity, but no effect on GB1,
FT CAM1 or CML8 binding."
FT /evidence="ECO:0000269|PubMed:27014878"
FT MUTAGEN 577..584
FT /note="Missing: Loss of interaction with GB1."
FT /evidence="ECO:0000269|PubMed:27014878"
SQ SEQUENCE 716 AA; 78307 MW; 80737FABB2E1C27E CRC64;
MLASLIIFVA LLCNVTVISG LNDEGFALLT FKQSVHDDPT GSLNNWNSSD ENACSWNGVT
CKELRVVSLS IPRKNLYGSL PSSLGFLSSL RHLNLRSNRF YGSLPIQLFH LQGLQSLVLY
GNSFDGSLSE EIGKLKLLQT LDLSQNLFNG SLPLSILQCN RLKTLDVSRN NLSGPLPDGF
GSAFVSLEKL DLAFNQFNGS IPSDIGNLSN LQGTADFSHN HFTGSIPPAL GDLPEKVYID
LTFNNLSGPI PQTGALMNRG PTAFIGNTGL CGPPLKDLCQ GYQLGLNASY PFIPSNNPPE
DSDSTNSETK QKSSGLSKSA VIAIVLCDVF GICLVGLLFT YCYSKFCACN RENQFGVEKE
SKKRASECLC FRKDESETPS ENVEHCDIVP LDAQVAFNLE ELLKASAFVL GKSGIGIVYK
VVLENGLTLA VRRLGEGGSQ RFKEFQTEVE AIGKLKHPNI ASLRAYYWSV DEKLLIYDYV
SNGNLATALH GKPGMMTIAP LTWSERLRIM KGIATGLVYL HEFSPKKYVH GDLKPSNILI
GQDMEPKISD FGLARLANIA GGSSPTIQSN RIIQTDQQPQ ERQQHHHKSV SSEFTAHSSS
GSYYQAPETL KMVKPSQKWD VYSYGIILLE LIAGRSPAVE VGTSEMDLVR WVQVCIEEKK
PLCDVLDPCL APEAETEDEI VAVLKIAISC VNSSPEKRPT MRHVSDTLDR LPVAGD
