CRI4_MAIZE
ID CRI4_MAIZE Reviewed; 901 AA.
AC O24585;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Putative receptor protein kinase CRINKLY4;
DE EC=2.7.11.1;
DE Flags: Precursor;
GN Name=CR4;
OS Zea mays (Maize).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX NCBI_TaxID=4577;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. B73;
RX PubMed=8703079; DOI=10.1126/science.273.5280.1406;
RA Becraft P.W., Stinard P.S., McCarty D.R.;
RT "CRINKLY4: a TNFR-like receptor kinase involved in maize epidermal
RT differentiation.";
RL Science 273:1406-1409(1996).
RN [2]
RP HOMODIMERIZATION.
RX PubMed=18539132; DOI=10.1016/j.abb.2008.05.010;
RA Stokes K.D., Gururaj Rao A.;
RT "Dimerization properties of the transmembrane domains of Arabidopsis
RT CRINKLY4 receptor-like kinase and homologs.";
RL Arch. Biochem. Biophys. 477:219-226(2008).
CC -!- FUNCTION: Putative receptor protein kinase. Could play a role in a
CC differentiation signal. The CRINKLY4 (CR4) mutation affects leaf
CC epidermis differentiation such that cell size and morphology are
CC altered, and surface functions are compromised, allowing graft-like
CC fusions between organs.
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 -!- 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;
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Endosome, multivesicular body membrane
CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
CC Note=Also localized into protein export bodies. {ECO:0000250}.
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; U67422; AAB09771.1; -; mRNA.
DR PIR; T04108; T04108.
DR RefSeq; NP_001335655.1; NM_001348726.1.
DR AlphaFoldDB; O24585; -.
DR SMR; O24585; -.
DR STRING; 4577.GRMZM2G051637_P01; -.
DR PaxDb; O24585; -.
DR PRIDE; O24585; -.
DR EnsemblPlants; Zm00001eb406780_T001; Zm00001eb406780_P001; Zm00001eb406780.
DR EnsemblPlants; Zm00001eb406780_T002; Zm00001eb406780_P002; Zm00001eb406780.
DR GeneID; 542346; -.
DR Gramene; Zm00001eb406780_T001; Zm00001eb406780_P001; Zm00001eb406780.
DR Gramene; Zm00001eb406780_T002; Zm00001eb406780_P002; Zm00001eb406780.
DR KEGG; zma:542346; -.
DR MaizeGDB; 128723; -.
DR eggNOG; ENOG502QUN0; Eukaryota.
DR HOGENOM; CLU_009948_0_0_1; -.
DR OMA; TPAHFPF; -.
DR OrthoDB; 684563at2759; -.
DR Proteomes; UP000007305; Chromosome 10.
DR ExpressionAtlas; O24585; baseline and differential.
DR Genevisible; O24585; ZM.
DR GO; GO:0009986; C:cell surface; IEA:EnsemblPlants.
DR GO; GO:0030139; C:endocytic vesicle; IEA:EnsemblPlants.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
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:0009793; P:embryo development ending in seed dormancy; IEA:EnsemblPlants.
DR GO; GO:0048439; P:flower morphogenesis; IEA:EnsemblPlants.
DR GO; GO:0010311; P:lateral root formation; IEA:EnsemblPlants.
DR GO; GO:0090627; P:plant epidermal cell differentiation; IEA:EnsemblPlants.
DR GO; GO:0046777; P:protein autophosphorylation; IEA:EnsemblPlants.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IEA:EnsemblPlants.
DR GO; GO:0048829; P:root cap development; IEA:EnsemblPlants.
DR Gene3D; 2.130.10.30; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR001368; TNFR/NGFR_Cys_rich_reg.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00020; TNFR_c6; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00208; TNFR; 1.
DR SUPFAM; SSF50985; SSF50985; 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.
DR PROSITE; PS50050; TNFR_NGFR_2; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Developmental protein; Disulfide bond;
KW Endosome; Glycoprotein; Kinase; Membrane; Nucleotide-binding; Receptor;
KW Reference proteome; Repeat; Serine/threonine-protein kinase; Signal;
KW Transferase; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..901
FT /note="Putative receptor protein kinase CRINKLY4"
FT /id="PRO_0000024320"
FT TOPO_DOM 25..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..901
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 33..68
FT /note="1"
FT REPEAT 72..107
FT /note="2"
FT REPEAT 125..160
FT /note="3"
FT REPEAT 162..195
FT /note="4"
FT REPEAT 203..236
FT /note="5"
FT REPEAT 253..287
FT /note="6"
FT REPEAT 292..330
FT /note="7"
FT REPEAT 357..391
FT /note="TNFR-Cys"
FT DOMAIN 505..712
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 33..330
FT /note="7 X 36 AA repeats"
FT REGION 845..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 634
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 511..519
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 533
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT CARBOHYD 151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 338..365
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 368..382
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
FT DISULFID 372..390
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00206"
SQ SEQUENCE 901 AA; 97439 MW; 52F8481AC187E061 CRC64;
MDHVPALVLA GCCFLALLPG WACGLGSMSS IAVSYGEDGP VFCGLNSDGS HLVACFGADA
SVLYGAPPNI PFLGLTAGDG FVCGLLLDTR QPYCWGSNSY VKSGVPQPMV EGARYSELSA
GDNHLCALRA AQDGGRGSSA ATSLIDCWGY NMTATHAVDE AVSTVSAGSV FNCGLFARNR
TVFCWGDETV SGVVGLAPRD LHFQSIGAGG YHVCGVLENA QVFCWGRSLE MQQVVPSSAI
GDGDVNIVPM DAMSTVVGGR FHACGIRSLD HQVACWGFTL HNSTSPPKGL KMYALVAGDY
FTCGVPAETS LMPRCWGNSG PLALPMAVPP GICVPTACSH GYYEYVNHGE VGSIKVCKPA
NSRLCLPCST GCPEGLYESS PCNATADRVC QFDCLKCVTD ECLSFCLSQK RTKSRKLMAF
QMRIFVAEIV FAVVLVLSVS VTTCLYVRHK LRHCQCSNRE LRLAKSTAYS FRKDNMKIQP
DMEDLKIRRA QEFSYEELEQ ATGGFSEDSQ VGKGSFSCVF KGILRDGTVV AVKRAIKASD
VKKSSKEFHN ELDLLSRLNH AHLLNLLGYC EDGSERLLVY EFMAHGSLYQ HLHGKDPNLK
KRLNWARRVT IAVQAARGIE YLHGYACPPV IHRDIKSSNI LIDEDHNARV ADFGLSILGP
ADSGTPLSEL PAGTLGYLDP EYYRLHYLTT KSDVYSFGVV LLEILSGRKA IDMQFEEGNI
VEWAVPLIKA GDIFAILDPV LSPPSDLEAL KKIASVACKC VRMRGKDRPS MDKVTTALEH
ALALLMGSPC IEQPILPTEV VLGSSRMHKV SQMSSNHSCS ENELADGEDQ GIGYRAPSWI
TFPSVTSSQR RKSSASEADI VGRRATDGRN VGSSIGDGLR SLEEEIAPAS PQENLYLQHN
F
