RIK_MAIZE
ID RIK_MAIZE Reviewed; 616 AA.
AC Q32SG5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Protein RIK;
DE AltName: Full=Rough sheath 2-interacting KH domain protein;
DE Short=RS2-interacting KH domain protein;
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], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP INTERACTION WITH RS2.
RC STRAIN=cv. B73; TISSUE=Apices;
RX PubMed=16243907; DOI=10.1105/tpc.105.035477;
RA Phelps-Durr T.L., Thomas J., Vahab P., Timmermans M.C.P.;
RT "Maize rough sheath2 and its Arabidopsis orthologue ASYMMETRIC LEAVES1
RT interact with HIRA, a predicted histone chaperone, to maintain knox gene
RT silencing and determinacy during organogenesis.";
RL Plant Cell 17:2886-2898(2005).
CC -!- SUBUNIT: Interacts with RS2. {ECO:0000269|PubMed:16243907}.
CC -!- INTERACTION:
CC Q32SG5; Q9S7B2: RS2; NbExp=2; IntAct=EBI-761296, EBI-761350;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16243907}.
CC -!- TISSUE SPECIFICITY: Expressed in vegetative tissues. More abundant in
CC apices and young leaf primordia than in fully expanded leaf tissues.
CC {ECO:0000269|PubMed:16243907}.
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DR EMBL; AY940679; AAY24682.1; -; mRNA.
DR AlphaFoldDB; Q32SG5; -.
DR IntAct; Q32SG5; 1.
DR STRING; 4577.GRMZM2G079823_P01; -.
DR PaxDb; Q32SG5; -.
DR PRIDE; Q32SG5; -.
DR eggNOG; KOG1960; Eukaryota.
DR PRO; PR:Q32SG5; -.
DR Proteomes; UP000007305; Unplaced.
DR ExpressionAtlas; Q32SG5; baseline and differential.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR031121; RIK/BLOM7.
DR PANTHER; PTHR15744; PTHR15744; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..616
FT /note="Protein RIK"
FT /id="PRO_0000299131"
FT DOMAIN 198..304
FT /note="KH"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..566
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 616 AA; 65608 MW; 1B9697DB68B51DBA CRC64;
MTEDRAHKVA DEPAASGRQS PERKKRKWDQ PAEDLVSAAV TAAAVSGMPV MNFGALPGVV
LPGVTAYGAA TLPSVVPVPY SLPPHIAPSV LQNAAAAAQK LSQAKIPDEV IAREIVINDA
DPSVRYKLTK RQTQEEIQKC TNTVIITRGK YHPPNLLPDG EKPLYLHISA GSQLKDTAER
IKAVDRAASM IEEILKQGTT SESISVPFSS STGQAVRPFS ASVFLGFDAD PSLNITARIR
GPNDQYINHI MKETGVTVVL RGKDSENLGS CHSEASQQPL HLYLTSMHLK NLEAAKVLAE
NLLDTVAAEF GASRISSSKV YGAVPPPQQL LAGVDTSGTK SDVHYIVGPN VLSGATHSFA
STGVIAPVVA PAVTVQSGAP TYSGVPLPSN MAYPIPPANG GAFYSGYGDI YPQATPLQQL
AFTLKHASSS ATQAVPVTST PTSMATKGNS ILDAEMDKRS RRKFQELPVS KGPATESQNS
QQGSKFVKTG LDSSGNIGSS SIAPPKKVHP GSNGMLPQEE ADMPSHLSIS TKMLPPPLKS
MLPLPPRSMP PPPPKSMPPP PPKFPSDEFL SRNENKFFPL KEPTAPPRSF DAISVLPSER
RPREPKEEKN KRHTCV