ID   RSH1_MAIZE              Reviewed;         351 AA.
AC   Q41853;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Homeobox protein rough sheath 1;
GN   Name=RS1;
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=7557382; DOI=10.1101/gad.9.18.2292;
RA   Schneeberger R.G., Becraft P.W., Hake S., Freeling M.;
RT   "Ectopic expression of the knox homeo box gene rough sheath1 alters cell
RT   fate in the maize leaf.";
RL   Genes Dev. 9:2292-2304(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 229-316.
RC   TISSUE=Ear of corn, and Seedling;
RX   PubMed=7866030; DOI=10.2307/3869914;
RA   Kerstetter R., Vollbrecht E., Lowe B., Veit B., Yamaguchi J., Hake S.;
RT   "Sequence analysis and expression patterns divide the Maize knotted1-like
RT   homeobox genes into two classes.";
RL   Plant Cell 6:1877-1887(1994).
CC   -!- FUNCTION: Plays a possible role in patterning the placement of lateral
CC       organs along the axis of the shoot. Mutations in RS1 alters cell fate
CC       and causes unregulated cell division and expansion in the leaf.
CC       Probably binds to the DNA sequence 5'-TGAC-3'.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the shoot apical meristem in a
CC       circular pattern preceding leaf initiation, but is not detectable in
CC       leaf primordia or mature leaves in normal plants. Rings of RS1
CC       expression subtend leaf insertion sites in the shoot, and lateral organ
CC       primordia in inflorescence and floral meristems.
CC   -!- SIMILARITY: Belongs to the TALE/KNOX homeobox family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00559}.
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DR   EMBL; L44133; AAA86287.1; -; mRNA.
DR   PIR; T03946; T03946.
DR   AlphaFoldDB; Q41853; -.
DR   SMR; Q41853; -.
DR   STRING; 4577.GRMZM2G028041_P01; -.
DR   PaxDb; Q41853; -.
DR   PRIDE; Q41853; -.
DR   eggNOG; KOG0773; Eukaryota.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; Q41853; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00086; homeodomain; 1.
DR   InterPro; IPR005539; ELK_dom.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR008422; Homeobox_KN_domain.
DR   InterPro; IPR005540; KNOX1.
DR   InterPro; IPR005541; KNOX2.
DR   Pfam; PF03789; ELK; 1.
DR   Pfam; PF05920; Homeobox_KN; 1.
DR   Pfam; PF03790; KNOX1; 1.
DR   Pfam; PF03791; KNOX2; 1.
DR   SMART; SM01188; ELK; 1.
DR   SMART; SM00389; HOX; 1.
DR   SMART; SM01255; KNOX1; 1.
DR   SMART; SM01256; KNOX2; 1.
DR   SUPFAM; SSF46689; SSF46689; 1.
DR   PROSITE; PS51213; ELK; 1.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; DNA-binding; Homeobox; Nucleus; Reference proteome.
FT   CHAIN           1..351
FT                   /note="Homeobox protein rough sheath 1"
FT                   /id="PRO_0000049275"
FT   DOMAIN          232..252
FT                   /note="ELK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00559"
FT   DNA_BIND        253..316
FT                   /note="Homeobox; TALE-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          187..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   351 AA;  38795 MW;  ED0798D3502FF8DA CRC64;
     MDQSFGNLGA GAGSSSGGSN SKAAATAVSS SSFLQLPLST ASPAYYGAPL ALLHHAAAAP
     SSSQQHQQQQ HHHHYARHGA EMSAAEAEAI KAKIVAHPQY SALLAAYLDC QKVGAPPDVL
     ERLTAMAAKL DASAAGRHEP RDPELDQFME AYCNMLVKYR EELTRPIDEA MEFLKRVEAQ
     LDCISGGGGS SSARLSLADG KSEGVGSSED DMDPNGREND PPEIDPRAED KELKYQLLKK
     YSGYLSSLRQ EFSKKKKKGK LPKEARQKLL HWWELHYKWP YPSETEKIAL AESTGLDQKQ
     INNWFINQRK RHWKPSEDMP FVMMEGFHPQ NAAALYMDGP FMRDGMYRLG S