STM_ARATH
ID STM_ARATH Reviewed; 382 AA.
AC Q38874; Q8RXJ1; Q9MAV3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 25-MAY-2022, entry version 168.
DE RecName: Full=Homeobox protein SHOOT MERISTEMLESS {ECO:0000303|PubMed:8538741};
GN Name=STM {ECO:0000303|PubMed:8538741};
GN OrderedLocusNames=At1g62360 {ECO:0000312|Araport:AT1G62360};
GN ORFNames=F2401.9 {ECO:0000312|EMBL:AAF70849.1};
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].
RC STRAIN=cv. Wassilewskija;
RX PubMed=8538741; DOI=10.1038/379066a0;
RA Long J.A., Moan E.I., Medford J.I., Barton M.K.;
RT "A member of the KNOTTED class of homeodomain proteins encoded by the STM
RT gene of Arabidopsis.";
RL Nature 379:66-69(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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] OF 57-382.
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 FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10079219; DOI=10.1242/dev.126.8.1563;
RA Aida M., Ishida T., Tasaka M.;
RT "Shoot apical meristem and cotyledon formation during Arabidopsis
RT embryogenesis: interaction among the CUP-SHAPED COTYLEDON and SHOOT
RT MERISTEMLESS genes.";
RL Development 126:1563-1570(1999).
RN [6]
RP INTERACTION WITH BEL1.
RX PubMed=11701881; DOI=10.2307/3871587;
RA Bellaoui M., Pidkowich M.S., Samach A., Kushalappa K., Kohalmi S.E.,
RA Modrusan Z., Crosby W.L., Haughn G.W.;
RT "The Arabidopsis BELL1 and KNOX TALE homeodomain proteins interact through
RT a domain conserved between plants and animals.";
RL Plant Cell 13:2455-2470(2001).
RN [7]
RP FUNCTION.
RX PubMed=11934861; DOI=10.1242/dev.129.8.1957;
RA Byrne M.E., Simorowski J., Martienssen R.A.;
RT "ASYMMETRIC LEAVES1 reveals knox gene redundancy in Arabidopsis.";
RL Development 129:1957-1965(2002).
RN [8]
RP INTERACTION WITH TALE/BELL PROTEINS, AND SUBCELLULAR LOCATION.
RX PubMed=16513846; DOI=10.1093/nar/gkl016;
RA Cole M., Nolte C., Werr W.;
RT "Nuclear import of the transcription factor SHOOT MERISTEMLESS depends on
RT heterodimerization with BLH proteins expressed in discrete sub-domains of
RT the shoot apical meristem of Arabidopsis thaliana.";
RL Nucleic Acids Res. 34:1281-1292(2006).
RN [9]
RP INTERACTION WITH BLH8/PNF.
RX PubMed=16741748; DOI=10.1007/s00425-006-0298-9;
RA Kanrar S., Onguka O., Smith H.M.S.;
RT "Arabidopsis inflorescence architecture requires the activities of KNOX-
RT BELL homeodomain heterodimers.";
RL Planta 224:1163-1173(2006).
RN [10]
RP INTERACTION WITH MBP2C, SUBCELLULAR LOCATION, AND HOMODIMERIZATION.
RX PubMed=17965274; DOI=10.1105/tpc.107.044354;
RA Winter N., Kollwig G., Zhang S., Kragler F.;
RT "MPB2C, a microtubule-associated protein, regulates non-cell-autonomy of
RT the homeodomain protein KNOTTED1.";
RL Plant Cell 19:3001-3018(2007).
RN [11]
RP INTERACTION WITH CCT8.
RX PubMed=21868675; DOI=10.1126/science.1205727;
RA Xu X.M., Wang J., Xuan Z., Goldshmidt A., Borrill P.G., Hariharan N.,
RA Kim J.Y., Jackson D.;
RT "Chaperonins facilitate KNOTTED1 cell-to-cell trafficking and stem cell
RT function.";
RL Science 333:1141-1144(2011).
RN [12]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH FTIP3 AND FTIP4.
RC STRAIN=cv. Columbia;
RX PubMed=29742441; DOI=10.1016/j.celrep.2018.04.033;
RA Liu L., Li C., Song S., Teo Z.W.N., Shen L., Wang Y., Jackson D., Yu H.;
RT "FTIP-dependent STM trafficking regulates shoot meristem development in
RT Arabidopsis.";
RL Cell Rep. 23:1879-1890(2018).
CC -!- FUNCTION: Required for shoot apical meristem (SAM) formation during
CC embryogenesis. Negatively regulates ASYMMETRIC LEAVES1 (AS1) and
CC ASYMMETRIC LEAVES2 (AS2 or LBD6). Probably binds to the DNA sequence
CC 5'-TGAC-3'. Binds to RNA (By similarity).
CC {ECO:0000250|UniProtKB:P24345, ECO:0000269|PubMed:10079219,
CC ECO:0000269|PubMed:11934861}.
CC -!- SUBUNIT: Forms homodimers (PubMed:17965274). May form heterodimeric
CC complexes with TALE/BELL proteins BEL1, BLH2, BLH3, BLH8/PNF, BLH9/PNY
CC and ATH1. Interacts with CCT8 (PubMed:21868675). Binds to MBP2C; this
CC interaction reduces RNA binding capacity (PubMed:17965274). Interacts
CC with FTIP3 and FTIP4 (PubMed:29742441). {ECO:0000269|PubMed:17965274,
CC ECO:0000269|PubMed:21868675, ECO:0000269|PubMed:29742441}.
CC -!- INTERACTION:
CC Q38874; P48731: ATH1; NbExp=9; IntAct=EBI-530523, EBI-912904;
CC Q38874; Q38897: BEL1; NbExp=9; IntAct=EBI-530523, EBI-1153783;
CC Q38874; Q9SJ56: BLH1; NbExp=3; IntAct=EBI-530523, EBI-1148379;
CC Q38874; Q9FWS9: BLH3; NbExp=4; IntAct=EBI-530523, EBI-912915;
CC Q38874; Q94KL5: BLH4; NbExp=3; IntAct=EBI-530523, EBI-1153797;
CC Q38874; O65685: BLH6; NbExp=3; IntAct=EBI-530523, EBI-1153881;
CC Q38874; Q9LZM8: BLH9; NbExp=7; IntAct=EBI-530523, EBI-530473;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000255|PROSITE-ProRule:PRU00559, ECO:0000269|PubMed:16513846,
CC ECO:0000269|PubMed:29742441}. Cell junction, plasmodesma
CC {ECO:0000269|PubMed:29742441}. Cytoplasm {ECO:0000269|PubMed:17965274}.
CC Endosome {ECO:0000269|PubMed:29742441}. Cell membrane
CC {ECO:0000269|PubMed:29742441}. Note=Association with TALE/BELL proteins
CC is necessary for nuclear location (PubMed:16513846). Dynamic
CC localization via a plasmodesmata-mediated cell-to-cell transport. This
CC shuttle is repressed by MBP2C binding in cytosolic punctae, at
CC microtubules (PubMed:17965274). Subcellular localization and
CC trafficking is regulated by FTIP3 and FTIP4, which promote endosome
CC localization (PubMed:29742441). {ECO:0000269|PubMed:16513846,
CC ECO:0000269|PubMed:17965274, ECO:0000269|PubMed:29742441}.
CC -!- TISSUE SPECIFICITY: Expressed in all four types of shoot apical
CC meristems (SAM) i.e. in vegetative, axillary, inflorescence and floral.
CC -!- DEVELOPMENTAL STAGE: First expressed in early to mid-globular-stage
CC embryos. In late globular stage, detected as a stripe running medially
CC across the top of the embryo. In heart stage embryo, expression is
CC restricted to a notch between the cotyledons, in both hypodermal and
CC protoderm cells. In the bending-cotyledon stage, localized in the SAM,
CC but disappears from the boundary region of cotyledon margins (BCM). In
CC seedlings and adult plants found in all shoot apical meristems. In the
CC inflorescence meristem, expression disappears as floral buds are
CC initiated and reappears in the later floral meristem where it is found
CC in the central portion of the developing gyneocium. Also detected in
CC the L1 layer of embryo. {ECO:0000269|PubMed:10079219}.
CC -!- SIMILARITY: Belongs to the TALE/KNOX homeobox family.
CC {ECO:0000255|PROSITE-ProRule:PRU00559}.
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DR EMBL; U32344; AAC49148.1; -; mRNA.
DR EMBL; AC003113; AAF70849.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33958.1; -; Genomic_DNA.
DR EMBL; AY080857; AAL87330.1; -; mRNA.
DR PIR; S68456; S68456.
DR PIR; T01446; T01446.
DR RefSeq; NP_176426.1; NM_104916.4.
DR AlphaFoldDB; Q38874; -.
DR SMR; Q38874; -.
DR BioGRID; 27755; 17.
DR IntAct; Q38874; 18.
DR STRING; 3702.AT1G62360.1; -.
DR iPTMnet; Q38874; -.
DR PaxDb; Q38874; -.
DR PRIDE; Q38874; -.
DR ProteomicsDB; 245218; -.
DR EnsemblPlants; AT1G62360.1; AT1G62360.1; AT1G62360.
DR GeneID; 842534; -.
DR Gramene; AT1G62360.1; AT1G62360.1; AT1G62360.
DR KEGG; ath:AT1G62360; -.
DR Araport; AT1G62360; -.
DR TAIR; locus:2027089; AT1G62360.
DR eggNOG; KOG0773; Eukaryota.
DR HOGENOM; CLU_040111_0_0_1; -.
DR InParanoid; Q38874; -.
DR OMA; ATHPGHY; -.
DR OrthoDB; 1095305at2759; -.
DR PhylomeDB; Q38874; -.
DR PRO; PR:Q38874; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q38874; baseline and differential.
DR Genevisible; Q38874; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0009506; C:plasmodesma; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:TAIR.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0048440; P:carpel development; IMP:TAIR.
DR GO; GO:0009691; P:cytokinin biosynthetic process; TAS:TAIR.
DR GO; GO:0010582; P:floral meristem determinacy; IGI:TAIR.
DR GO; GO:0010497; P:plasmodesmata-mediated intercellular transport; ISS:UniProtKB.
DR GO; GO:0009934; P:regulation of meristem structural organization; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0019827; P:stem cell population maintenance; TAS:TAIR.
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 1: Evidence at protein level;
KW Cell junction; Cell membrane; Cytoplasm; Developmental protein;
KW DNA-binding; Endosome; Homeobox; Membrane; Nucleus; Reference proteome;
KW RNA-binding.
FT CHAIN 1..382
FT /note="Homeobox protein SHOOT MERISTEMLESS"
FT /id="PRO_0000049316"
FT DOMAIN 262..282
FT /note="ELK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00559"
FT DNA_BIND 283..346
FT /note="Homeobox; TALE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 26..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 115
FT /note="S -> F (in Ref. 1; AAC49148)"
FT /evidence="ECO:0000305"
FT CONFLICT 229..233
FT /note="Missing (in Ref. 2; AAF70849)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="G -> D (in Ref. 1; AAC49148)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 382 AA; 42753 MW; 6227D3DE4093E732 CRC64;
MESGSNSTSC PMAFAGDNSD GPMCPMMMMM PPIMTSHQHH GHDHQHQQQE HDGYAYQSHH
QQSSSLFLQS LAPPQGTKNK VASSSSPSSC APAYSLMEIH HNEIVAGGIN PCSSSSSSAS
VKAKIMAHPH YHRLLAAYVN CQKVGAPPEV VARLEEACSS AAAAAASMGP TGCLGEDPGL
DQFMEAYCEM LVKYEQELSK PFKEAMVFLQ RVECQFKSLS LSSPSSFSGY GETAIDRNNN
GSSEEEVDMN NEFVDPQAED RELKGQLLRK YSGYLGSLKQ EFMKKRKKGK LPKEARQQLL
DWWSRHYKWP YPSEQQKLAL AESTGLDQKQ INNWFINQRK RHWKPSEDMQ FVVMDATHPH
HYFMDNVLGN PFPMDHISST ML
