LHX3_XENLA
ID LHX3_XENLA Reviewed; 395 AA.
AC P36200;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=LIM/homeobox protein Lhx3;
DE Short=LIM homeobox protein 3;
DE AltName: Full=Homeobox protein LIM-3;
DE Short=xLIM-3;
GN Name=lhx3; Synonyms=lim3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8103491; DOI=10.1006/dbio.1993.1237;
RA Taira M., Hayes W.P., Otani H., Dawid I.B.;
RT "Expression of LIM class homeobox gene Xlim-3 in Xenopus development is
RT limited to neural and neuroendocrine tissues.";
RL Dev. Biol. 159:245-256(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 162-200.
RX PubMed=1347750; DOI=10.1101/gad.6.3.356;
RA Taira M., Jamrich M., Good P.J., Dawid I.B.;
RT "The LIM domain-containing homeo box gene Xlim-1 is expressed specifically
RT in the organizer region of Xenopus gastrula embryos.";
RL Genes Dev. 6:356-366(1992).
RN [3]
RP INTERACTION WITH LDB1 AND RNF12.
RX PubMed=12874135; DOI=10.1242/dev.00621;
RA Hiratani I., Yamamoto N., Mochizuki T., Ohmori S.-Y., Taira M.;
RT "Selective degradation of excess Ldb1 by Rnf12/RLIM confers proper Ldb1
RT expression levels and Xlim-1/Ldb1 stoichiometry in Xenopus organizer
RT functions.";
RL Development 130:4161-4175(2003).
CC -!- FUNCTION: May be involved in the specification and maintenance of
CC differentiation of distinct neuronal and neuroendocrine tissues. Early
CC marker for the pituitary and pineal lineages, it may be involved in
CC specifying these lineages.
CC -!- SUBUNIT: Interacts with ldb1 and with the N-terminus of rnf12.
CC {ECO:0000269|PubMed:12874135}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In dorsal regions at neural tube and tailbud stages
CC and in adults predominantly in the pituitary gland and weakly in the
CC eye and brain.
CC -!- DEVELOPMENTAL STAGE: First detectable at the neural plate stage in the
CC stomodeal-hypophyseal (pituitary) anlage and in the neural plate. At
CC later stages it persists in the pituitary and pineal, retina, hindbrain
CC and spinal cord.
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DR EMBL; Z22702; CAA80402.1; -; mRNA.
DR EMBL; Z11589; CAA77674.1; -; mRNA.
DR PIR; S38821; S38821.
DR RefSeq; NP_001081623.1; NM_001088154.1.
DR AlphaFoldDB; P36200; -.
DR SMR; P36200; -.
DR GeneID; 397959; -.
DR KEGG; xla:397959; -.
DR CTD; 397959; -.
DR Xenbase; XB-GENE-865930; lhx3.L.
DR OrthoDB; 1174754at2759; -.
DR Proteomes; UP000186698; Chromosome 8L.
DR Bgee; 397959; Expressed in camera-type eye and 4 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00412; LIM; 2.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00132; LIM; 2.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Activator; DNA-binding; Homeobox; LIM domain; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..395
FT /note="LIM/homeobox protein Lhx3"
FT /id="PRO_0000075786"
FT DOMAIN 28..78
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 87..141
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DNA_BIND 154..213
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 208..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 174
FT /note="N -> D (in Ref. 2; CAA77674)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 395 AA; 44031 MW; 31A97C70A683C539 CRC64;
MLLERVRTGT QKSSDMCGYT GSPEIPQCAG CNQHIVDRFI LKVLDRHWHS KCLKCNDCQI
QLAEKCFSRG DSVYCKDDFF KRFGTKCAAC QQGIPPTQVV RRAQEFVYHL HCFACIVCKR
QLATGDEFYL MEDSRLVCKA DYETAKQREA ESTAKRPRTT ITAKQLETLK NAYNNSPKPA
RHVREQLSSE TGLDMRVVQV WFQNRRAKEK RLKKDAGRQR WGQYFRNMKR SRGNSKSDKD
SIQEEGPDSD AEVSFTDEPS MSEMNHSNGI YNSLNDSSPV LGRQAGSNGP FSLEHGGIPT
QDQYHNLRSN SPYGIPQSPA SLQSMPGHQS LLSNLAFPDT GLGIIGQGGQ GVAPTMRVIG
VNGPSSDLST GSSGGYPDFP VSPASWLDEV DHTQF