LHX3_PIG
ID LHX3_PIG Reviewed; 383 AA.
AC O97581;
DT 25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=LIM/homeobox protein Lhx3;
DE Short=LIM homeobox protein 3;
DE AltName: Full=Homeobox protein LIM-3;
DE AltName: Full=Homeobox protein P-LIM;
DE Flags: Fragment;
GN Name=LHX3;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000312|EMBL:AAC99331.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Pituitary;
RX PubMed=10195693; DOI=10.1016/s0303-7207(98)00213-5;
RA Meier B.C., Price J.R., Parker G.E., Bridwell J.L., Rhodes S.J.;
RT "Characterization of the porcine Lhx3/LIM-3/P-Lim LIM homeodomain
RT transcription factor.";
RL Mol. Cell. Endocrinol. 147:65-74(1999).
CC -!- FUNCTION: Required for the establishment of the specialized cells of
CC the pituitary gland and the nervous system. Involved in the development
CC of interneurons and motor neurons in cooperation with LDB1 and ISL1.
CC Acts as a transcriptional activator. Binds to and activates the
CC promoter of the alpha-glycoprotein gene, and synergistically enhances
CC transcription from the prolactin promoter in cooperation with
CC POU1F1/Pit-1 (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:10195693}.
CC -!- SUBUNIT: Interacts with POU1F1. At neuronal promoters, interacts with
CC LDB1, in motor neurons LDB1 is displaced by ISL1 and a ternary complex
CC is formed in which ISL1 contacts both LHX3 and LDB1.
CC {ECO:0000250|UniProtKB:P50481, ECO:0000250|UniProtKB:Q9UBR4}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- DOMAIN: The LIM domain specifically interacts with the Pit-1 POU domain
CC and is required for synergistic interactions with Pit-1, but not for
CC basal transcriptional activation events.
CC {ECO:0000250|UniProtKB:P50481}.
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DR EMBL; AF063245; AAC99331.1; -; mRNA.
DR AlphaFoldDB; O97581; -.
DR SMR; O97581; -.
DR InParanoid; O97581; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA: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 2: Evidence at transcript level;
KW Activator; DNA-binding; Homeobox; LIM domain; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN <1..383
FT /note="LIM/homeobox protein Lhx3"
FT /id="PRO_0000075783"
FT DOMAIN 14..73
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 73..136
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DNA_BIND 142..201
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 197..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 48
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBR4"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBR4"
FT MOD_RES 212
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBR4"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBR4"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAC99331.1"
SQ SEQUENCE 383 AA; 41825 MW; 0331CC13D8DA0EA7 CRC64;
WEGRPQELGG KEIPLCAGCD QHILDRFILK ALDRHWHSKC LKCSDCHTPL AERCFSRGES
LYCKDDFFKR FGTKCAACQL GIPPTQVVRR AQDFVYHLHC FACVVCKRQL ATGDEFYLME
DSRLVCKADY ETAKQREAEA TAKRPRTTIT AKQLETLKSA YNTSPKPARH VREQLSSETG
LDMRVVQVWF QNRRAKEKRL KKDAGRQRWG QYFRNMKRAR GGSKSDKDSV QEEGQDSDAE
VSFTDEPSMA EMGPANGLYG GLGEPAPALG RPSGAPGSFP LEHGGLAGPE QYGELRPSSP
YGVPSSPAAL QSLPGPQPLL SSLVYPEAGL GLVPAGPPGG PPPMRVLAGN GPSSDLSTGS
SGGYPDFPAS PASWLDEVDH AQF
