ID   LDB1_XENTR              Reviewed;         373 AA.
AC   Q6NVL6;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=LIM domain-binding protein 1;
DE            Short=LDB-1;
GN   Name=ldb1 {ECO:0000312|EMBL:AAH67989.1};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1] {ECO:0000312|EMBL:AAH67989.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Gastrula {ECO:0000312|EMBL:AAH67989.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to the LIM domain of a wide variety of LIM domain-
CC       containing transcription factors. Acts as a coactivator together with
CC       otx2 to stimulate lhx1/lim1-mediated activation of the gsc promoter in
CC       the Spemann organizer. Acts synergistically with lhx1/lim1 and ssbp in
CC       axis formation (By similarity). {ECO:0000250|UniProtKB:P70060,
CC       ECO:0000305}.
CC   -!- SUBUNIT: Forms homodimers and heterodimers. Interacts with and
CC       activates lhx1/lim1. The stoichiometry of lhx1/lim1 and ldb1 is
CC       important for their function and an excess of ldb1 can inhibit
CC       lhx1/lim1 function. When bound to lhx1/lim1, escapes degradation by
CC       rnf12. Interacts with the N-terminal region of rnf12 (By similarity).
CC       {ECO:0000250|UniProtKB:P70060}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- DOMAIN: The dimerization domain is located in the N-terminus.
CC       {ECO:0000250|UniProtKB:P70662}.
CC   -!- PTM: Undergoes rnf12-mediated ubiquitin-proteasome-dependent
CC       degradation. {ECO:0000250|UniProtKB:P70060}.
CC   -!- SIMILARITY: Belongs to the LDB family. {ECO:0000255}.
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DR   EMBL; BC067989; AAH67989.1; -; mRNA.
DR   RefSeq; NP_998843.1; NM_213678.1.
DR   AlphaFoldDB; Q6NVL6; -.
DR   SMR; Q6NVL6; -.
DR   PaxDb; Q6NVL6; -.
DR   DNASU; 407886; -.
DR   GeneID; 407886; -.
DR   KEGG; xtr:407886; -.
DR   CTD; 8861; -.
DR   Xenbase; XB-GENE-493239; ldb1.
DR   eggNOG; KOG2181; Eukaryota.
DR   HOGENOM; CLU_032597_0_0_1; -.
DR   InParanoid; Q6NVL6; -.
DR   OrthoDB; 849287at2759; -.
DR   Reactome; R-XTR-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Proteomes; UP000008143; Chromosome 7.
DR   Proteomes; UP000790000; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0030274; F:LIM domain binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   InterPro; IPR030167; LDB1.
DR   InterPro; IPR041363; LID.
DR   InterPro; IPR029005; LIM-bd/SEUSS.
DR   PANTHER; PTHR10378; PTHR10378; 1.
DR   PANTHER; PTHR10378:SF7; PTHR10378:SF7; 1.
DR   Pfam; PF17916; LID; 1.
DR   Pfam; PF01803; LIM_bind; 2.
DR   PROSITE; PS51957; LID; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Nucleus; Reference proteome.
FT   CHAIN           1..373
FT                   /note="LIM domain-binding protein 1"
FT                   /id="PRO_0000284555"
FT   DOMAIN          298..337
FT                   /note="LIM interaction domain (LID)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01302"
FT   REGION          248..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          329..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   373 AA;  42656 MW;  4E1A8420B20FA446 CRC64;
     MLDRDVGPTP MYPPTYLEPG IGRHTPYGNQ TDYRIFELNK RLQNWTEECD NLWWDAFTTE
     FFEDDAMLTI TFCLEDGPKR YTIGRTLIPR YFRSIFEGGA TELYYVLKHP KESFHNNFVS
     LDCDQCTMVT QHGKPMFTQV CVEGRLYLEF MFDDMMRIKT WHFSIRQHRE LIPRSILAMH
     AQDPQMLDQL SKNITRCGLS NSTLNYLRLC VILEPMQELM SRHKTYSLSP RDCLKTCLFQ
     KWQRMVAPPA EPARQAPNKR RKRKMSGGST MSSGGGNTNN SNSKKKSPAS TFALSSQDVM
     VVGEPTLMGG EFGDEDERLI TRLENTQFDA ANGIDDEDSF NNSPALGANS PWNSKPPSSQ
     ESKSENPTSQ ASQ