LDB1_CHICK
ID LDB1_CHICK Reviewed; 411 AA.
AC O42252; Q1EQX0; Q78CQ9; Q9PWE7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=LIM domain-binding protein 1;
DE Short=LDB-1;
DE AltName: Full=Carboxyl-terminal LIM domain-binding protein 2;
DE Short=CLIM-2;
DE AltName: Full=LIM domain-binding factor CLIM2;
DE Short=cLdb1;
DE AltName: Full=Neural Src-interacting protein;
DE AltName: Full=Nuclear LIM interactor;
GN Name=LDB1 {ECO:0000312|EMBL:BAE95403.1}; Synonyms=CLIM2, NSIP;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAB82581.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND C).
RC STRAIN=Brown leghorn {ECO:0000312|EMBL:AAB82581.1};
RC TISSUE=Neuroretina {ECO:0000312|EMBL:AAB82581.1};
RA Mikhailik A., Dezelee P., Calothy G.;
RT "Neural src interacting protein (NSIP).";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAD34208.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), AND TISSUE SPECIFICITY.
RC TISSUE=Limb {ECO:0000269|PubMed:10431247};
RX PubMed=10431247; DOI=10.1038/11970;
RA Bach I., Rodriguez-Esteban C., Carriere C., Bhushan A., Krones A.,
RA Rose D.W., Glass C.K., Andersen B., Izpisua-Belmonte J.-C., Rosenfeld M.G.;
RT "RLIM inhibits functional activity of LIM homeodomain transcription factors
RT via recruitment of the histone deacetylase complex.";
RL Nat. Genet. 22:394-399(1999).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAE95403.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), AND ALTERNATIVE SPLICING.
RC TISSUE=Fetus {ECO:0000269|PubMed:16815859};
RX PubMed=16815859; DOI=10.1093/jb/mvj134;
RA Tran Y.H., Xu Z., Kato A., Mistry A.C., Goya Y., Taira M., Brandt S.J.,
RA Hirose S.;
RT "Spliced isoforms of LIM-domain-binding protein (CLIM/NLI/Ldb) lacking the
RT LIM-interaction domain.";
RL J. Biochem. 140:105-119(2006).
CC -!- FUNCTION: Binds to the LIM domain of a wide variety of LIM domain-
CC containing transcription factors. {ECO:0000305}.
CC -!- SUBUNIT: Forms homodimers and heterodimers.
CC {ECO:0000250|UniProtKB:P70662}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=c {ECO:0000269|Ref.1};
CC IsoId=O42252-1; Sequence=Displayed;
CC Name=a {ECO:0000269|Ref.1};
CC IsoId=O42252-2; Sequence=VSP_052323;
CC Name=b {ECO:0000269|PubMed:16815859};
CC IsoId=O42252-3; Sequence=VSP_052323, VSP_052325, VSP_052326;
CC Name=d {ECO:0000269|PubMed:10431247};
CC IsoId=O42252-4; Sequence=VSP_052323, VSP_052324;
CC -!- TISSUE SPECIFICITY: First expressed at stages 15-16 in presumptive limb
CC mesoderm. As limb outgrowth proceeds, expressed in the entire limb bud,
CC concentrating in the distal mesoderm throughout limb development. Both
CC hindlimbs and forelimbs exhibit similar expression patterns.
CC {ECO:0000269|PubMed:10431247}.
CC -!- DOMAIN: The dimerization domain is located in the N-terminus.
CC {ECO:0000250|UniProtKB:P70662}.
CC -!- MISCELLANEOUS: [Isoform b]: Due to intron retention. Lacks LIM-binding
CC domain. {ECO:0000269|PubMed:16815859}.
CC -!- SIMILARITY: Belongs to the LDB family. {ECO:0000255}.
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DR EMBL; AF026037; AAB82581.1; -; mRNA.
DR EMBL; AF026038; AAB82582.1; -; mRNA.
DR EMBL; AF069991; AAD34208.1; -; mRNA.
DR EMBL; AB250385; BAE95403.1; -; mRNA.
DR RefSeq; NP_990401.1; NM_205070.1. [O42252-1]
DR RefSeq; XP_015144067.1; XM_015288581.1.
DR RefSeq; XP_015144068.1; XM_015288582.1. [O42252-2]
DR RefSeq; XP_015144069.1; XM_015288583.1. [O42252-2]
DR AlphaFoldDB; O42252; -.
DR SMR; O42252; -.
DR STRING; 9031.ENSGALP00000012348; -.
DR PaxDb; O42252; -.
DR Ensembl; ENSGALT00000012362; ENSGALP00000012348; ENSGALG00000007641. [O42252-1]
DR Ensembl; ENSGALT00000085289; ENSGALP00000061942; ENSGALG00000007641. [O42252-2]
DR GeneID; 395952; -.
DR KEGG; gga:395952; -.
DR CTD; 8861; -.
DR VEuPathDB; HostDB:geneid_395952; -.
DR eggNOG; KOG2181; Eukaryota.
DR GeneTree; ENSGT00390000005639; -.
DR InParanoid; O42252; -.
DR OMA; KMSVGCA; -.
DR OrthoDB; 849287at2759; -.
DR PhylomeDB; O42252; -.
DR Reactome; R-GGA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR PRO; PR:O42252; -.
DR Proteomes; UP000000539; Chromosome 6.
DR Bgee; ENSGALG00000007641; Expressed in ovary and 13 other tissues.
DR ExpressionAtlas; O42252; baseline.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; 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:0009948; P:anterior/posterior axis specification; ISS:UniProtKB.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
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:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0016055; P:Wnt signaling pathway; 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 Alternative splicing; Nucleus; Reference proteome.
FT CHAIN 1..411
FT /note="LIM domain-binding protein 1"
FT /id="PRO_0000284554"
FT DOMAIN 336..375
FT /note="LIM interaction domain (LID)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01302"
FT REGION 284..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform a, isoform b and isoform d)"
FT /evidence="ECO:0000303|PubMed:10431247,
FT ECO:0000303|PubMed:16815859, ECO:0000303|Ref.1"
FT /id="VSP_052323"
FT VAR_SEQ 334..335
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000303|PubMed:10431247"
FT /id="VSP_052324"
FT VAR_SEQ 336..359
FT /note="DVMVVGEPTLMGGEFGDEDERLIT -> VSIPFPFSLPSPGWRGGLPAPGIG
FT (in isoform b)"
FT /evidence="ECO:0000303|PubMed:16815859"
FT /id="VSP_052325"
FT VAR_SEQ 360..411
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000303|PubMed:16815859"
FT /id="VSP_052326"
FT CONFLICT 50
FT /note="P -> A (in Ref. 2; AAD34208)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="L -> F (in Ref. 3; BAE95403)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 411 AA; 46606 MW; 672F2125EA2683EA CRC64;
MSVGCACPGC SSKSFKLYSP KEPPNGNAFP PFHPGTMLDR DVGPTPMYPP TYLEPGIGRH
TPYGNQTDYR IFELNKRLQN WTEECDNLWW DAFTTEFFED DAMLTITFCL EDGPKRYTIG
RTLIPRYFRS IFEGGATELY YVLKHPKESF HNNFVSLDCD QCTMVTQHGK PMFTQVCVEG
RLYLEFMFDD MMRIKTWHFS IRQHRELIPR SILAMHAQDP QMLDQLSKNI TRCGLSNSTL
NYLRLCVILE PMQELMSRHK TYSLSPRDCL KTCLFQKWQR MVAPPAEPAR QQPSKRRKRK
MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF GDEDERLITR
LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES KSENPTSQAS Q
