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LDB1A_DANRE
ID   LDB1A_DANRE             Reviewed;         374 AA.
AC   O73715; Q1EQX3; Q4V929; Q5XFY5;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=LIM domain-binding protein 1-A;
DE            Short=LDB-1-A;
DE   AltName: Full=LIM domain-binding protein 4;
DE            Short=LDB-4;
DE            Short=zLdb4;
GN   Name=ldb1a; Synonyms=ldb4;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAC15798.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND TISSUE SPECIFICITY.
RX   PubMed=9507128; DOI=10.1016/s0925-4773(97)00202-5;
RA   Toyama R., Kobayashi M., Tomita T., Dawid I.B.;
RT   "Expression of LIM-domain binding protein (ldb) genes during zebrafish
RT   embryogenesis.";
RL   Mech. Dev. 71:197-200(1998).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAE95400.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), SUBCELLULAR LOCATION, ALTERNATIVE
RP   SPLICING, AND TISSUE SPECIFICITY.
RC   TISSUE=Gill {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).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAH84686.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND D).
RC   TISSUE=Olfactory epithelium {ECO:0000312|EMBL:AAH97093.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Binds to the LIM domain of a wide variety of LIM domain-
CC       containing transcription factors. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16815859}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=a {ECO:0000269|PubMed:9507128};
CC         IsoId=O73715-1; Sequence=Displayed;
CC       Name=b {ECO:0000269|PubMed:16815859};
CC         IsoId=O73715-2; Sequence=VSP_052332, VSP_052333;
CC       Name=c;
CC         IsoId=O73715-3; Sequence=VSP_052330, VSP_052332, VSP_052333;
CC       Name=d;
CC         IsoId=O73715-4; Sequence=VSP_052331, VSP_052332, VSP_052333;
CC   -!- TISSUE SPECIFICITY: Expressed ubiquitously in the embryo and adult.
CC       {ECO:0000269|PubMed:16815859, ECO:0000269|PubMed:9507128}.
CC   -!- MISCELLANEOUS: [Isoform b]: Lacks LIM-binding domain.
CC       {ECO:0000269|PubMed:16815859}.
CC   -!- MISCELLANEOUS: [Isoform c]: Lacks LIM-binding domain.
CC       {ECO:0000269|PubMed:16815859, ECO:0000305}.
CC   -!- MISCELLANEOUS: [Isoform d]: Lacks LIM-binding domain.
CC       {ECO:0000269|PubMed:16815859, ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the LDB family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH84686.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF031378; AAC15798.1; -; mRNA.
DR   EMBL; AB250382; BAE95400.1; -; mRNA.
DR   EMBL; BC084686; AAH84686.1; ALT_INIT; mRNA.
DR   EMBL; BC097093; AAH97093.1; -; mRNA.
DR   RefSeq; NP_571391.1; NM_131316.1. [O73715-1]
DR   AlphaFoldDB; O73715; -.
DR   SMR; O73715; -.
DR   STRING; 7955.ENSDARP00000107739; -.
DR   PaxDb; O73715; -.
DR   Ensembl; ENSDART00000015773; ENSDARP00000003158; ENSDARG00000010137. [O73715-1]
DR   Ensembl; ENSDART00000150376; ENSDARP00000125601; ENSDARG00000010137. [O73715-2]
DR   GeneID; 30579; -.
DR   KEGG; dre:30579; -.
DR   CTD; 30579; -.
DR   ZFIN; ZDB-GENE-990415-138; ldb1a.
DR   eggNOG; KOG2181; Eukaryota.
DR   GeneTree; ENSGT00390000005639; -.
DR   HOGENOM; CLU_032597_0_0_1; -.
DR   InParanoid; O73715; -.
DR   OMA; CPRPTPM; -.
DR   OrthoDB; 849287at2759; -.
DR   PhylomeDB; O73715; -.
DR   Reactome; R-DRE-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   PRO; PR:O73715; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   Bgee; ENSDARG00000010137; Expressed in retina and 25 other tissues.
DR   ExpressionAtlas; O73715; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0030274; F:LIM domain binding; IDA:ZFIN.
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; IBA:GO_Central.
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; 1.
DR   PROSITE; PS51957; LID; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Nucleus; Reference proteome.
FT   CHAIN           1..374
FT                   /note="LIM domain-binding protein 1-A"
FT                   /id="PRO_0000284774"
FT   DOMAIN          299..338
FT                   /note="LIM interaction domain (LID)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01302"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          322..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..297
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1
FT                   /note="M -> MHQNAAGCACRPVCTYCCSSKSFKLYSPKEPPNGSAFPPFHPGAM
FT                   (in isoform c)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_052330"
FT   VAR_SEQ         298
FT                   /note="Q -> QVP (in isoform d)"
FT                   /evidence="ECO:0000303|Ref.3"
FT                   /id="VSP_052331"
FT   VAR_SEQ         299..315
FT                   /note="DVMVVGEPTLMGGEFGD -> DLVGTKTCTVPELEDRS (in isoform
FT                   b, isoform c and isoform d)"
FT                   /evidence="ECO:0000303|PubMed:16815859, ECO:0000303|Ref.3"
FT                   /id="VSP_052332"
FT   VAR_SEQ         316..374
FT                   /note="Missing (in isoform b, isoform c and isoform d)"
FT                   /evidence="ECO:0000303|PubMed:16815859, ECO:0000303|Ref.3"
FT                   /id="VSP_052333"
FT   CONFLICT        48
FT                   /note="Missing (in Ref. 3; AAH84686)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        240
FT                   /note="F -> V (in Ref. 3; AAH97093)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   374 AA;  42715 MW;  BF955A2764C579A8 CRC64;
     MLDRDVGPTP MYPPSYMEPG IGRHTPYGNQ TDYRIFELNK RLQNWTEQDC DNLWWDAFTT
     EFFEDDAMLT ITFCLEDGPK RYTIGRTLIP RYFRSIFEGG ATELFYVLKH PKESFHNNFV
     SLDCDQCTMV TQNGKPMFTQ VCVEGRLYLE FMFDDMMRIK TWHFSIRQHR EVVPRSILAM
     HAQDPQMLDQ LSKNITRCGL SNSTLNYLRL CVILEPMQEL MSRHKTYSLS PRDCLKTCLF
     QKWQRMVAPP AEPARQAPNK RRKRKMSGGS TMSSGGGNNN NSNSKKKSPA SSFALSSQDV
     MVVGEPTLMG GEFGDEDERL ITRLENTQFD AANGIDDEDS FNSSPTMGTN SPWNSKAPSS
     QQGKNDNPSS QSSQ
 
 
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