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LIN32_CAEEL
ID   LIN32_CAEEL             Reviewed;         142 AA.
AC   Q10574;
DT   02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Protein lin-32;
DE   AltName: Full=Abnormal cell lineage protein 32;
GN   Name=lin-32 {ECO:0000312|WormBase:T14F9.5};
GN   Synonyms=hlh-7 {ECO:0000312|WormBase:T14F9.5};
GN   ORFNames=T14F9.5 {ECO:0000312|WormBase:T14F9.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF GLU-81 AND LEU-95.
RC   STRAIN=Bristol N2;
RX   PubMed=7800042; DOI=10.1038/373074a0;
RA   Zhao C., Emmons S.W.;
RT   "A transcription factor controlling development of peripheral sense organs
RT   in C. elegans.";
RL   Nature 373:74-78(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, INTERACTION WITH HLH-2, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP   GLU-81 AND LEU-95.
RX   PubMed=11076762; DOI=10.1242/dev.127.24.5415;
RA   Portman D.S., Emmons S.W.;
RT   "The basic helix-loop-helix transcription factors LIN-32 and HLH-2 function
RT   together in multiple steps of a C. elegans neuronal sublineage.";
RL   Development 127:5415-5426(2000).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=31386623; DOI=10.7554/elife.46703;
RA   Lee J., Taylor C.A., Barnes K.M., Shen A., Stewart E.V., Chen A.,
RA   Xiang Y.K., Bao Z., Shen K.;
RT   "A Myt1 family transcription factor defines neuronal fate by repressing
RT   non-neuronal genes.";
RL   Elife 8:0-0(2019).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=32665354; DOI=10.1534/g3.120.401547;
RA   Zhang A., Noma K., Yan D.;
RT   "Regulation of Gliogenesis by lin-32/Atoh1 in Caenorhabditis elegans.";
RL   G3 (Bethesda) 10:3271-3278(2020).
CC   -!- FUNCTION: Probable transcription factor which binds the E box motif 5'-
CC       CA[TC][AG]TG-3' (PubMed:11076762). Essential for the specification of
CC       the neuroblast cell fate in the development of peripheral sense organs
CC       (PubMed:7800042). Its role in the generation of sensory neurons may be
CC       through positively regulating the expression of the zinc finger protein
CC       ztf-11 during postdeirid neurogenesis (PubMed:31386623). Required for
CC       specification of cell fate, acting in concert with lin-32, in the
CC       development of the male-specific genital sensilla (simple sense organs)
CC       known as rays (PubMed:11076762). Involved in regulating glial
CC       specification, perhaps by suppressing a glial fate in different
CC       lineages during early embryogenesis (PubMed:32665354).
CC       {ECO:0000269|PubMed:11076762, ECO:0000269|PubMed:31386623,
CC       ECO:0000269|PubMed:32665354, ECO:0000269|PubMed:7800042}.
CC   -!- SUBUNIT: Forms a heterodimer with hlh-2. {ECO:0000269|PubMed:11076762}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31386623,
CC       ECO:0000269|PubMed:7800042}.
CC   -!- TISSUE SPECIFICITY: Expressed in PVD motor neurons.
CC       {ECO:0000269|PubMed:31386623}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in V5 postdeirid lineage cells in L2
CC       larvae (PubMed:31386623). Expressed in the nine ray lineage Rn.a
CC       neuroblasts and their progeny, Rn.aa and Rn.ap (PubMed:11076762).
CC       {ECO:0000269|PubMed:11076762, ECO:0000269|PubMed:31386623}.
CC   -!- DISRUPTION PHENOTYPE: Knockout results in ectopic AMsh glial cells and
CC       also ectopic amphid socket (AMso) cells, another type of glia, from a
CC       different cell lineage (PubMed:32665354). Some animals are missing
CC       dorsal, but not ventral, CEPsh glial cells (PubMed:32665354). Mean
CC       number of ectopic AMsh glial cells increases on cnd-1 or ngn-1 mutant
CC       backgrounds (PubMed:32665354). {ECO:0000269|PubMed:32665354}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA67360.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; U15418; AAA67360.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BX284606; CCD68944.1; -; Genomic_DNA.
DR   PIR; T29378; T29378.
DR   RefSeq; NP_508410.2; NM_076009.2.
DR   AlphaFoldDB; Q10574; -.
DR   SMR; Q10574; -.
DR   BioGRID; 56200; 2.
DR   IntAct; Q10574; 2.
DR   STRING; 6239.T14F9.5; -.
DR   PaxDb; Q10574; -.
DR   EnsemblMetazoa; T14F9.5.1; T14F9.5.1; WBGene00003018.
DR   GeneID; 191703; -.
DR   KEGG; cel:CELE_T14F9.5; -.
DR   UCSC; T14F9.5; c. elegans.
DR   CTD; 191703; -.
DR   WormBase; T14F9.5; CE33318; WBGene00003018; lin-32.
DR   eggNOG; KOG4395; Eukaryota.
DR   GeneTree; ENSGT00940000168200; -.
DR   HOGENOM; CLU_1798134_0_0_1; -.
DR   InParanoid; Q10574; -.
DR   OMA; KKKCRRY; -.
DR   OrthoDB; 1642317at2759; -.
DR   PRO; PR:Q10574; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00003018; Expressed in embryo and 3 other tissues.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:WormBase.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:WormBase.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
DR   GO; GO:0007568; P:aging; IMP:UniProtKB.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR   GO; GO:0003398; P:glial cell differentiation involved in amphid sensory organ development; IMP:UniProtKB.
DR   GO; GO:0021780; P:glial cell fate specification; IMP:UniProtKB.
DR   GO; GO:0051179; P:localization; IMP:WormBase.
DR   GO; GO:0014014; P:negative regulation of gliogenesis; IMP:UniProtKB.
DR   GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR   GO; GO:0048666; P:neuron development; IMP:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR   GO; GO:0048665; P:neuron fate specification; IMP:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; DNA-binding; Neurogenesis; Nucleus;
KW   Reference proteome.
FT   CHAIN           1..142
FT                   /note="Protein lin-32"
FT                   /id="PRO_0000127261"
FT   DOMAIN          72..124
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          30..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         81
FT                   /note="E->K: In u282; 99% loss of the male-specific genital
FT                   sensilla (simple sense organs) known as rays, and tail
FT                   touch insensitivity."
FT                   /evidence="ECO:0000269|PubMed:11076762,
FT                   ECO:0000269|PubMed:7800042"
FT   MUTAGEN         95
FT                   /note="L->F: In e1926; aberrant development of all three
FT                   cell types forming the male-specific genital sensilla
FT                   (simple sense organs) known as rays. 81% ray loss. Ray loss
FT                   phenotype exacerbated on hlh-2 mutant background.
FT                   Drastically reduces binding to DNA as a heterodimer with
FT                   hlh-2."
FT                   /evidence="ECO:0000269|PubMed:11076762,
FT                   ECO:0000269|PubMed:7800042"
SQ   SEQUENCE   142 AA;  16480 MW;  DA20245666C65E8D CRC64;
     MSWEQYQMYV PQCHPSFMYQ GSIQSTMTTP LQSPNFSLDS PNYPDSLSNG GGKDDKKKCR
     RYKTPSPQLL RMRRSAANER ERRRMNTLNV AYDELREVLP EIDSGKKLSK FETLQMAQKY
     IECLSQILKQ DSKNENLKSK SG
 
 
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