SP30L_DANRE
ID SP30L_DANRE Reviewed; 178 AA.
AC Q6NYV5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Histone deacetylase complex subunit SAP30L;
DE AltName: Full=Sin3 corepressor complex subunit SAP30L;
DE AltName: Full=Sin3-associated protein p30-like;
GN Name=sap30l;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=22821512; DOI=10.1002/jcb.24298;
RA Teittinen K.J., Groenroos T., Parikka M., Junttila S., Uusimaeki A.,
RA Laiho A., Korkeamaeki H., Kurppa K., Turpeinen H., Pesu M., Gyenesei A.,
RA Raemet M., Lohi O.;
RT "SAP30L (Sin3A-associated protein 30-like) is involved in regulation of
RT cardiac development and hematopoiesis in zebrafish embryos.";
RL J. Cell. Biochem. 113:3843-3852(2012).
CC -!- FUNCTION: Functions as transcription repressor, probably via its
CC interaction with histone deacetylase complexes (PubMed:22821512).
CC Required for normal expression of numerous target genes
CC (PubMed:22821512). Involved in the functional recruitment of the class
CC 1 Sin3-histone deacetylase complex (HDAC) to the nucleolus. Binds DNA,
CC apparently without sequence-specificity, and bends bound double-
CC stranded DNA. Binds phosphoinositol phosphates (phosphoinositol 3-
CC phosphate, phosphoinositol 4-phosphate and phosphoinositol 5-phosphate)
CC via the same basic sequence motif that mediates DNA binding and nuclear
CC import (By similarity). {ECO:0000250|UniProtKB:Q9HAJ7,
CC ECO:0000269|PubMed:22821512}.
CC -!- SUBUNIT: Interacts with components of the histone deacetylase complex
CC sin3a, hdac1 and hdac2. Binds histones and nucleosomes.
CC {ECO:0000250|UniProtKB:Q9HAJ7}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q9HAJ7}.
CC -!- TISSUE SPECIFICITY: Detected in embryos at 2dpf (at protein level).
CC Widely expressed during embryogenesis and in adults.
CC {ECO:0000269|PubMed:22821512}.
CC -!- DOMAIN: The zinc-finger domain mediates direct interaction with DNA and
CC phosphoinositol phosphates (phosphoinositol 3-phosphate,
CC phosphoinositol 4-phosphate and phosphoinositol 5-phosphate). In vitro
CC oxydation causes reversible disulfide bond formation between Cys
CC residues in the zinc-finger domain and reversible loss of zinc ion
CC binding. {ECO:0000250|UniProtKB:Q9HAJ7}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown causes defects in embryonic
CC heart morphogenesis and pericardiac edema, with defects in heart
CC function that are visible already at 3 dpf. In addition, erythrocytes
CC appear pale due to decreased hemoglobin content.
CC {ECO:0000269|PubMed:22821512}.
CC -!- SIMILARITY: Belongs to the SAP30 family. {ECO:0000305}.
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DR EMBL; BC066447; AAH66447.1; -; mRNA.
DR RefSeq; NP_999868.1; NM_214703.1.
DR AlphaFoldDB; Q6NYV5; -.
DR SMR; Q6NYV5; -.
DR STRING; 7955.ENSDARP00000028875; -.
DR PaxDb; Q6NYV5; -.
DR PRIDE; Q6NYV5; -.
DR Ensembl; ENSDART00000029763; ENSDARP00000028875; ENSDARG00000030213.
DR GeneID; 327079; -.
DR KEGG; dre:327079; -.
DR CTD; 79685; -.
DR ZFIN; ZDB-GENE-030131-5287; sap30l.
DR eggNOG; ENOG502QWFH; Eukaryota.
DR GeneTree; ENSGT00390000006633; -.
DR HOGENOM; CLU_097961_1_0_1; -.
DR InParanoid; Q6NYV5; -.
DR OMA; QCARTKR; -.
DR OrthoDB; 1520155at2759; -.
DR PhylomeDB; Q6NYV5; -.
DR TreeFam; TF324135; -.
DR Reactome; R-DRE-3214815; HDACs deacetylate histones.
DR PRO; PR:Q6NYV5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 21.
DR Bgee; ENSDARG00000030213; Expressed in muscle tissue and 36 other tissues.
DR GO; GO:0000118; C:histone deacetylase complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0044378; F:non-sequence-specific DNA binding, bending; ISS:UniProtKB.
DR GO; GO:0031491; F:nucleosome binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; ISS:UniProtKB.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; ISS:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0001947; P:heart looping; IMP:ZFIN.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 6.10.160.20; -; 1.
DR InterPro; IPR024145; His_deAcase_SAP30/SAP30L.
DR InterPro; IPR038291; SAP30_C_sf.
DR InterPro; IPR025718; SAP30_Sin3-bd.
DR InterPro; IPR025717; SAP30_zn-finger.
DR PANTHER; PTHR13286; PTHR13286; 1.
DR Pfam; PF13867; SAP30_Sin3_bdg; 1.
DR Pfam; PF13866; zf-SAP30; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; DNA-binding; Lipid-binding; Metal-binding; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..178
FT /note="Histone deacetylase complex subunit SAP30L"
FT /id="PRO_0000309502"
FT ZN_FING 24..72
FT /note="Atypical"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..85
FT /note="Important for DNA and phosphoinositide binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HAJ7"
FT MOTIF 81..86
FT /note="Nuclear localization signal (NLS)"
FT /evidence="ECO:0000250|UniProtKB:Q9HAJ7"
FT COMPBIAS 82..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 24..25
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 33..69
FT /note="Redox-active"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 178 AA; 20589 MW; B8D77CD68E98FA13 CRC64;
MNGFSTEEDS HDGPPAPPFF GQSCCLIEDA ERCGRPAGNA SFSKRIQKSI SQRKLKLDID
KSVRHLYICD FHKNFIQSVR NKRKRKTSDD GGESPDHEVE VPEVDLFQLQ VNTLRRYKRH
YKIQTRPGLN KAQLAETVSR HFRNIPVNEK ETLTYFIYMV KSSKSRLDQK SDSSKQVE
