PAF1_DANRE
ID PAF1_DANRE Reviewed; 503 AA.
AC Q4U0S5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=RNA polymerase II-associated factor 1 homolog;
DE AltName: Full=PD2-like protein;
GN Name=paf1; Synonyms=paf1l;
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 [MRNA].
RA Amsterdam A., Hopkins N.;
RT "Danio rerio PD2-like mRNA.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTR9.
RX PubMed=21338598; DOI=10.1016/j.ydbio.2011.02.011;
RA Langenbacher A.D., Nguyen C.T., Cavanaugh A.M., Huang J., Lu F., Chen J.N.;
RT "The PAF1 complex differentially regulates cardiomyocyte specification.";
RL Dev. Biol. 353:19-28(2011).
CC -!- FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple
CC functions during transcription by RNA polymerase II. PAF1C associates
CC with RNA polymerase II, is involved in transcriptional elongation and
CC in histone modifications including methylation on histone H3 'Lys-4'
CC (H3K4me3) (By similarity). PAF1C seems to be required for multiple
CC steps in cardiac formation. Involved in the migration of myocardial
CC precursors to the midline and the differentiation of the
CC atrioventricular boundary in the developing heart. {ECO:0000250,
CC ECO:0000269|PubMed:21338598}.
CC -!- SUBUNIT: Component of the PAF1 complex, which at least consists of
CC cdc73, paf1, leo1, ctr9 and rtf1 (By similarity). The PAF1 complex
CC interacts with PHF5A (By similarity). Interacts with ctr9
CC (PubMed:21338598). {ECO:0000250|UniProtKB:Q8K2T8,
CC ECO:0000250|UniProtKB:Q8N7H5, ECO:0000269|PubMed:21338598}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21338598}.
CC -!- SIMILARITY: Belongs to the PAF1 family. {ECO:0000305}.
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DR EMBL; DQ022213; AAY44602.1; -; mRNA.
DR EMBL; BC139613; AAI39614.1; -; mRNA.
DR RefSeq; NP_001019624.1; NM_001024453.1.
DR AlphaFoldDB; Q4U0S5; -.
DR SMR; Q4U0S5; -.
DR IntAct; Q4U0S5; 1.
DR STRING; 7955.ENSDARP00000064443; -.
DR GeneID; 553020; -.
DR KEGG; dre:553020; -.
DR CTD; 54623; -.
DR ZFIN; ZDB-GENE-050506-101; paf1.
DR eggNOG; KOG2478; Eukaryota.
DR InParanoid; Q4U0S5; -.
DR OrthoDB; 599989at2759; -.
DR PhylomeDB; Q4U0S5; -.
DR Reactome; R-DRE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DRE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-DRE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR PRO; PR:Q4U0S5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IDA:ZFIN.
DR GO; GO:0005634; C:nucleus; IDA:ZFIN.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0000993; F:RNA polymerase II complex binding; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; IMP:UniProtKB.
DR GO; GO:0016570; P:histone modification; IEA:InterPro.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:UniProtKB.
DR InterPro; IPR007133; RNA_pol_II-assoc_Paf1.
DR PANTHER; PTHR23188; PTHR23188; 1.
DR Pfam; PF03985; Paf1; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..503
FT /note="RNA polymerase II-associated factor 1 homolog"
FT /id="PRO_0000326404"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 352..381
FT /evidence="ECO:0000255"
FT COMPBIAS 360..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..428
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..472
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 58216 MW; B8EE86A45B9D9DEE CRC64;
MAPTIQTQAQ REDGHRSSAH RTVPERSGVV CRVKYGNSLP DIPFDPKFIT YPFDQHRFVQ
YKATSLEKQH KHELLTEPDL GVTIDLINPD TYRIDPNILL DPADEKLLEE EIQAPSSSKR
SQQHAKVVPW MRKTEYISTE FNRYGVSNEK VEVKIGVSVK QQFTEEEIYK DRDSQIAAIE
KTFEDAQKSI SQHYSKPRVT PVEVLPVFPD FKMWINPCAQ VIFDSDPAPK DVSAPAGVDM
MSQAMIRGMM DEEGNQFVAY FLPNEDTMRK RKRDVEEELD YMPEEVYEYK IAREYNWNVK
NKASKGYEEN YFFIFRDADG VYYNELETRV RLSKRRAKVG AQSSTNAVLV CKHRDMNEKE
LEAQEARKAQ LENHEPEDEE EELDLEKDMQ EDSGEEREKP SDSENSESES EREEEERPAD
EDEEEEEDEE SVKRRRERKS SGSESGDDRQ ARDEEEIFGS DDDSEEEEEE EEEGGARRRS
NSSSVQHSAS ERASDSSDAS DSD
