ELOA1_RAT
ID ELOA1_RAT Reviewed; 773 AA.
AC Q63187;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Elongin-A;
DE Short=EloA;
DE AltName: Full=Elongin 110 kDa subunit;
DE AltName: Full=RNA polymerase II transcription factor SIII subunit A1;
DE AltName: Full=SIII p110;
DE AltName: Full=Transcription elongation factor B polypeptide 3;
GN Name=Eloa; Synonyms=Tceb3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7660129; DOI=10.1126/science.7660129;
RA Aso T., Lane W.S., Conaway J.W., Conaway R.C.;
RT "Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase
RT II.";
RL Science 269:1439-1443(1995).
RN [2]
RP FUNCTION, AND SUBUNIT.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8244996; DOI=10.1016/s0021-9258(19)74431-7;
RA Bradsher J.N., Jackson K.W., Conaway R.C., Conaway J.W.;
RT "RNA polymerase II transcription factor SIII. I. Identification,
RT purification, and properties.";
RL J. Biol. Chem. 268:25587-25593(1993).
RN [3]
RP FUNCTION, ACTIVATION DOMAIN, INTERACTION WITH ELONGIN BC COMPLEX, AND
RP MUTAGENESIS OF THR-549; LEU-550 AND CYS-554.
RX PubMed=8896449; DOI=10.1002/j.1460-2075.1996.tb00940.x;
RA Aso T., Haque D., Barstead R.J., Conaway R.C., Conaway J.W.;
RT "The inducible elongin A elongation activation domain: structure, function
RT and interaction with the elongin BC complex.";
RL EMBO J. 15:5557-5566(1996).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP INTERACTION WITH ERCC6 AND CUL5.
RX PubMed=28292928; DOI=10.1074/jbc.c117.777946;
RA Weems J.C., Slaughter B.D., Unruh J.R., Boeing S., Hall S.M., McLaird M.B.,
RA Yasukawa T., Aso T., Svejstrup J.Q., Conaway J.W., Conaway R.C.;
RT "Cockayne syndrome B protein regulates recruitment of the Elongin A
RT ubiquitin ligase to sites of DNA damage.";
RL J. Biol. Chem. 292:6431-6437(2017).
CC -!- FUNCTION: SIII, also known as elongin, is a general transcription
CC elongation factor that increases the RNA polymerase II transcription
CC elongation past template-encoded arresting sites. Subunit A is
CC transcriptionally active and its transcription activity is strongly
CC enhanced by binding to the dimeric complex of the SIII regulatory
CC subunits B and C (elongin BC complex). {ECO:0000269|PubMed:8244996,
CC ECO:0000269|PubMed:8896449}.
CC -!- SUBUNIT: Heterotrimer of an A (ELOA, ELOA2 or ELOA3P), ELOB and ELOC
CC subunit (PubMed:8244996, PubMed:8896449). Interacts with ERCC6; the
CC interaction is induced by DNA damaging agents or inhibitors of RNA
CC polymerase II elongation (PubMed:28292928). Interacts (via BC-box) with
CC CUL5 (PubMed:28292928). {ECO:0000269|PubMed:28292928,
CC ECO:0000269|PubMed:8244996}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}.
CC -!- DOMAIN: The BC-box, which mediates binding to the elongin BC complex,
CC has the consensus sequence [APST]-L-x(3)-C-x(3)-[AILV].
CC {ECO:0000269|PubMed:8896449}.
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DR EMBL; L46816; AAA82095.1; -; mRNA.
DR PIR; A57244; A57244.
DR AlphaFoldDB; Q63187; -.
DR SMR; Q63187; -.
DR CORUM; Q63187; -.
DR IntAct; Q63187; 5.
DR MINT; Q63187; -.
DR STRING; 10116.ENSRNOP00000059109; -.
DR iPTMnet; Q63187; -.
DR PhosphoSitePlus; Q63187; -.
DR PaxDb; Q63187; -.
DR PRIDE; Q63187; -.
DR UCSC; RGD:3827; rat.
DR RGD; 3827; Eloa.
DR eggNOG; KOG2821; Eukaryota.
DR InParanoid; Q63187; -.
DR PhylomeDB; Q63187; -.
DR Reactome; R-RNO-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-RNO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-RNO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-RNO-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:Q63187; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070449; C:elongin complex; ISO:RGD.
DR GO; GO:0005634; C:nucleus; TAS:RGD.
DR GO; GO:0090734; C:site of DNA damage; IDA:UniProtKB.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; TAS:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; ISO:RGD.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR010684; RNA_pol_II_trans_fac_SIII_A.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR Pfam; PF06881; Elongin_A; 1.
DR Pfam; PF08711; Med26; 1.
DR SMART; SM00509; TFS2N; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR PROSITE; PS50181; FBOX; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
PE 1: Evidence at protein level;
KW Acetylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..773
FT /note="Elongin-A"
FT /id="PRO_0000086962"
FT DOMAIN 4..79
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT DOMAIN 565..609
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT REGION 79..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 521..680
FT /note="Activation domain"
FT /evidence="ECO:0000269|PubMed:8896449"
FT REGION 549..558
FT /note="BC-box"
FT /evidence="ECO:0000269|PubMed:8896449"
FT REGION 671..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..342
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8CB77"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14241"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14241"
FT MOD_RES 430
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8CB77"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14241"
FT MUTAGEN 549
FT /note="T->I: Reduces transcription activity."
FT /evidence="ECO:0000269|PubMed:8896449"
FT MUTAGEN 550
FT /note="L->S: Reduces transcription activity and abolishes
FT heterotrimeric formation."
FT /evidence="ECO:0000269|PubMed:8896449"
FT MUTAGEN 554
FT /note="C->F: Reduces transcription activity."
FT /evidence="ECO:0000269|PubMed:8896449"
SQ SEQUENCE 773 AA; 87203 MW; AEEE76E6953165AD CRC64;
MAAESALQVV EKLQARLAAN PDPKKLLKYL KKLSVLPITV DILVETGVGK TVNSFRKHEQ
VGNFARDLVA QWKKLVPVER NNEAEDQDFE KSNSRKRPRD VPQQEEEAEG NYQESWQASG
SQPYSPEHRQ KKHRKLPELE RPHKVAHGHE RRDERKRCHK VSPPYSSDPE SSDYGHVQSP
PPSSPHQMYT DLSRSPEMDQ EPIVSHPKPG KVHSNTFQDR LGVSHLGEHQ GKGAVSQNKP
HKSSHKEKRP VDARGDEKSS VMGREKSHKA SSKEESRRLL SEDSAKEKLP SSVVKKEKDR
EGNSLKKKLS PALDVASDNH FKKPKHKDSE KIKSDKNKQS VDSVDSGRGT GDPLPRAKDK
VPNNLKAQEG KVRTNSDRKS PGSLPKVEEM DMDDEFEQPT MSFESYLSYD QPRKKKKKVV
KTSGTALGEK GLKKKDSKST SKNLNSAQKL PKANENKSDK LQPAGAEPTR PRKVPTDVLP
ALPDIPLPAI QTNYRPLPSL ELISSFQPKR KAFSSPQEEE EAGFTGRRMN SKMQVYSGSK
CAYLPKMMTL HQQCIRVLKN NIDSIFEVGG VPYSVLEPVL ERCTPDQLYR IEECNHVLIE
ETDQLWKVHC HRDFKEERPE EYESWREMYL RLQDAREQRL RLLTNNIRSA HANKPKGRQA
KMAFVNSVAK PPRDVRRRQE KFGTGGAAVP EKVRIKPAPY TTGSSHVPAS NSSSSFHSSP
EELAYEGPST SSAHLAPVAS SSVSYDPRKP AVKKIAPMMA KTIKAFKNRF SRR
