TCEA2_RAT
ID TCEA2_RAT Reviewed; 299 AA.
AC Q63799;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Transcription elongation factor A protein 2;
DE AltName: Full=Protein S-II-T1;
DE AltName: Full=Testis-specific S-II;
DE AltName: Full=Transcription elongation factor S-II protein 2;
DE AltName: Full=Transcription elongation factor TFIIS.l;
GN Name=Tcea2; Synonyms=Siit1;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=8300645; DOI=10.1016/s0021-9258(17)42053-9;
RA Xu Q., Nakanishi T., Sekimizu K., Natori S.;
RT "Cloning and identification of testis-specific transcription elongation
RT factor S-II.";
RL J. Biol. Chem. 269:3100-3103(1994).
CC -!- FUNCTION: Necessary for efficient RNA polymerase II transcription
CC elongation past template-encoded arresting sites. The arresting sites
CC in DNA have the property of trapping a certain fraction of elongating
CC RNA polymerases that pass through, resulting in locked ternary
CC complexes. Cleavage of the nascent transcript by S-II allows the
CC resumption of elongation from the new 3'-terminus.
CC {ECO:0000269|PubMed:8300645}.
CC -!- SUBUNIT: Interacts with the basal transcription factor GTF2B. Interacts
CC with REXO1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Testis specific. {ECO:0000269|PubMed:8300645}.
CC -!- SIMILARITY: Belongs to the TFS-II family. {ECO:0000305}.
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DR EMBL; D12927; BAA02310.1; -; mRNA.
DR PIR; A53004; A53004.
DR RefSeq; NP_476439.1; NM_057098.1.
DR AlphaFoldDB; Q63799; -.
DR SMR; Q63799; -.
DR STRING; 10116.ENSRNOP00000022073; -.
DR PaxDb; Q63799; -.
DR PRIDE; Q63799; -.
DR GeneID; 29575; -.
DR KEGG; rno:29575; -.
DR UCSC; RGD:61825; rat.
DR CTD; 6919; -.
DR RGD; 61825; Tcea2.
DR VEuPathDB; HostDB:ENSRNOG00000016288; -.
DR eggNOG; KOG1105; Eukaryota.
DR HOGENOM; CLU_037637_2_0_1; -.
DR InParanoid; Q63799; -.
DR OMA; KMVTRKS; -.
DR OrthoDB; 1579101at2759; -.
DR PhylomeDB; Q63799; -.
DR PRO; PR:Q63799; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000016288; Expressed in testis and 20 other tissues.
DR Genevisible; Q63799; RN.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:RGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.472.30; -; 1.
DR Gene3D; 1.20.930.10; -; 1.
DR InterPro; IPR035100; TF_IIS-typ.
DR InterPro; IPR003617; TFIIS/CRSP70_N_sub.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR003618; TFIIS_cen_dom.
DR InterPro; IPR036575; TFIIS_cen_dom_sf.
DR InterPro; IPR017923; TFIIS_N.
DR InterPro; IPR006289; TFSII.
DR InterPro; IPR001222; Znf_TFIIS.
DR Pfam; PF08711; Med26; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR Pfam; PF07500; TFIIS_M; 1.
DR PIRSF; PIRSF006704; TF_IIS; 1.
DR SMART; SM00510; TFS2M; 1.
DR SMART; SM00509; TFS2N; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR SUPFAM; SSF46942; SSF46942; 1.
DR SUPFAM; SSF47676; SSF47676; 1.
DR TIGRFAMs; TIGR01385; TFSII; 1.
DR PROSITE; PS51321; TFIIS_CENTRAL; 1.
DR PROSITE; PS51319; TFIIS_N; 1.
DR PROSITE; PS00466; ZF_TFIIS_1; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..299
FT /note="Transcription elongation factor A protein 2"
FT /id="PRO_0000121451"
FT DOMAIN 5..82
FT /note="TFIIS N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00649"
FT DOMAIN 138..254
FT /note="TFIIS central"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00651"
FT ZN_FING 257..297
FT /note="TFIIS-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT REGION 82..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 289
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00472"
FT MOD_RES 59
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23193"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P23193"
FT CROSSLNK 57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q15560"
SQ SEQUENCE 299 AA; 33528 MW; 24BF8D56ECE3BB3F CRC64;
MGKEEEIARI ARRLDKMVTR KNAEGAMDLL RELKNMPITL HLLQSTRVGM SVNALRKQSS
DEELIALAKS LIKSWKKLLD VSDGKSRDQG RGTPLPTSSS KDASGTTDLS CKKPDPPRTS
STPRITTFPQ VPITCDAVRN KCREMLTLAL QTDHDHVAVG VSCEHLSSQI EECIFLDVGN
TDMKYKNRVR SRISNLKDAK NPGLRRNVLC GAITPQQIAV MTSEEMASDE LKEIRKAMTK
EAIREHQMAR TGGTQTDLFT CNKCRKKNCT YTQVQTRSSD EPMTTYVVCN ECGNRWKFC
