THOC1_RAT
ID THOC1_RAT Reviewed; 343 AA.
AC P59924;
DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=THO complex subunit 1;
DE Short=Tho1;
DE AltName: Full=Liver regeneration-related protein LRRG175;
DE AltName: Full=Nuclear matrix protein p84;
GN Name=Thoc1; ORFNames=Da2-19;
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 [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L.,
RA Wang S.F., Han H.P., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J., Shi J.B.,
RA Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for efficient export of polyadenylated RNA. Acts as
CC component of the THO subcomplex of the TREX complex which is thought to
CC couple mRNA transcription, processing and nuclear export, and which
CC specifically associates with spliced mRNA and not with unspliced pre-
CC mRNA. TREX is recruited to spliced mRNAs by a transcription-independent
CC mechanism, binds to mRNA upstream of the exon-junction complex (EJC)
CC and is recruited in a splicing- and cap-dependent manner to a region
CC near the 5' end of the mRNA where it functions in mRNA export to the
CC cytoplasm via the TAP/NFX1 pathway. Regulates transcriptional
CC elongation of a subset of genes. Involved in genome stability by
CC preventing co-transcriptional R-loop formation (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Participates in an apoptotic pathway which is characterized
CC by activation of caspase-6, increases in the expression of BAK1 and
CC BCL2L1 and activation of NF-kappa-B. This pathway does not require
CC p53/TP53, nor does the presence of p53/TP53 affect the efficiency of
CC cell killing. Activates a G2/M cell cycle checkpoint prior to the onset
CC of apoptosis. Apoptosis is inhibited by association with RB1. Essential
CC for early embryonic development. Required for normal gene expression
CC during postnatal testis development (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the THO complex, which is composed of THOC1,
CC THOC2, THOC3, THOC5, THOC6 and THOC7; together with at least
CC ALYREF/THOC4, DDX39B, SARNP/CIP29 and CHTOP, THO forms the
CC transcription/export (TREX) complex which seems to have a dynamic
CC structure involving ATP-dependent remodeling. Binds to the
CC hypophosphorylated form of RB1. Interacts with THOC2, THOC5, DDX39B and
CC RNA polymerase II (By similarity). Interacts with LUZP4 (By
CC similarity). {ECO:0000250|UniProtKB:Q8R3N6,
CC ECO:0000250|UniProtKB:Q96FV9}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Nucleus,
CC nucleoplasm {ECO:0000250}. Nucleus matrix {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Note=Can shuttle between the nucleus and cytoplasm.
CC Nuclear localization is required for induction of apoptotic cell death.
CC Translocates to the cytoplasm during the early phase of apoptosis
CC execution (By similarity). {ECO:0000250}.
CC -!- DOMAIN: An intact death domain is needed for apoptosis. {ECO:0000250}.
CC -!- PTM: Expression is altered specifically during apoptosis and is
CC accompanied by the appearance of novel forms with smaller apparent
CC molecular mass. {ECO:0000250}.
CC -!- PTM: Polyubiquitinated, leading to proteasomal degradation; probably
CC involves NEDD4. {ECO:0000250}.
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DR EMBL; AY325254; AAP92655.1; -; mRNA.
DR AlphaFoldDB; P59924; -.
DR SMR; P59924; -.
DR STRING; 10116.ENSRNOP00000051059; -.
DR iPTMnet; P59924; -.
DR PhosphoSitePlus; P59924; -.
DR PaxDb; P59924; -.
DR PRIDE; P59924; -.
DR Ensembl; ENSRNOT00000045976; ENSRNOP00000051059; ENSRNOG00000032739.
DR UCSC; RGD:1308657; rat.
DR RGD; 1308657; Thoc1.
DR eggNOG; KOG2491; Eukaryota.
DR GeneTree; ENSGT00390000016232; -.
DR HOGENOM; CLU_069636_0_0_1; -.
DR InParanoid; P59924; -.
DR OMA; CKLETRE; -.
DR PhylomeDB; P59924; -.
DR TreeFam; TF314796; -.
DR PRO; PR:P59924; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000032739; Expressed in thymus and 16 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0000347; C:THO complex; ISO:RGD.
DR GO; GO:0000445; C:THO complex part of transcription export complex; ISO:RGD.
DR GO; GO:0000346; C:transcription export complex; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; ISS:UniProtKB.
DR GO; GO:0048297; P:negative regulation of isotype switching to IgA isotypes; ISS:UniProtKB.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
DR GO; GO:0000018; P:regulation of DNA recombination; ISS:UniProtKB.
DR GO; GO:0032784; P:regulation of DNA-templated transcription, elongation; ISO:RGD.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR GO; GO:0046784; P:viral mRNA export from host cell nucleus; ISO:RGD.
DR Gene3D; 1.10.533.10; -; 1.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR000488; Death_domain.
DR InterPro; IPR013544; DUF1725.
DR InterPro; IPR021861; THO_THOC1.
DR PANTHER; PTHR13265; PTHR13265; 1.
DR Pfam; PF00531; Death; 1.
DR Pfam; PF08333; DUF1725; 2.
DR Pfam; PF11957; efThoc1; 1.
DR SMART; SM00005; DEATH; 1.
DR SUPFAM; SSF47986; SSF47986; 1.
DR PROSITE; PS50017; DEATH_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Apoptosis; Cytoplasm; DNA-binding; Isopeptide bond;
KW mRNA processing; mRNA splicing; mRNA transport; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..343
FT /note="THO complex subunit 1"
FT /id="PRO_0000072522"
FT DOMAIN 13..31
FT /note="DUF1725 1"
FT DOMAIN 60..79
FT /note="DUF1725 2"
FT DOMAIN 248..331
FT /note="Death"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00064"
FT REGION 211..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96FV9"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FV9"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96FV9"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96FV9"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96FV9"
FT CROSSLNK 258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96FV9"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96FV9"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q96FV9"
SQ SEQUENCE 343 AA; 40243 MW; 7AA1C87DE90227BD CRC64;
MEYYSAIKNN DIMKFLSKWM GVEEIIPKAG KEPDVLQQTM DTENVVYLHN GLLLSYNDFM
KFIGKWMELE YIILSEFCEE RASYTKLKRG VWKRSAPEDF LDKRPNKKIL IGNEELTRLW
NLCPDNMEAC KLETREYMPI LEEFFEEAIE QADAENMVES EYKAINNSNY GWSTLRFLAW
RSPHFFQPTN QQFKNMTEYL ENMVIKLAKE LPPHSEEIKT GEDEDEEDND ALLKENESPD
VRQDKPITGE RIESLTNKLD EQWKILAPYL EIKDSDIRQI ECYSEDMKKR AKQLLVAWKD
QEGVHETTDN LIGALNKSGL SDLAESLTND TETNSYLLSL LFY
