THOC5_BOVIN
ID THOC5_BOVIN Reviewed; 683 AA.
AC A4IFQ0; A5D9B7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=THO complex subunit 5 homolog;
GN Name=THOC5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as component of the THO subcomplex of the TREX complex
CC which is thought to couple mRNA transcription, processing and nuclear
CC export, and which specifically associates with spliced mRNA and not
CC with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a
CC transcription-independent mechanism, binds to mRNA upstream of the
CC exon-junction complex (EJC) and is recruited in a splicing- and cap-
CC dependent manner to a region near the 5' end of the mRNA where it
CC functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway.
CC THOC5 in conjunction with ALYREF/THOC4 functions in NXF1-NXT1 mediated
CC nuclear export of HSP70 mRNA; both proteins enhance the RNA binding
CC activity of NXF1 and are required for NXF1 localization to the nuclear
CC rim. Involved in transcription elongation and genome stability.
CC Involved in alternative polyadenylation site choice by recruiting CPSF6
CC to 5' region of target genes; probably mediates association of the TREX
CC and CFIm complexes (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Regulates the expression of myeloid transcription factors
CC CEBPA, CEBPB and GAB2 by enhancing the levels of phosphatidylinositol
CC 3,4,5-trisphosphate. May be involved in the differentiation of
CC granulocytes and adipocytes. Essential for hematopoietic primitive cell
CC survival and plays an integral role in monocytic development (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with phosphorylated CSF1R. Component of the THO
CC complex, which is composed of THOC1, THOC2, THOC3, THOC5, THOC6 and
CC THOC7; together with at least ALYREF/THOC4, DDX39B, SARNP/CIP29 and
CC CHTOP, THO forms the transcription/export (TREX) complex which seems to
CC have a dynamic structure involving ATP-dependent remodeling. Interacts
CC with THOC1, ALYREF/THOC4, and THOC7. Interacts (via N-terminus) with
CC the NTF2 domain of NXF1. Forms a complex with CEBPB. Interacts with
CC CPSF6; indicative for an association with the cleavage factor Im (CFIm)
CC complex. Interacts with LUZP4. Interacts with NCBP3 (By similarity).
CC {ECO:0000250|UniProtKB:Q13769, ECO:0000250|UniProtKB:Q8BKT7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13769}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q13769}. Note=Shuttles between nucleus and
CC cytoplasm. {ECO:0000250|UniProtKB:Q13769}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A4IFQ0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A4IFQ0-2; Sequence=VSP_029321;
CC -!- PTM: Phosphorylated on tyrosine upon binding to activated CSF1R; which
CC causes a dissociation of the two proteins. Phosphorylation on Ser-5
CC and/or Ser-6 is required for nuclear export. Phosphorylated on Thr-328
CC in insulin-stimulated adipocytes (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the THOC5 family. {ECO:0000305}.
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DR EMBL; BT030536; ABQ12976.1; -; mRNA.
DR EMBL; BC134698; AAI34699.1; -; mRNA.
DR RefSeq; NP_001077185.1; NM_001083716.2. [A4IFQ0-1]
DR RefSeq; XP_005218127.1; XM_005218070.3.
DR RefSeq; XP_010812401.1; XM_010814099.2.
DR AlphaFoldDB; A4IFQ0; -.
DR SMR; A4IFQ0; -.
DR STRING; 9913.ENSBTAP00000029505; -.
DR PaxDb; A4IFQ0; -.
DR PRIDE; A4IFQ0; -.
DR GeneID; 533001; -.
DR KEGG; bta:533001; -.
DR CTD; 8563; -.
DR eggNOG; KOG2216; Eukaryota.
DR InParanoid; A4IFQ0; -.
DR OrthoDB; 1048314at2759; -.
DR TreeFam; TF314812; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000445; C:THO complex part of transcription export complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IBA:GO_Central.
DR GO; GO:0060215; P:primitive hemopoiesis; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR019163; THO_Thoc5.
DR PANTHER; PTHR13375; PTHR13375; 1.
DR Pfam; PF09766; FmiP_Thoc5; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cytoplasm; Differentiation;
KW Isopeptide bond; mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW Phosphoprotein; Reference proteome; RNA-binding; Transport;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13769"
FT CHAIN 2..683
FT /note="THO complex subunit 5 homolog"
FT /id="PRO_0000310554"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..199
FT /note="Interaction with THOC7"
FT /evidence="ECO:0000250|UniProtKB:Q13769"
FT REGION 2..144
FT /note="Interaction with CSF1R"
FT /evidence="ECO:0000250|UniProtKB:Q8BKT7"
FT REGION 302..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..10
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q13769"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKT7"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BKT7"
FT MOD_RES 225
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13769"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13769"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13769"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13769"
FT MOD_RES 328
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13769"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13769"
FT VAR_SEQ 282
FT /note="C -> CAHRKSSQPPRQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16305752"
FT /id="VSP_029321"
FT CONFLICT 236
FT /note="N -> I (in Ref. 1; ABQ12976)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 683 AA; 78530 MW; BF0E6CD9A1DA73C9 CRC64;
MSSESSKKRK PKVIRSDGAP AEGKRTRSDT EQEGKYYSEE AEVDLRDPGR DYELYKYTCQ
ELQRLMAEIQ DLKSRGGKDA AVEIEDRRIQ SCVHFMTLKK LNRLAHIRLK KGRDQTHEAK
QKVDAYHLQL QNLLYEVMHL QKEITKCLEF KSKHEEIDLV SLEEFYKEAP PDISKAEVTM
GDPHQQTLAR LDWELEQRKR LAEKYRECLS NKEKILKEIE VKKEYLSSLQ PRLNSNMQAS
LPVQEYLFMP FDQAHKQYET ARHLPPPLYV LFVQATAYGQ ACDKMLSVAI EGSVDEAKAL
FKPPEDSQDD ESDSDAEEEQ TTKRRRPTLG VQLDDKRKEM LKRHPLSVLL DLKCKDDSVL
HLTFYYLMNL NIMTVKARVT TATELITPIS AGDLLSPDSV LSCLYPGDHG KKTPNPANQY
QFDKVGILTL RDYVLDLGHP YLWVQKLGGL HFPKEQPQHT VITDHSLSAS HMETTMKLLK
TRVQSRLALH KQFASLEHGI VPVTSDCHYL FPAKVVSRLV KWVTIAHEDY TELHFTKDIV
EAGLAGDTNL YYMALVERGT AKLQAAVVLN PGYSSIPPIF QLCLNWKGEK TNNNDDNIRA
MESEVNVCYK ELCGPRPGHQ LLTNQLQRLC VLLDVYLETE SHDDSVEGPK EFPQEKMCLR
LFRGPSRIKP FKYNHPQGFF SHR
