THOC5_RAT
ID THOC5_RAT Reviewed; 682 AA.
AC Q68FX7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=THO complex subunit 5 homolog;
DE AltName: Full=Fms-interacting protein;
GN Name=Thoc5; Synonyms=Fmip;
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=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 -!- 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-327
CC in insulin-stimulated adipocytes (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the THOC5 family. {ECO:0000305}.
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DR EMBL; BC079058; AAH79058.1; -; mRNA.
DR RefSeq; NP_001012153.1; NM_001012153.1.
DR AlphaFoldDB; Q68FX7; -.
DR SMR; Q68FX7; -.
DR STRING; 10116.ENSRNOP00000011281; -.
DR iPTMnet; Q68FX7; -.
DR PhosphoSitePlus; Q68FX7; -.
DR PaxDb; Q68FX7; -.
DR PRIDE; Q68FX7; -.
DR GeneID; 360972; -.
DR KEGG; rno:360972; -.
DR UCSC; RGD:1304991; rat.
DR CTD; 8563; -.
DR RGD; 1304991; Thoc5.
DR VEuPathDB; HostDB:ENSRNOG00000008456; -.
DR eggNOG; KOG2216; Eukaryota.
DR HOGENOM; CLU_023759_1_0_1; -.
DR InParanoid; Q68FX7; -.
DR OMA; WNGCHTS; -.
DR OrthoDB; 1048314at2759; -.
DR PhylomeDB; Q68FX7; -.
DR Reactome; R-RNO-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-RNO-72187; mRNA 3'-end processing.
DR Reactome; R-RNO-73856; RNA Polymerase II Transcription Termination.
DR PRO; PR:Q68FX7; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000008456; Expressed in testis and 20 other tissues.
DR Genevisible; Q68FX7; RN.
DR GO; GO:0005737; C:cytoplasm; 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:0003729; F:mRNA binding; ISO:RGD.
DR GO; GO:0001824; P:blastocyst development; ISO:RGD.
DR GO; GO:0000902; P:cell morphogenesis; ISO:RGD.
DR GO; GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; ISO:RGD.
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:0045650; P:negative regulation of macrophage differentiation; ISO:RGD.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; ISS:UniProtKB.
DR GO; GO:0060215; P:primitive hemopoiesis; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; ISO:RGD.
DR GO; GO:2000035; P:regulation of stem cell division; ISO:RGD.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR GO; GO:0017145; P:stem cell division; ISO:RGD.
DR GO; GO:0046784; P:viral mRNA export from host cell nucleus; ISO:RGD.
DR InterPro; IPR019163; THO_Thoc5.
DR PANTHER; PTHR13375; PTHR13375; 1.
DR Pfam; PF09766; FmiP_Thoc5; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Differentiation; Isopeptide bond; mRNA processing;
KW mRNA splicing; mRNA transport; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q13769"
FT CHAIN 2..682
FT /note="THO complex subunit 5 homolog"
FT /id="PRO_0000310556"
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 300..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 7..10
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 317..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 327
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"
SQ SEQUENCE 682 AA; 78660 MW; 0877FFE0E861F1F4 CRC64;
MSSESSKKRK PKVIRSDGTP TEGKRNRSDT EQEGRYYSEE AEVDLRDPGR DYELYKYTCQ
ELQRLMAEIQ DLKSKGSKDV AIEIEERRIQ SCVHFMTLKK LNRLAHIRLK KGRDQTHEAK
QKVDAYHLQL QNLLYEVMHL QKEITKCLEF KSKHEEIDLV SLEEFYSEAP PNISKAEITM
GDPHQQTLAR LDWELEQRKR LAEKYRECLS NKEKILKEIE VKKEYLSSLQ PRLNSIMQAS
LPVQEYLFMP FDQAHKQYET ARHLPPPLYV LFVQATAYGQ ACDKTLSVAI EGSVDEAKAL
FKPPEDSQDD ESDSDAEEEQ TTRRRPTLGV QLDDKRKEML KRHPLSVLLD LKCKDNSVLH
LTFFYLMNLN IMTVKAKVTT AMELITPISA GDLLSPDSVL SCLYPGDHGK KTPNPANQYQ
FDKVGILTLR DYVLELGHPY LWVQKLGGLH FPKEQPQHTV MADHSQSASH METTMKLLKT
RVQSRLALHK QFASLEHGIV PVTSECQYLF PAKVVSRLVK WMIMAHEDYM ELHFTKDIVE
AGLAGDTNLY YLALIERGTA KLQAAVVLNP GYSSIPPVFR LCLNWKGEKT NSNDDNIRAM
ESEVNVCYRE LCGPRPSHQL LTNQLQRLCV LLDVYLETES HDDSVEGPKE FPQEKMCLRL
FRGPSRMKPF KYNHPQGFFS HR
