THOC2_DASNO
ID THOC2_DASNO Reviewed; 1613 AA.
AC C1FXW9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=THO complex subunit 2;
DE Short=Tho2;
GN Name=THOC2;
OS Dasypus novemcinctus (Nine-banded armadillo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Xenarthra; Cingulata; Dasypodidae; Dasypus.
OX NCBI_TaxID=9361;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for efficient export of polyadenylated RNA and
CC spliced mRNA. Acts as component of the THO subcomplex of the TREX
CC complex which is thought to couple mRNA transcription, processing and
CC nuclear export, and which specifically associates with spliced mRNA and
CC not 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 Plays a role for proper neuronal development.
CC {ECO:0000250|UniProtKB:Q8NI27}.
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. Interacts with THOC1,
CC POLDIP3 and ZC3H11A (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Nucleus speckle
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the THOC2 family. {ECO:0000305}.
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DR EMBL; DP001089; ACO71284.1; -; Genomic_DNA.
DR AlphaFoldDB; C1FXW9; -.
DR SMR; C1FXW9; -.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0000347; C:THO complex; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0048699; P:generation of neurons; ISS:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR040007; Tho2.
DR InterPro; IPR021418; THO_THOC2_C.
DR InterPro; IPR021726; THO_THOC2_N.
DR InterPro; IPR032302; THOC2_N.
DR PANTHER; PTHR21597; PTHR21597; 1.
DR Pfam; PF11262; Tho2; 1.
DR Pfam; PF11732; Thoc2; 1.
DR Pfam; PF16134; THOC2_N; 2.
PE 3: Inferred from homology;
KW Coiled coil; mRNA processing; mRNA splicing; mRNA transport; Nucleus;
KW Phosphoprotein; RNA-binding; Transport.
FT CHAIN 1..1613
FT /note="THO complex subunit 2"
FT /id="PRO_0000384398"
FT REGION 1182..1586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 293..339
FT /evidence="ECO:0000255"
FT COILED 896..965
FT /evidence="ECO:0000255"
FT COILED 1464..1491
FT /evidence="ECO:0000255"
FT MOTIF 923..928
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1202..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1236
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1264..1380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1446..1508
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1586
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1222
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:B1AZI6"
FT MOD_RES 1384
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1442
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1449
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1485
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1515
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
SQ SEQUENCE 1613 AA; 184947 MW; 8B54BF3F9173D195 CRC64;
MAAATVVVPA EWIKNWEKSG RGEFLHLCRI LSENKGHDSS TYRDFQQALY ELSYHVIKGN
LKHEQASNVL NDISEFREDM PSILADVFCI LDIETNCLEE KSKRDYFTQL VLACLYLVSD
TVLKERLDPE TLESLGLIKQ SQQFNQKSVK IKTKLFYKQQ KFNLLREENE GYAKLIAELG
QDLSGNITSD LILENIKSLI GCFNLDPNRV LDVILEVFEC RPEHDDFFIS LLESYMSMCE
PQTLCHILGF KFKFYQEPNG ETPSSLYRVA AVLLQFNLID LDDLYVHLLP ADNSIMDEHK
REIVEAKQIV RKLTMVVLSS EKIDEREKEK EKEEEKVEKP PDNQKLGLLE ALLKIGDWQH
AQNIMDQMPP YYAASHKLIA LAICKLIHIT IEPLYRRVGV PKGAKGSPVN ALQNKRAPKQ
AENFEDLRRD VFNMFCYLGP HLSHDPILFA KVVRIGKSFM KEFQSDGSKS EDKEKTEVIL
SCLLSITDQV LLPSLSLMDC NACMSEELWG MFKTFPYQHR YRLYGQWKNE TYNSHPLLVK
VKAQTIDRAK YIMKRLTKEN VKPSGRQIGK LSHSNPTILF DYILSQIQKY DNLITPVVDS
LKYLTSLNYD VLAYCIIEAL ANPEKERMKH DDTTISSWLQ SLASFCGAVF RKYPIDLAGL
LQYVANQLKA GKSFDLLILK EVVQKMAGIE ITEEMTMEQL EAMTGGEQLK AEGGYFGQIR
NTKKSSQRLK DALLDHDLAL PLCLLMAQQR NGVIFQEGGE KHLKLVGKLY DQCHDTLVQF
GGFLASNLST EDYIKRVPSI DVLCNEFHTP HDAAFFLSRP MYAHHISSKY DELKKSEKGS
KQQHKVHKYI TSCEMVMAPV HEAVVSLHVS KVWDDISPQF YATFWSLTMY DLAVPHTSYE
REVNKLKIQM KAIDDNQEMP PNKKKKEKER CTALQDKLLE EEKKQMEHVQ RVLQRLKLEK
DNWLLAKSTK NETITKFLQL CIFPRCIFSA IDAVYCARFV ELVHQQKTPN FSTLLCYDRV
FSDIIYTVAS CTENEASRYG RFLCCMLETV TRWHSDRATY EKECGNYPGF LTILRATGFD
GGNKADQLDY ENFRHVVHKW HYKLTKASVH CLETGEYTHI RNILIVLTKI LPWYPKVLNL
GQALERRVHK ICQEEKEKRP DLYALAMGYS GQLKSRKPYM IPENEFHNKD PPPRNAVASV
QNGPGGGPSS SSIGSASKSD ESSTEETDKS RERSQCSVKA VNKASSATPK GNSSNGNSGS
NSKAVKENEK EKGKEKEKEK KEKTPATTPE ARVLGKDGKE KPKEERPNKD EKARETKERT
PKSDKEKEKF KKEEKAKDEK FKTAIPNVES KSTQEKEREK EPSRERDIAK DMKSKENVKG
GEKTAVSGSL KSPVPRSDIA EPEREQKRRK IDTHPSPSHS STVKDSLIEL KESSAKLYIN
HTPPPLSKSK EREMDKKDLD KSRERSRERE KKDEKDRKER KRDHSNNDRE VPPDLTKRRK
EENGTMGVSK HKSESPCESP YANEKDKEKN KSKSSGKEKS SDSFKSEKMD KISSGGKKES
RHDKEKIEKK EKRDSSGGKE EKKQYPFHLN NALNQCMESF DADNVLKVYS SVV
