THOC2_CALJA
ID THOC2_CALJA Reviewed; 1600 AA.
AC B0KWH8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=THO complex subunit 2;
DE Short=Tho2;
GN Name=THOC2;
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Benjamin B., Blakesley R.W., Bouffard G.G., Brinkley C.,
RA Brooks S., Chu G., Chub I., Coleman H., Fuksenko T., Gestole M.,
RA Gregory M., Guan X., Gupta J., Gurson N., Han E., Han J., Hansen N.,
RA Hargrove A., Hines-Harris K., Ho S.-L., Hu P., Hunter G., Hurle B.,
RA Idol J.R., Johnson T., Knight E., Kwong P., Lee-Lin S.-Q., Legaspi R.,
RA Madden M., Maduro Q.L., Maduro V.B., Margulies E.H., Masiello C.,
RA Maskeri B., McDowell J., Merkulov G., Montemayor C., Mullikin J.C.,
RA Park M., Prasad A., Ramsahoye C., Reddix-Dugue N., Riebow N., Schandler K.,
RA Schueler M.G., Sison C., Smith L., Stantripop S., Thomas J.W., Thomas P.J.,
RA Tsipouri V., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (FEB-2008) 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; DP000579; ABY90124.1; -; Genomic_DNA.
DR RefSeq; XP_017823950.1; XM_017968461.1.
DR AlphaFoldDB; B0KWH8; -.
DR SMR; B0KWH8; -.
DR STRING; 9483.ENSCJAP00000029803; -.
DR GeneID; 100399788; -.
DR KEGG; cjc:100399788; -.
DR CTD; 57187; -.
DR eggNOG; KOG1874; Eukaryota.
DR InParanoid; B0KWH8; -.
DR OrthoDB; 979205at2759; -.
DR Proteomes; UP000008225; Unplaced.
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; Reference proteome; RNA-binding; Transport.
FT CHAIN 1..1600
FT /note="THO complex subunit 2"
FT /id="PRO_0000384397"
FT REGION 321..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1600
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 1239..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1265..1381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1447..1509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1588
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 1385
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1390
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1443
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1486
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
FT MOD_RES 1516
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI27"
SQ SEQUENCE 1600 AA; 183794 MW; 634873AE3B5FB55B CRC64;
MAAAAVVVPA EWIKNWEKSG RGEFLHLCRI LSENKSLESS TYRDFQQALY ELSYHVIKGN
LKHEQASNVL NDISEFREDM PSILADVFCI LDIETNCLEE KSKRDNFTQL VLACLYLVSD
TVLKERLDPE TLESLGLIKQ SQQFNQKSVK IKTKLFYKQQ KFNLLREENE GYAKLIAELG
QDLSGSITSD LMLENIKSLI GCFNLDPNRV LDIILEVFEC RPEHDDFFMS LLESYMSMCE
PQTLCHILGF KFKFYQEPNG ETPSSLYRVA AVLLQFNLID LDDLYVHLLP ADNCIMDEHK
REIAEAKQIV RKLTMVVLSS EKMDDREKEK EKEEEKVERP PDNQKLGLLE ALLKIGDWQH
AQNIMDQMPP YYAASHKLIA LAICKLIHIT IEPLYRRVGV PKGAKGSPVN ALQNKRAPKQ
AESFEDLRRD VFNMFCYLGP HLSHDPILFA KVVRIGKSFM KEFQSDGSKQ EDKEKTEVIL
SCFLSTADQV LLPSLSLMDC NACMSEELWG MFKTFPYQYR 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
GRFLASNLST 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 GQLKSRKSYM IPENEFHHKD PPPRNAVASV
QNGPGGGPSS SSTGSSSKSD ESSTEETDKS RERSQCGVKA VNKASNTTPK GNSSNGNSGS
NSNKAVKEND KEKGKEKEKE KKEKTPATTP EARVLGKDGK EKPKEERPNK DEKARETKER
TPKSDKEKEK FKKEEKVKDE KFKTTIPNAE SKSSQERERE KEPSRERDIA KEMKSKENVK
GGEKTPVSGS LKSPVPRSDI PEPEREQKRR KIDTHPSPSH SSTVKDSLIE LKESSAKLYV
NHTPAPLSKS KEREMDKKDL DKSRERSRER EKKDEKDRKE RKRDHSNNDR EVPPDLIKRR
KEENGTMGVS KHKSESPCES PYPNEKDKEK NKSKSSGKEK GSDSFKSEKM DKISSGGKKE
SRHDKEKIEK KEKRDSSGGK EEKKQYPFHL DVFSQYNGKL
