ID A0A2K5Z1I8_MANLE Unreviewed; 1593 AA.
AC A0A2K5Z1I8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=THO complex subunit 2 {ECO:0000256|ARBA:ARBA00019596};
GN Name=THOC2 {ECO:0000313|Ensembl:ENSMLEP00000021666.1};
OS Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Mandrillus.
OX NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000021666.1, ECO:0000313|Proteomes:UP000233140};
RN [1] {ECO:0000313|Ensembl:ENSMLEP00000021666.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025995}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the THOC2 family.
CC {ECO:0000256|ARBA:ARBA00007857}.
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DR RefSeq; XP_011856891.1; XM_012001501.1.
DR SMR; A0A2K5Z1I8; -.
DR STRING; 9568.ENSMLEP00000021666; -.
DR Ensembl; ENSMLET00000045168.1; ENSMLEP00000021666.1; ENSMLEG00000034817.1.
DR GeneID; 105554873; -.
DR CTD; 57187; -.
DR GeneTree; ENSGT00710000106792; -.
DR OMA; QERWTCI; -.
DR OrthoDB; 179356at2759; -.
DR Proteomes; UP000233140; Unplaced.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0000445; C:THO complex part of transcription export complex; IEA:Ensembl.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0001824; P:blastocyst development; IEA:Ensembl.
DR GO; GO:0000902; P:cell morphogenesis; IEA:Ensembl.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IEA:Ensembl.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IEA:Ensembl.
DR GO; GO:0017145; P:stem cell division; IEA:Ensembl.
DR InterPro; IPR040007; Tho2.
DR InterPro; IPR021418; THO_THOC2_C.
DR InterPro; IPR021726; THO_THOC2_N.
DR InterPro; IPR032302; THOC2_N.
DR PANTHER; PTHR21597:SF0; THO COMPLEX SUBUNIT 2; 1.
DR PANTHER; PTHR21597; THO2 PROTEIN; 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 {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT DOMAIN 11..418
FT /note="THO complex subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16134"
FT DOMAIN 420..566
FT /note="THO complex subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16134"
FT DOMAIN 568..643
FT /note="THO complex subunitTHOC2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11732"
FT DOMAIN 873..1173
FT /note="THO complex subunitTHOC2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11262"
FT REGION 322..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1184..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 896..959
FT /evidence="ECO:0000256|SAM:Coils"
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..1585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1593 AA; 182802 MW; B569B39C6600FC2C CRC64;
MAAAAVVVPA EWIKNWEKSG RGEFLHLCRI LSENKSHDSS TYRDFQQALY ELSYHVIKGN
LKHEQASNVL NDISEFREDM PSILADVFCI LDIETNCLEE KSKRDYFTQL VLACLYLVSD
TVLKERLDPE TLESLGLIKQ SQQFNQKSVK IKTKLFYKQQ KFNLLREENE GYAKLIAELG
QDLSGSITSD LILENIKSLI GCFNLDPNRV LDVILEVFEC RPEHDDFFIS LLESYMSMCE
PQTLCHILGF KFKFYQEPNG ETPSSLYRVA AVLLQFNLID LDDLYVHLLP ADNCIMDEHK
REIAEAKQIV RKLTMVVLSS EKMDEREKEK EKEEEKVEKP PDNQKLGLLE ALLKIGDWQH
AQNIMDQMPP YYAASHKLIA LAICKLIHIT IEPLYRRVGV PKGAKGSPVN ALQNKRAPKQ
AESFEDLRRD VFNMFCYLGP HLSHDPILFA KVVRIGKSFM KEFQSDGSKQ 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
REVNKLKVQM 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 SSIGSASKSD ESSTEETDKS RERSQCGVKA VNKASSTTPK GNSSNGNSGS
NSNKAVKEND KEKGKEKEKE KKEKTPATTP EARVLGKDGK EKPKEERPNK DEKARETKER
TPKSDKEKEK FKKEEKAKDE KFKTTVPNAE SKSTQERERE KEPSRERDIA KEMKSKENVK
GGEKTPVSGS LKSPVPRSDI PEPEREQKRR KIDTHPSPSH SSTVKDSLIE LKESSAKLYI
NHTPPPLSKS KEREMDKKDL DKSRERSRER EKKDEKDRKE RKRDHSNNDR EVPPDLTKRR
KEENGTMGVS KHKSESPCES PYPNEKDKEK NKSKSSGKEK GSDSFKSEKM DKISSGGKKE
SRHDKEKIEK KEKRDSSGGK EEKKHHKSSD KHR
//
