ID A0A3P8S521_AMPPE Unreviewed; 1407 AA.
AC A0A3P8S521;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=THO complex subunit 2 {ECO:0000256|ARBA:ARBA00019596};
OS Amphiprion percula (Orange clownfish) (Lutjanus percula).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Amphiprion.
OX NCBI_TaxID=161767 {ECO:0000313|Ensembl:ENSAPEP00000007202.1, ECO:0000313|Proteomes:UP000265080};
RN [1] {ECO:0000313|Ensembl:ENSAPEP00000007202.1, ECO:0000313|Proteomes:UP000265080}
RP NUCLEOTIDE SEQUENCE.
RA Lehmann R.;
RT "Finding Nemo's genes: A chromosome-scale reference assembly of the genome
RT of the orange clownfish Amphiprion percula.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPEP00000007202.1}
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 Ensembl; ENSAPET00000007400.1; ENSAPEP00000007202.1; ENSAPEG00000004792.1.
DR GeneTree; ENSGT00710000106792; -.
DR Proteomes; UP000265080; Chromosome 15.
DR GO; GO:0000347; C:THO complex; IEA:InterPro.
DR GO; GO:0006406; P:mRNA export from nucleus; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
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:UP000265080}.
FT DOMAIN 10..361
FT /note="THO complex subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16134"
FT DOMAIN 384..514
FT /note="THO complex subunit 2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF16134"
FT DOMAIN 516..591
FT /note="THO complex subunitTHOC2 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF11732"
FT DOMAIN 821..1121
FT /note="THO complex subunitTHOC2 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11262"
FT REGION 283..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1134..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 844..907
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1142..1167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1185..1209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1211..1318
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1330..1344
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1352..1389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1407 AA; 160889 MW; 264E94ED625898E8 CRC64;
MATLILPDIQ AALYELCWQV VQGNLKLDLV ASVLGDMMEL RDDMPSILAD VFSILDLETG
ALEEKNKRDH YTQLVGACLF FVPEAILKER LDPETLESLG LIKQAHQFNQ KIVKIKTKLF
YKQQKFNLLR EENEGYAKLI TELGQDLSGN ITSHVVLESI KSLIGCFNLD PNRVLDIILE
VYESRSDQDE FFLSLIKSYM CEPLTLCHIL GFKFKFYQEP NEETPKSLYH IAAALLHHNL
IELEDLYVHL MPLDTTIIEE HKRDISEAKQ IARKLVMVVL PSEKNEDKEK EKEKEEEKNE
RPPDNQKLGL LEALLRIGDW HHAQSIMDQM PSFYATSHKA IALALCQLVH LTVEPLYRRA
GVPKGARGCV MHPLRNKRAP RPAENFEDLR RDTFSMLCYL GPHLSHDPIL FAKIVRLGKG
FMKEDTLLSC FLSIADQVLL PSLSLMECNA CMSEELWGLF KLFPYQHRYR LYGQWKNETY
SSHPLLVKVK AQTVERAKYI MKRLTKENVK QSGRQIGKLS HSNPTILFDY MLSQIQWYDN
LIVPVVDSLK YLTSLNYDVL AYCIIEALAN PEKEKMKHDD TTISSWLQSL ASLCGAVFRK
YPIELAGLLQ YVTNQLKAGK SFDLLILKEV VQKMAGIEIT DEMTSEQLEA MTGGEQLKAE
GGYFGQIRNT KKSSQRLKDA LLDHELALPL CLLMAQQRNG VVFLEGGEKH LKLVGHLYDQ
CHDTLVQFGG FLASNLSTED YIKRVPSIDI LCNQFHTPHD AAFFLSRPMY AHQILSKYDE
LKKAEKGNRQ QQKVHKYVAA CEQVMTPVHE AVVSLHPARV WDDLRPQFYA TFWSLTMYDL
AVPHSAYERE VNKLKVQIKA IEENPEIPLN KKKKEKERCT ALQEKLQEEE KKQLEHVQRV
LHRLKLEKDN WLLAKSTKNE TITKFLQLCL FPRCIFSSID AVYCARFVEL VHQQKTPNFC
TLLCYDRVFS AIIYTVASCT ENESHRYGRF LCCMLETVTR WHSDRATYEK ECVNYPGFLT
IFRATGFDGG NKADQLDYEN FRHVVHKWHY MLTKASVHCL ETGDYTHIRN ILIVLTKILP
CYPKVLNLGQ ALECRVHKIC LEEKDKRPDL YALAMGYSGR LKSQKVHMVP ENEFHHKEQP
ARSATPASQQ NGPGSTGKPA TSTSKTEEGT SEDGDRGKDK SQGTAKPVNK ANSAAAKVTT
SNGNGALNST KAVKERDDKE KSGKEKKEKK EKTPGSTPET KAENRREKQR DERAGKEERV
AREGKEKTPK ADREKVKPEE KSNKDDKAKA GNGEPVEPSR ERDAIKESKS KEKGDRSAVA
GSLKSPVPRS ESAESERDKG APDYVKLFRI SLARSKSRER ETEKKDSENT QGRSKEKKEE
KDRKDRKRVS IASTLVKKSF WKSWCSD
//
