TPR_XENLA
ID TPR_XENLA Reviewed; 1997 AA.
AC Q5EE04; P79992;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 42.
DE RecName: Full=Nucleoprotein TPR;
DE AltName: Full=NPC-associated intranuclear protein;
DE AltName: Full=Translocated promoter region and nuclear basket protein;
DE Flags: Fragment;
GN Name=tpr;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=9024684; DOI=10.1083/jcb.136.3.515;
RA Cordes V.C., Reidenbach S., Rackwitz H.R., Franke W.W.;
RT "Identification of protein p270/Tpr as a constitutive component of the
RT nuclear pore complex-attached intranuclear filaments.";
RL J. Cell Biol. 136:515-529(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Yang H.S., Deng H.X., Peng F., Zhao X., Wei Y.Q.;
RT "Serological screening of cDNA expression library.";
RL Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTS WITH KPNB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9531546; DOI=10.1083/jcb.141.1.31;
RA Shah S., Tugendreich S., Forbes D.;
RT "Major binding sites for the nuclear import receptor are the internal
RT nucleoporin Nup153 and the adjacent nuclear filament protein Tpr.";
RL J. Cell Biol. 141:31-49(1998).
CC -!- FUNCTION: Component of the nuclear pore complex (NPC), a complex
CC required for the trafficking across the nuclear envelope. Functions as
CC a scaffolding element in the nuclear phase of the NPC essential for
CC normal nucleocytoplasmic transport of proteins and mRNAs, plays a role
CC in the establishment of nuclear-peripheral chromatin
CC compartmentalization in interphase, and in the mitotic spindle
CC checkpoint signaling during mitosis. Involved in the quality control
CC and retention of unspliced mRNAs in the nucleus. Implicated in nuclear
CC export of mRNAs transcribed from heat shock gene promoters. May play a
CC limited role in the regulation of nuclear protein export. May be
CC involved in the formation and/or maintenance of NPC-associated
CC perinuclear heterochromatin exclusion zones (HEZs). Finally, may act as
CC a spatial regulator of the spindle-assembly checkpoint (SAC) response
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Part of the nuclear pore complex (NPC) (By
CC similarity). Interacts with nuclear receptor KPNB1; the interaction
CC occurs in a RanGTP-dependent manner. Associates with the Importin
CC alpha/Importin beta receptor. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P12270}. Nucleus
CC membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P12270}; Nucleoplasmic side
CC {ECO:0000250|UniProtKB:P12270, ECO:0000269|PubMed:9531546}. Nucleus
CC envelope {ECO:0000250|UniProtKB:P12270}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:9024684}. Cytoplasm {ECO:0000250|UniProtKB:P12270}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P12270}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P12270}.
CC Nucleus membrane {ECO:0000250|UniProtKB:P12270}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:P12270}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P12270}. Note=Localized to the nucleoplasmic
CC side of the nuclear pore complex (NPC) core structure, forming a
CC fibrous structure called the nuclear basket. Localized to the nuclear
CC periphery and in intranuclear spheroidal structures. Localized at NPC-
CC attached intranuclear filament bundles projecting into the nuclear
CC interior (PubMed:9024684). Colocalized with nup153 at the nuclear pore
CC complex (PubMed:9531546). {ECO:0000269|PubMed:9024684,
CC ECO:0000269|PubMed:9531546}.
CC -!- TISSUE SPECIFICITY: Expressed in epithelial cells, oocytes and egg (at
CC protein level). {ECO:0000269|PubMed:9024684,
CC ECO:0000269|PubMed:9531546}.
CC -!- SIMILARITY: Belongs to the TPR family. {ECO:0000305}.
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DR EMBL; U69669; AAB48031.1; -; mRNA.
DR EMBL; AY902464; AAW82480.1; -; mRNA.
DR AlphaFoldDB; Q5EE04; -.
DR SMR; Q5EE04; -.
DR PRIDE; Q5EE04; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005868; C:cytoplasmic dynein complex; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
DR GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0034399; C:nuclear periphery; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; ISS:UniProtKB.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0031072; F:heat shock protein binding; ISS:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0017056; F:structural constituent of nuclear pore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034605; P:cellular response to heat; ISS:UniProtKB.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; ISS:UniProtKB.
DR GO; GO:0046832; P:negative regulation of RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045947; P:negative regulation of translational initiation; ISS:UniProtKB.
DR GO; GO:0031453; P:positive regulation of heterochromatin assembly; ISS:UniProtKB.
DR GO; GO:0090316; P:positive regulation of intracellular protein transport; ISS:UniProtKB.
DR GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; ISS:UniProtKB.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0006606; P:protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0010965; P:regulation of mitotic sister chromatid separation; ISS:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; ISS:UniProtKB.
DR GO; GO:0070849; P:response to epidermal growth factor; ISS:UniProtKB.
DR GO; GO:0006405; P:RNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0006404; P:RNA import into nucleus; ISS:UniProtKB.
DR InterPro; IPR012929; TPR/MLP1.
DR Pfam; PF07926; TPR_MLP1_2; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Coiled coil; Cytoplasm;
KW Cytoskeleton; Kinetochore; Membrane; Mitosis; mRNA transport;
KW Nuclear pore complex; Nucleus; Protein transport; Reference proteome;
KW Translocation; Transport.
FT CHAIN <1..1997
FT /note="Nucleoprotein TPR"
FT /id="PRO_0000422102"
FT REGION 672..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1752
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1795..1832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1870..1997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1..36
FT /evidence="ECO:0000255"
FT COILED 101..277
FT /evidence="ECO:0000255"
FT COILED 335..1103
FT /evidence="ECO:0000255"
FT COILED 1129..1305
FT /evidence="ECO:0000255"
FT COMPBIAS 672..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1438..1487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1602..1667
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1875..1898
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1922..1964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 1997 AA; 226054 MW; 8EAFE39C1C6E9EC7 CRC64;
QEQHSQLEAA KTQVEKDMGE KISNLERELE NANDLLCSTK RKGVMLSEEE LTAMSPTAAA
VAKVVKPGMK LTELYNAYVE TQDKLLMEKQ ENKRITKYLD EIVKEVEAKS PILKRQREEY
ERMQKTVASL SAKLEQAMRE IQRMQDETDK ANKCSSVLER ENQRLELQIK DLSQQIRVLL
MELEEARGNF VQRDDVSSAN ISSSSEVITQ HLVTYRNIEE LQQQNQRLLV ALRELGEAKE
REEQESTSSR VSELEKELEN ALSELQQLRE ARSHQMTLVE SIVRQRDMYR ILLSQTTGVV
LPAQDETALT STPRKSPGVS LDGSTSTPAA VVVSDSTEAA EARAALKQLQ EVFENYRKEK
AENDRMLNEQ HDKLQEQVTE LRSQNTKIST QLEFASKRYE MLQDNVEGYR REITALQEKT
QKLSATTQKQ EQIINTLTHD LRAANEKLAV AEVRAENLKR EKELLKMSEV RLTQERESLV
AEQRGQNLLL TNLQTIQVTL ERSETEIKQR YNNQIEKLEQ ELAQTKKKLE HEIEQRHLLG
KNQDVQVLEL KKQYEMELNL HNNTKELLKN SHKEISVLKQ QLNSFELQLA SRSSQQAANR
DKDVNIEDVE EIKTKLRQSE ELVNDLKERL KTATSNVEQY RSVVLNLEES LNKEKQVTEE
VRKTIEVRLK ESSEYQSQLE KKMMESEKEK QELRDEKHKT VEQMEQQVTQ LRQSLSSLQA
EVQQALQRAT TSASNEQKAK QDCQEQARIA AEAQNKYERE LMLHAADVEA LQAAKKQLTS
ASAIRHKCEE TAQKAGSQLL ESRASWEERE RMLKEEVSQI QSRCKDLEKQ NGLLHEQIES
LSKKMVTSVQ EGALNMSFGE EGKSQEQVME ILRFVRREKE IAEARFEVAQ VECLRYRQRI
EHMERELHEL QDSLNAEREK VQVTAKTMAQ HEELMKKTET MNVLIESNKI LREENEKQEQ
ELQQLQAKIR KLESNILPLQ ESNAELSEKS GMLQAEKKLL EEDVRRWRAR TQHLLSQQKD
TDAEEYKKLL SEREVNTKRI QQLTEETGKL KTEVARTNAS LNTCQSQLQS VKDDLTKIKA
EKEKLQKELD AKILDIQEKI KTITQVKKIG RRYKTQYEEL KVTHDKMVAE ASSAKADQLQ
EQASQKEVQE LKDSLQRSEA KVTTMQTTVD NMQKTLDDKD NEIKEHQEQI SRMQAELSHL
HKDLQDKTAQ EEQMRQQINE KEEKTKKTLL VVRQKLAQNN GAKEQLTREN EDLKQKNANL
EQQKEELEVR MSALRSQYDG RISRLERELR EQQERHHEQR DEPQETTRIP QQRQITLQPT
TAAGERGSAN TSEPPTANIK PTPSKVTTAA VPVNKSTPRA SIRPMVTPAA VSTPTSTPTA
TVMPTTQVDQ QEVQSEGQME HVPVFGSASG SVRSTSPNVQ SSLPQPILTL QQQTQTTAFV
QPTQQSHATI ESPTQETPVE IVQSSPVERP TTSSTFGTYS ATPSSSIPKR PREEEEDSTI
ETPEQIADDT DQQRTKKRKE EDIEEKTETE AVINTEDALH ILTQCSNMEF PLEEEIVESP
IQTSQVIESQ APEQLQNVQS TQDSLQDTPP KKTHNLVIVI SDEENEDEQE GYEEEEQEDE
EEDEDDAGIG EGDDSNEETG SADGNEDYEG DDAEEADGTD PDTETEDSMT AGEGNQRAAD
SQNIGDSGVV TAESTFSQET REQPSSASDR QGPRPPQSPR RQAHPPRLTI LAPPQELGPP
PAQRIPVARR QSVGRGLQLT PGVGGMQHFF DEEDRTVPST PTLVVPHRTD GFAEAIHSPQ
VAGVPRFRFG PPEDMPQASS SHSDLGQLAS QGGLGMYDTP LFLAHEEESG GRSVPTTPLQ
VAAPVSVFAE NPAADTSDHA SQSVPMVTTS TGNVPTSVDS GAADEGDEVF VEAESEGIGA
ESTLEMDTQQ EEPVQPSEAD LPSTSQDPPS SSIADTSSSK PKPRRVWLQP QPGGRPFKRS
RGGSDFRGRG GINRSNI
