ID   F6UV28_CANLF            Unreviewed;      2361 AA.
AC   F6UV28;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2019, sequence version 2.
DT   17-JUN-2020, entry version 56.
DE   SubName: Full=Translocated promoter region, nuclear basket protein {ECO:0000313|Ensembl:ENSCAFP00000020227};
GN   Name=TPR {ECO:0000313|Ensembl:ENSCAFP00000020227,
GN   ECO:0000313|VGNC:VGNC:53807};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615 {ECO:0000313|Ensembl:ENSCAFP00000020227, ECO:0000313|Proteomes:UP000002254};
RN   [1] {ECO:0000313|Ensembl:ENSCAFP00000020227, ECO:0000313|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000020227,
RC   ECO:0000313|Proteomes:UP000002254};
RX   PubMed=16341006; DOI=10.1038/nature04338;
RG   Broad Sequencing Platform;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2] {ECO:0000313|Ensembl:ENSCAFP00000020227}
RP   IDENTIFICATION.
RC   STRAIN=Boxer {ECO:0000313|Ensembl:ENSCAFP00000020227};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
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DR   EMBL; AAEX03005165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 9612.ENSCAFP00000020227; -.
DR   PaxDb; F6UV28; -.
DR   PRIDE; F6UV28; -.
DR   Ensembl; ENSCAFT00000021777; ENSCAFP00000020227; ENSCAFG00000013717.
DR   VGNC; VGNC:53807; TPR.
DR   eggNOG; KOG4674; Eukaryota.
DR   eggNOG; ENOG410XSA1; LUCA.
DR   GeneTree; ENSGT00730000111014; -.
DR   HOGENOM; CLU_001059_0_0_1; -.
DR   TreeFam; TF350364; -.
DR   Reactome; R-CFA-159227; Transport of the SLBP independent Mature mRNA.
DR   Reactome; R-CFA-159230; Transport of the SLBP Dependant Mature mRNA.
DR   Reactome; R-CFA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR   Reactome; R-CFA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR   Reactome; R-CFA-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR   Reactome; R-CFA-191859; snRNP Assembly.
DR   Reactome; R-CFA-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-CFA-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-CFA-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR   Reactome; R-CFA-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-CFA-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-CFA-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-CFA-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-CFA-4615885; SUMOylation of DNA replication proteins.
DR   Reactome; R-CFA-5578749; Transcriptional regulation by small RNAs.
DR   Proteomes; UP000002254; Chromosome 7.
DR   Bgee; ENSCAFG00000013717; Expressed in prefrontal cortex and 2 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR   GO; GO:0005868; C:cytoplasmic dynein complex; IEA:Ensembl.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:Ensembl.
DR   GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR   GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR   GO; GO:0042405; C:nuclear inclusion body; IEA:Ensembl.
DR   GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR   GO; GO:0034399; C:nuclear periphery; IEA:Ensembl.
DR   GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR   GO; GO:0044615; C:nuclear pore nuclear basket; IEA:Ensembl.
DR   GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0070840; F:dynein complex binding; IEA:Ensembl.
DR   GO; GO:0031072; F:heat shock protein binding; IEA:Ensembl.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
DR   GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0017056; F:structural constituent of nuclear pore; IBA:GO_Central.
DR   GO; GO:0015631; F:tubulin binding; IEA:Ensembl.
DR   GO; GO:0035457; P:cellular response to interferon-alpha; IEA:Ensembl.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint; IEA:Ensembl.
DR   GO; GO:0006406; P:mRNA export from nucleus; IBA:GO_Central.
DR   GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IEA:Ensembl.
DR   GO; GO:0046832; P:negative regulation of RNA export from nucleus; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IEA:Ensembl.
DR   GO; GO:0006999; P:nuclear pore organization; IEA:Ensembl.
DR   GO; GO:0031453; P:positive regulation of heterochromatin assembly; IEA:Ensembl.
DR   GO; GO:0090267; P:positive regulation of mitotic cell cycle spindle assembly checkpoint; IEA:Ensembl.
DR   GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR   GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR   GO; GO:1901673; P:regulation of mitotic spindle assembly; IBA:GO_Central.
DR   GO; GO:0070849; P:response to epidermal growth factor; IEA:Ensembl.
DR   GO; GO:0006404; P:RNA import into nucleus; IEA:Ensembl.
DR   InterPro; IPR012929; TPR/MLP1.
DR   Pfam; PF07926; TPR_MLP1_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002254}.
FT   DOMAIN          1037..1164
FT                   /note="TPR_MLP1_2"
FT                   /evidence="ECO:0000259|Pfam:PF07926"
FT   REGION          911..933
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1617..1672
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1801..2123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2225..2361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          29..49
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          68..95
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          112..171
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          218..280
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          320..365
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          426..512
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          542..602
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          663..750
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          758..799
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          825..866
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          995..1069
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1094..1114
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1133..1167
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1219..1253
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1267..1301
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1309..1343
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1352..1414
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1467..1550
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1562..1596
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        911..925
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1617..1634
FT                   /note="Polyampholyte"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1635..1672
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1801..1825
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1878..1896
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1903..1936
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1943..1983
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1998..2012
FT                   /note="Acidic"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2019..2068
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2069..2088
FT                   /note="Pro-rich"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2225..2258
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2294..2323
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2361 AA;  267279 MW;  1E93618F15C1F589 CRC64;
     MAAVLQQVLE RTELNKLPKS VQNKLEKFLA DQQSEIDGLK GRHEKFKVES EQQYFEIEKR
     LSHSQERLVN ETRECQSLRL DLEKLTNHRA LVEKKKNFKF VRVPNFPFGS QFTRTKEELE
     AEKRDLVRTN ERLSQELEYL TEDFKRLNEK LKESNATKGD LQLKLDELQA SDVSVKYREK
     RLEQEKELLH NQNTWLNTEL KTKTDELLAL GREKGNEILE LKCNLENKKE EVSRMEEQMS
     GLKTSNENLQ KHVEELLTKL KEAKEQQASM EEKFHNELNA HIKLSNLYKS AADDSEAKSN
     ELTRAVDELH KLLKEAGEAN KAIQDHLLEV EESKDQMEKE MLEKIGKLEK ELENANDLLS
     ATKRKGAILS EEELAAMSPT AAAVAKIVKP GMKLTELYNA YVETQDQLLL EKLENKRINK
     YLDEIVKEVE AKAPILKRQR EEYERAQKAV ASLSVKLEQA MKEIQRLQED TDKANKHSSV
     LERDNQRMEI QIKDLSQQIR VLLMELEEAR GNHVIRDEEV SSADISSSSE VISQHLVSYR
     NIEELQQQNQ RLLVALRELG ETREREEQET TSSKIAELQL KLENALTELE QLRESRQHQM
     QLVDSIVRQR DMYRILLSQR GVAIPLQPSS LEDISLASTP KRSSTSQTAS TPAPVPVIES
     AEAIEAKAAL KQLQEIFENY KKEKADNEKI QNEQLEKLQD QITDLRSQNT KISTQLDFAS
     KRYEMLQDNV EGYRREITSL HERNQKLTAT TQKQEQIINT MTQDLRGANE KLAVAEVRAE
     NLKKEKEMLK LSEVRLSQQR ESLLAEQRGQ NLLLTNLQTI QGILERSETE TKQRLSSQIE
     KLEHEISHLK KKLENEVEQR HTLTRNLDVQ LLDTKRQLDT ETNLHLNTKE LLKNAQKEIA
     TLKQHLSNME VQLASQSSQR TGKGQPSNKE DVDDLLSQLR QAEEQVNDLK ERLKTSTSNV
     EQYRAMVTSL EESLNKEKQV TEEVRKNIEV RLKESAEFQT QLEKKLMEVE KEKQELQDDK
     RKAIESMEHQ LSELKKTLNS VQNEVQEALQ RASTALSNEQ QARRDCQEQA KIAVEAQNKY
     ERELMLHAAD VEALQAAKEQ VSKMASVRQH LEETTQKAES QLLECKASWE ERERMLKDEV
     SKCMSRCEDL EKQNRLLHDQ IEKLSDKVVA SVKEGVQGPL NVSLSEEGKS QEQILEILRF
     IRREKEIAET RFEVAQVESL RYRQRVELLE RELQELQDSL NAEREKVQVT AKTMAQHEEL
     MKKTETMNVV METNKMLREE KERLEQDLQQ MQAKVRKLEL DILPLQEANA ELSEKSGMLQ
     AEKKLLEEDV KRWKARNQHL VSQQKDPDTE EYRKLLSEKE VHTKRIQQLT EEIGRLKAEI
     ARSNASLTNN QNLIQSLKED LNKVRTEKET IQKDLDAKII DIQEKVKTIT QVKKIGRRYK
     TQYEELKAQQ DKVMETSAQS SGDHQEQHVS VQEMQELKET LNQAETKAKS LESQVENLQK
     TLSEKEAEAR NLQEQTVQLQ CELSRLRQDL QDRTTQEEQL RQQITEKEEK TRKAIVAAKS
     KIAHLAGVKD QLTKENEELK QRNGALDQQK DELDVRMTAL KSQYEGRISR LERELREHQE
     RHLEQRDEPQ EPTNKVPEQQ RQITLKTTPA SGERGIASTS DPPTANIKPT PVVSTPSKVT
     AAAMAGNKST PRASIRPMVT PATVTNPTTT PTATVMPTTQ VESQEAMQSE GPVEHVPVFG
     STSGSVRSTS PNVQPSIPQP ILTVQQQTQA TAFVQPTQQS HPQIEPANQE LSPNIVEVVQ
     SSPVERPSTS TAVFGTVSAT PSSSLPKRTR EEEEDSTIEA SDQVSDDTVE MPLPKKLKSV
     TPVGTEEEVM AEESTDGEVE TQVYNQDSQD SIGEGVTQGD YTPMEDSEET SQSLQIDLGP
     LQSDQQTTTS SQDGQGKGDD VIVIDSDDEE EDDDENDGEH EDYEEDEEDD DDDEDDTGMG
     DEGEDSNEGT GSADGNDGYE ADDAEGGDGT DPGTETEESM GGGESNQRAA DSQNSGEGNT
     GTAESSFSQD ISREQQPSSA SERQTPRAPQ SPRRPPHPLP PRLTIHAPPQ ELGPPVQRIQ
     MTRRQSVGRG LQLTPGIGGM QQHFFDDEDR TVPSTPTLVV PHRTDGFAEA IHSPQVAGVP
     RFRFGPPEDM PQTSSSHSDL GQLASQGGLG MYETPLFLAH EEESGGRSVP TTPLQVAAPV
     TVFTESTTSD ASEHASQSVP MVTTSTGTLS TTNETATGDD GDEVFVEAES EGISSEAGLE
     IDSQQEEEPV QASDESDLPS TSQDPPSSSS VDTSSSQPKP FRRVRLQTTL RQGVRGRQFN
     RQRGVSHAMG GRGGINRGNI N
//