ID A0A286ZJ74_PIG Unreviewed; 2518 AA.
AC A0A286ZJ74;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Nucleoprotein TPR {ECO:0000256|ARBA:ARBA00019789};
GN Name=TPR {ECO:0000313|Ensembl:ENSSSCP00000031528.1,
GN ECO:0000313|VGNC:VGNC:108623};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000031528.1, ECO:0000313|Proteomes:UP000008227};
RN [1] {ECO:0000313|Ensembl:ENSSSCP00000031528.1, ECO:0000313|Proteomes:UP000008227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000031528.1,
RC ECO:0000313|Proteomes:UP000008227};
RG Porcine genome sequencing project;
RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSSCP00000031528.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TPR family. {ECO:0000256|ARBA:ARBA00005274}.
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DR SMR; A0A286ZJ74; -.
DR STRING; 9823.ENSSSCP00000031528; -.
DR PaxDb; 9823-ENSSSCP00000016515; -.
DR Ensembl; ENSSSCT00000056338.3; ENSSSCP00000031528.1; ENSSSCG00000015576.5.
DR VGNC; VGNC:108623; TPR.
DR GeneTree; ENSGT00730000111014; -.
DR InParanoid; A0A286ZJ74; -.
DR Reactome; R-SSC-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-SSC-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-SSC-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR Reactome; R-SSC-191859; snRNP Assembly.
DR Reactome; R-SSC-3301854; Nuclear Pore Complex (NPC) Disassembly.
DR Reactome; R-SSC-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SSC-5578749; Transcriptional regulation by small RNAs.
DR Proteomes; UP000008227; Chromosome 9.
DR Bgee; ENSSSCG00000015576; Expressed in mesenteric lymph node and 42 other cell types or tissues.
DR ExpressionAtlas; A0A286ZJ74; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005868; C:cytoplasmic dynein complex; 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 signaling; 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 formation; 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 Gene3D; 1.10.287.1490; -; 2.
DR InterPro; IPR012929; TPR/MLP1.
DR PANTHER; PTHR18898:SF2; NUCLEOPROTEIN TPR; 1.
DR PANTHER; PTHR18898; NUCLEOPROTEIN TPR-RELATED; 1.
DR Pfam; PF07926; TPR_MLP1_2; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A286ZJ74};
KW Reference proteome {ECO:0000313|Proteomes:UP000008227}.
FT DOMAIN 1194..1321
FT /note="Nucleoprotein TPR/MLP1"
FT /evidence="ECO:0000259|Pfam:PF07926"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1066..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1774..1829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1958..2289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2382..2518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..327
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 374..436
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 494..521
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 582..668
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 698..751
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 820..956
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 982..1023
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1376..1571
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 10..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1774..1791
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1792..1829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1958..1982
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2035..2053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2060..2093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2100..2140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2155..2169
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2176..2223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2226..2245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2382..2414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2451..2480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2518 AA; 282921 MW; B69DA125D383F6BD CRC64;
MMSTVWRHLA DKWSRGRRGK SGGGEKEEGR GGAELGTRRN QKNYSSQRPA RRDVGGEESR
KEEGRTGSEA ASEPGFPGCT ASGGGRGRCG AFGAAANAGL GFPGSRRGSL RRAGAREPPS
EAAEAAAQAS GSSWSSSFIV SAPSAPGAAV PGPFDMAAVL QQVLERAELN KLPKSVQNKL
EKFLADQQSE IDGLKGRHEK FKVESEQQYF EIEKRLSHSQ ERLVNETREC QSLRLELEKL
NNQLKALTEK NKELEVAQDR SIAIQSQFTR TKEELEAEKR DLIRTNERLS QELEYLTEDV
KRLNEKLKES NATKGELQLK LDELQASDVS VKYREKRLEQ EKELLHNQNT WLNTELKTKT
DELLALGREK GNEILELKCN LENKKEEVSR MEEQMNGLKT SNENLQKHVE DLLTKLKEAK
EQQASMEEKF HNELNAHIKL SNLYKSAADD SEAKSNELTR AVDELHKLLK EAGEANKAIQ
DHLLEVEESK GQMEKEMLEK IGKLEKELEN ANDLLSATKR KGAILSEEEL AAMSPTAAAV
AKIVKPGMKL TELYNAYVET QDQLLLEKLE NKRINKYLDE IVKEVEAKAP ILKRQREEYE
RAQKAVASLS VKLEQAMKEI QRLQEDTDKA NKHSSVLERD NQRMEIQIKD LSQQIRVLLM
ELEEARGNHV IRDEEVSSAD ISSSSEVISQ HLVSYRNIEE LQQQNQRLLV ALRELGETRE
REEQETTSSK ITELQLKLES ALTELEQLRE SRQHQMHLVD SIVRQRDMYR ILLSQTTGVV
IPLQASGLED ISLVSTPKRS STSQTVSTPA SVPVIESAEA IEAKAALKQL QEIFENYKKE
KADNEKMQNE QLEKLQEQVT DLRSQNTKIS TQLDFASKRY EMLQDNVEGY RREITSLHER
NQKLTATTQK QEQIINTMTQ DLRGANEKLA VAEVRAENLK KEKEMLKLSE VRLSQQRESL
LAEQRGQNLL LTNLQTIQGI LERSETETKQ RLSNQIEKLE HEISHLKKKL ENEVEQRHTL
TRNLDVQLLD TKRQLDTETN LHLNTKELFK NAQKEIATLK QHLSNMEAQL ASQSSQRSGK
GQPSNKEDMD DLLSQLRQAE EQVNDLKERL KTSTSNVEQY RAMVTSLEES LNKEKQVAEE
VHKNIEVRLK ESAEFQTQLE KKLMEVEKEK QELQDDKRKA IESMEQQLSE LKKTLSSVQS
EVQEALQRAG TALSNEQQAR RDCQEQAKIA VEAQNKYERE LMLHAADVEA LQAAKEQVSK
MASVRQHLEE TTQKAESQLL ECKASWEERE RMLKDEVSKC VSRCEDLEKQ NRLLHDQIEK
LSDKVVASVK EGIQGPLNVS ISEEGKSQEQ ILEILRFIRR EKEIAETRFE VAQVESLRYR
QRVELLEREL QELQDSLNAE REKVQVTAKT MAQHEELMKK TETMNVVMET NKMLREEKER
LEQDLQQMQA KVRKLELDIL PLQEANAELS EKSGMLQAEK KLLEEDVKRW KARNQHLISQ
QKDPDTEEYR KLLSEKEVHT KRIQQLTEEI GRLKAEIARS NASLTNNQNL IQSLKEDLNK
VRTEKESIQK DLDAKIIDIQ EKVKTITQVK KIGRRYKTQY EELKAQQDKV METSAQSSGD
HQEQHVSVQE MQELKEALNQ AEAKSKSLES QVENLQKTLS EKEMEARNLQ EQTVQLQSEL
SRLRQDLQDR TTQEEQLRQQ ITEKEEKTRK AIVAAKSKIA HLAGVKDQLT KENEELKQRN
GALDQQKDEL DVRMTALKSQ YEGRISRLER ELREHQERHL EQRDEPQEPT NKVPEQQRQI
TLKTTPASGE RGIASTSDPP TANIKPTPVV STPSKVTAAA MAGNKSTPRA SIRPMVTPAT
VTNPTTTPTA TVMPTTQVES QEAMQSEGPV EHVPVFGSTS GSVRSTSPNV QPSIPQPILT
VQQQTQATAF VQPTQQSHPQ IEPTNQELSP NIVEVVQSSP VERPSTSTAV FGTVSATPSS
SLPKRTREEE EDSTIEASDQ ISDDTVEMPL PKKLKSVTPV GTEEEVMAEE STDGEVETQV
YNQDSQDSIG EGVTQGDYTP MEDSEETSQS LQIDLGPLQS DQQTTTSSQD GQGKGDDVIV
IDSDDEEEDD DENDGEHEDY EEDEEDDDDD EDDTGMGDEG EDSNEGTGSA DGNDGYEADD
AEGGDGTDPG TETEESMGGG ESNQRAADSQ NSGEGNTGTA ESSFSQEISR EQQPSSASER
QAPRAPQSPR RPPHPLPPRL TIHAPPQELG PPVQRIQMTR RQSVGRGLQL TPGIGGMQQH
FFDDEDRTVP STPTLVVPHR TDGFAEAIHS PQVAGVPRFR FGPPEDMPQT SSSHSDLGQL
ASQGGLGMYE TPLFLAHEEE SGGRSVPTTP LQVAAPVTVF TESTTSDASE HASQSVPMVT
TSTGTLSTTN ETAAGDDGDE VFVEAESEGI SSEAGLEIDS QQEEEPVQAS DESDLPSTSQ
DPPSSSSVDT SSSQPKPFRR VRLQTTLRPG VRGRQFNRQR GVSHAMGGRG GINRGNIN
//
