ID H0WA32_CAVPO Unreviewed; 2320 AA.
AC H0WA32;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Nucleoprotein TPR {ECO:0000256|ARBA:ARBA00019789};
GN Name=TPR {ECO:0000313|Ensembl:ENSCPOP00000019843.2};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000019843.2, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000019843.2}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000019843.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TPR family. {ECO:0000256|ARBA:ARBA00005274}.
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DR EMBL; AAKN02018444; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02018445; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 10141.ENSCPOP00000019843; -.
DR Ensembl; ENSCPOT00000022818.2; ENSCPOP00000019843.2; ENSCPOG00000019790.2.
DR VEuPathDB; HostDB:ENSCPOG00000019790; -.
DR eggNOG; KOG4674; Eukaryota.
DR GeneTree; ENSGT00730000111014; -.
DR HOGENOM; CLU_001059_0_0_1; -.
DR InParanoid; H0WA32; -.
DR OMA; HAQQNYE; -.
DR TreeFam; TF350364; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000019790; Expressed in heart left ventricle and 12 other cell types or tissues.
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: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; IEA:Ensembl.
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: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; IEA:Ensembl.
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 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447}.
FT DOMAIN 996..1123
FT /note="Nucleoprotein TPR/MLP1"
FT /evidence="ECO:0000259|Pfam:PF07926"
FT REGION 1413..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1576..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1761..2093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2184..2320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..180
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 234..296
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 336..381
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 442..528
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 558..618
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 680..816
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 842..883
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 954..1028
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1053..1126
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1178..1373
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1576..1593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1761..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1862..1895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1902..1942
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1957..1971
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1978..2027
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2028..2047
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2184..2217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2253..2281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2320 AA; 262403 MW; 1DAE7D220782D993 CRC64;
SALSAAVVAP RRLGDMAAVL QQVLERTELN KLPKLVQNKL EKFLADQQSE IDGLKGRHEK
FKVESEQQYF EIEKRLSHSQ ERLVNETREC QSLRLELEKL NNQLKTLTEK NRELEIAQDR
SITVQSQFTR TKEELEAEKR DLIRTNERLS QELEYLTEDV KRLNEKFKES NATKGELQLK
LDELQASDVS IKYREKRLEQ EKELLHNQNT WLNTELKTKT DELLALGREK GNEILELKCN
LENKKEEVSR LEEQMNGLKT SNEHLQKHVE DLLTKLKEAK EQQASMEEKF HNELNAHIKL
SNLYKSAADD SEAKSNELTR AVDELHKLLK DAGEANKAIQ DHLLEVEASK DQMEKEMLEK
IGKLEKELEN ANDLLSATKR KGAVLSEEEL AAMSPTAAAV AKIVKPGMKL TELYNAYVET
QDQLLLEKLE NKRINKYLDE IVKEVEAKAP ILKRQREEYE RAQKAVASLS AKLEQAMKEI
QRLQEDTDKA HKHSSVLERD NQRMEIQIKD LSQQIRVLLM ELEEARGNHV IRDEEVSSAD
ISSSSEVISQ HLVSYRNIEE LQQQNQRLLV ALRELGETRE KEEQETTSSK ITELQVKLES
ALTELEQLRE SRQHQMQLVD SIVRQRDMYR ILLSQTTGVV IPLQASSLDD ISIVSTPKRS
STSHTTSTPA PVPVIESPEA IEAKAALKQL QEIFENYKKE KTDNEKIQNE QLEKLQEQVT
DLRSQNTKIS TQLDFASKRY EMLQDNVEGY RREITSLQER NQKLTATTQK QEQIINTMTQ
DLRGANEKLA VAEVRAENLK KEKEMLKLSE VRLSQQRESL LAEQRGQNLL LTNLQTIQGI
LERSETETKQ RLSTQIEKLE HEISHLKKKL ENEVEQRHTL TRNLDVQLLD TKRQLDTETN
LHFNTKELLK NAQKEIATLK QYLSNMETQL ASQSSQRTGK EEVRKNIEVR LKESAEFQMQ
LEKKLMEVEK EKQELQDDKR KAIESMEQQL SELRKTLSSV QNEVQEALQR ASTALSNEQQ
ARRDCQEQAK IAVEAQNKYE RELMLHAADV EALQAAKEQV SKMASVRQHL EETTQKAESQ
LLECEASWEE RERMLKDEVA KCVSRCEDLE KQNRLLHDQI ENLSDKVVAS MKEGVQGTLN
VSLNEEGKSQ EQILEILRFI RREKEIAETR FEVAQVESLR YRQRVELLER ELQELQDSLN
AEREKVQVTA KTMAQHEELM KKTETMNVVM ETNKMLREEK ERLEQDLQQM QAKVRKLELD
ILPLQEANAE LSEKSGMLQA EKKLLEEDVK RWKARNQHLV NQQKDPDAEE YRKLLSEKEV
HTKRIQQLTE DVARLKAEIA RSNASLTNNQ NLIQSLKEDL NKVKTEKESI QKDLDAKIID
IQEKVKTITQ VKKIGRRYKT QYEELKAQQD KVLETSTQSS GDHQEQHVSV QEMQELKDTL
NQAETKSKSL ESQVDNLQKT LSEKETEARN LQEQTVQLQS ELTRLRQDLQ DRTTQEEQLR
QQITEKEEKT RKAIVAAKSK IAHLAGVKDQ LTKENEELKQ RNGALDQQKD ELDVRMTALK
SQYEGRISRL ERELREHQER HLEQRDEPQE PTSKVPEQQR QITLKTTPAS GERGIASTSD
PPTANIKPTP VVSTPSKVTA AAMAGNKSTP RASIRPMVTP ATVTNPTTTP TATVMPTTQV
ESQEAMQSEG PVEHVPVFGS TSGSVRSTSP NVQPSISQPI LTVQQQTQAT AFVQPTQQSH
PQIEPANQEL SPNIVEVVQS SPVERPSTST AVFGTVSATP SSSLPKRTRE EEEDNTIEAS
DQVSDDTVEM PLPKRLKTVT PVGTEEEVMA EESTDGEVET QVYNQDSQDS IGEGVTQGDY
TPIEDSEETS QSLQIDLGPL QPDQQTTTSS QDGQGKGDDV IVIDSDDEEE DDDENDGEHE
DYEEDEDDDD DDEDDTGMGD EGEDSNEGTG SADGNDGYEA DDAEGGDGTD PGTETEESMG
GGESNQRAAD SQNSGEGNSS TAESSFSQEI SREQQPSSAS ERQTPRAPQS PRRPPHPLPP
RLTIHAPPQE LGPPVQRIQM TRRQSVGRGL QLTPGIGGMQ QHFFDDEDRT VPSTPTLVVP
HRTDGFAEAI HSPQVAGVPR FRFGPPEDMP QTSSSHSDLG QLASQGGLGM YETPLFLAHE
EESGGRSVPT TPLQVAAPVT VFTESTTSDT SEHASQSVPM VTTSTGTLST TNETATGDDG
DEVFVEAESE GISSEAGLEI DSQQEEEPVQ ASDESDLPST SQDPPSSSSV DTSSSQPKPF
RRVRLQTALR QGVRSRQFNR QRGISHAVGG RGGINRGNIN
//
