TPR1_SCHPO
ID TPR1_SCHPO Reviewed; 1039 AA.
AC O42668; O42796;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Tetratricopeptide repeat protein 1;
GN Name=tpr1; ORFNames=SPAC27D7.14c, SPAC637.02c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10471809; DOI=10.1016/s0014-5793(99)01068-6;
RA Lichtenberg H., Heyer M., Hoefer M.;
RT "Tpr1, a Schizosaccharomyces pombe protein involved in potassium
RT transport.";
RL FEBS Lett. 457:363-368(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930; SER-932; SER-959;
RP SER-961; SER-964 AND SER-998, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Involved in promoting potassiumm ion uptake.
CC {ECO:0000269|PubMed:10471809}.
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DR EMBL; AF047464; AAC03120.1; -; mRNA.
DR EMBL; CU329670; CAA15833.1; -; Genomic_DNA.
DR PIR; T38447; T38447.
DR PIR; T43678; T43678.
DR RefSeq; NP_594620.1; NM_001020048.2.
DR AlphaFoldDB; O42668; -.
DR SMR; O42668; -.
DR BioGRID; 278554; 17.
DR STRING; 4896.SPAC27D7.14c.1; -.
DR TCDB; 8.A.13.1.1; the tetratricopeptide repeat (tpr1) family.
DR iPTMnet; O42668; -.
DR MaxQB; O42668; -.
DR PaxDb; O42668; -.
DR PRIDE; O42668; -.
DR EnsemblFungi; SPAC27D7.14c.1; SPAC27D7.14c.1:pep; SPAC27D7.14c.
DR GeneID; 2542077; -.
DR KEGG; spo:SPAC27D7.14c; -.
DR PomBase; SPAC27D7.14c; tpr1.
DR VEuPathDB; FungiDB:SPAC27D7.14c; -.
DR eggNOG; KOG2002; Eukaryota.
DR HOGENOM; CLU_003008_0_1_1; -.
DR InParanoid; O42668; -.
DR OMA; MSNCIEI; -.
DR PhylomeDB; O42668; -.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR PRO; PR:O42668; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0016593; C:Cdc73/Paf1 complex; IPI:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000993; F:RNA polymerase II complex binding; IBA:GO_Central.
DR GO; GO:0016570; P:histone modification; IEA:InterPro.
DR GO; GO:0006813; P:potassium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006362; P:transcription elongation from RNA polymerase I promoter; ISS:PomBase.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; ISS:PomBase.
DR Gene3D; 1.25.40.10; -; 5.
DR InterPro; IPR031101; Ctr9.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14027; PTHR14027; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 10.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF48452; SSF48452; 3.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 3.
PE 1: Evidence at protein level;
KW Coiled coil; Ion transport; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Repeat; TPR repeat; Transport.
FT CHAIN 1..1039
FT /note="Tetratricopeptide repeat protein 1"
FT /id="PRO_0000106375"
FT REPEAT 51..84
FT /note="TPR 1"
FT REPEAT 175..208
FT /note="TPR 2"
FT REPEAT 210..243
FT /note="TPR 3"
FT REPEAT 251..288
FT /note="TPR 4"
FT REPEAT 326..359
FT /note="TPR 5"
FT REPEAT 361..393
FT /note="TPR 6"
FT REPEAT 437..469
FT /note="TPR 7"
FT REPEAT 514..547
FT /note="TPR 8"
FT REPEAT 634..667
FT /note="TPR 9"
FT REPEAT 701..734
FT /note="TPR 10"
FT REPEAT 737..770
FT /note="TPR 11"
FT REPEAT 799..832
FT /note="TPR 12"
FT REGION 912..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 838..929
FT /evidence="ECO:0000255"
FT COMPBIAS 912..941
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 953..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1030
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 959
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 964
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 124..127
FT /note="YLEA -> NLGG (in Ref. 1; AAC03120)"
FT /evidence="ECO:0000305"
FT CONFLICT 195..196
FT /note="LK -> FR (in Ref. 1; AAC03120)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1039 AA; 119151 MW; 81363F2E45C391BC CRC64;
MEGFTLETHA SRIIEVPLLG QEDQSVEIDC SSLPSDATEL CEILVNEQAP REFWTKFAHE
YYIRGLREQA ILILKSGLET LKDSESLCIL NANIAAIYLS MAREAMLKKD TDLRDEQLRN
VRTYLEAANN IDSKSEINVL LHGIYRILLN PTDKESLENA ARCFDFVLQK SGGNILGFLG
KARILYAKGN YRSALKLYQR ALVSNPQFKP DPRIGIGLCF WNLDMKTDAL SAWTRVQQLD
PKNTVVDTYI GLYYYDLAFQ NVNNDSFVQN YGKALQHIQR AFKTRNNDPV ASSILERYVY
SKKNYEGCIK LAENVIQNSF SSSLIADGYY WMGRAYHQMG NNEKAMASYQ KAKAADDRHL
LSSVGIGQIQ ILQNDLTSAK LTFERIAEQN QSCFEALVVL GCLHASDSKP DLTKARMLLD
RAFNLVGSSK LPRVVDSDLY ITQARLWEKE DTKKSLGFLT RALDFLESAH MSVGPELLNN
IAVLQYHLGL IPEAHGNIIK AKSVLPDANP ELSLLLDYNL ARCEEELGNT SVASEAYVSI
LEKHPSFIDA RIRKCLLQLS NPNEETFKEI RHIMNADSQN LEVRAFFGWY LSKQKRRPVE
DPEVRHCSQT LRHWHDDIYS LVQLGNAYMR QAREFRVHND REKLKRQKLY IKAIQSYDQA
IKFDPKNAHA AQGIAIILAQ NRQFSKALLI LSKVREAIKD ATTLINIGNC LAELKQFSRA
IEVFETVYSS TGESDTYGVL SCLGRVWLQR GRESKNVDYL KESVRYATLA LEKNPENPSL
LFNVAFVQFQ LCELIRQKPE NSRTVEDLNF AMQQLDASIE TFTKLVSVEH PPYSPTSIEQ
RAKMAKNTTK RQLERAIQAQ IEYEKSVAAK LEDARIQREK EKARRLAEEE ALLKEKQERE
RQLQEERQKM QEEVLEWRKS QQKASEDDMS LSDDEEKQSG KKKKKDRKKR KSKSKQESSD
SGVSEDDEIP LSDARNKTKK RRVNRRVISE EYTFDQDSDA EGNQEEEVSR TIEEKQDNDI
TDNQDDNKEL NLFSEEDEE
