PBP1_TRYB2
ID PBP1_TRYB2 Reviewed; 550 AA.
AC Q57UZ7; D6XLI9;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=PAB1-binding protein 1 {ECO:0000303|PubMed:24470144};
DE AltName: Full=Ataxin-2 homolog {ECO:0000305};
DE AltName: Full=Poly(A)-binding protein-binding protein {ECO:0000305};
GN Name=PBP1 {ECO:0000303|PubMed:24470144};
GN ORFNames=Tb927.8.4540 {ECO:0000312|EMBL:AAX70572.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000312|Proteomes:UP000008524};
RN [1] {ECO:0000312|EMBL:AAZ13219.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|EMBL:AAZ13219.1};
RX PubMed=16020724; DOI=10.1126/science.1112181;
RA El-Sayed N.M., Myler P.J., Blandin G., Berriman M., Crabtree J.,
RA Aggarwal G., Caler E., Renauld H., Worthey E.A., Hertz-Fowler C.,
RA Ghedin E., Peacock C., Bartholomeu D.C., Haas B.J., Tran A.N.,
RA Wortman J.R., Alsmark U.C., Angiuoli S., Anupama A., Badger J.,
RA Bringaud F., Cadag E., Carlton J.M., Cerqueira G.C., Creasy T.,
RA Delcher A.L., Djikeng A., Embley T.M., Hauser C., Ivens A.C.,
RA Kummerfeld S.K., Pereira-Leal J.B., Nilsson D., Peterson J., Salzberg S.L.,
RA Shallom J., Silva J.C., Sundaram J., Westenberger S., White O.,
RA Melville S.E., Donelson J.E., Andersson B., Stuart K.D., Hall N.;
RT "Comparative genomics of trypanosomatid parasitic protozoa.";
RL Science 309:404-409(2005).
RN [2] {ECO:0000312|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [3] {ECO:0000305}
RP FUNCTION, INTERACTION WITH MKT1 AND ZC3H11, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=427 {ECO:0000303|PubMed:24470144};
RX PubMed=24470144; DOI=10.1093/nar/gkt1416;
RA Singh A., Minia I., Droll D., Fadda A., Clayton C., Erben E.;
RT "Trypanosome MKT1 and the RNA-binding protein ZC3H11: interactions and
RT potential roles in post-transcriptional regulatory networks.";
RL Nucleic Acids Res. 42:4652-4668(2014).
RN [4] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH LSM12; XAC1 AND MKT1 OR MKT1L, INTERACTION
RP WITH PBP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=427 {ECO:0000303|PubMed:32532821};
RX PubMed=32532821; DOI=10.1074/jbc.ra120.013306;
RA Melo do Nascimento L., Terrao M., Marucha K.K., Liu B., Egler F.,
RA Clayton C.;
RT "The RNA-associated proteins MKT1 and MKT1L form alternative PBP1-
RT containing complexes in Trypanosoma brucei.";
RL J. Biol. Chem. 295:10940-10955(2020).
CC -!- FUNCTION: Involved in post-transcriptional regulation of gene
CC expression (PubMed:24470144). Promotes mRNA stabilization by bridging
CC poly(A)-binding protein to mRNAs (PubMed:24470144).
CC {ECO:0000269|PubMed:24470144}.
CC -!- SUBUNIT: Forms a complex composed of at least MKT1, PBP1, XAC1 and
CC LSM12 (PubMed:32532821). Forms a complex composed of at least MKT1L,
CC PBP1, XAC1 and LSM12 (PubMed:32532821). Within the complex, interacts
CC with MKT1 (via C-terminus); the interaction is direct (PubMed:24470144,
CC PubMed:32532821). Interacts (via C-terminus) with ZC3H11; the
CC interaction is direct (PubMed:24470144). {ECO:0000269|PubMed:24470144,
CC ECO:0000269|PubMed:32532821}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:24470144}.
CC Cytoplasm, Stress granule {ECO:0000269|PubMed:24470144}. Note=Localizes
CC to polysomes (PubMed:24470144). Localizes to starvation-induced stress
CC granules but not heat shock-induced stress granules (PubMed:24470144).
CC {ECO:0000269|PubMed:24470144}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the procyclic and bloodstream forms
CC (at protein level). {ECO:0000269|PubMed:24470144}.
CC -!- SIMILARITY: Belongs to the ataxin-2 family. {ECO:0000305}.
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DR EMBL; AC159448; AAX70572.1; -; Genomic_DNA.
DR EMBL; CP000071; AAZ13219.1; -; Genomic_DNA.
DR RefSeq; XP_847285.1; XM_842192.1.
DR AlphaFoldDB; Q57UZ7; -.
DR STRING; 5691.AAZ13219; -.
DR PaxDb; Q57UZ7; -.
DR GeneID; 3659452; -.
DR KEGG; tbr:Tb927.8.4540; -.
DR VEuPathDB; TriTrypDB:Tb927.8.4540; -.
DR eggNOG; KOG2375; Eukaryota.
DR InParanoid; Q57UZ7; -.
DR OMA; TRNLQHR; -.
DR Proteomes; UP000008524; Chromosome 8.
DR GO; GO:0005737; C:cytoplasm; IDA:GeneDB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IDA:GeneDB.
DR GO; GO:0140517; F:protein-RNA adaptor activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0048255; P:mRNA stabilization; IDA:UniProtKB.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:GeneDB.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR GO; GO:0034063; P:stress granule assembly; IBA:GO_Central.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR025852; SM_dom_ATX.
DR PANTHER; PTHR12854; PTHR12854; 1.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Reference proteome; Translation regulation.
FT CHAIN 1..550
FT /note="PAB1-binding protein 1"
FT /id="PRO_0000451927"
FT REGION 201..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..283
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..506
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 550 AA; 59599 MW; 7142DE319D2B4CCF CRC64;
MEGSHSSNME RLEYLYLNLV GQVVQVRLVD DMCVEGLFVA CTDVDAETDA GIMICCTRNL
ASAKRSPLSP SCVNFTDDLF IPYQSIVMIE VQNAKIRTET PGRPDTGRAD FSATKFDWAD
DGVSELLESE PHQTGTWNQF EANEKSFGVK TTYKEEFYTT RLDHSKITEE QRAQADRLAR
EIESSSTRGI AHRMEREECL HDDEGLDEGQ LYSDVHRPQE KKPPYVPPST GGRKLVNEPP
PVPAAAAPAT APTTAPAAAP APAAAPPAAA PAAAAPPPPP AATSMADDGS MRHKRMNEDP
HHMQYDANQT AAGFNPAAAP YTPMKPGAAV PVVDFLASLA DAISNNDMCY DCEPHWPGMC
NLFYDQDDSS YSQQNYEAAA MPPSHSMNMH MYVNSQPNIP NAHRGYQGPL GRVPHNQSMP
MHHMQGQGFH HEMHHHQAFH GMGNYSSQHH NPPIQEYAPH KGQQGVVSRP GMRQGKGGGA
SRVEPQQPVS ANTASSPPPV PTVDSAPNEV KPPAKLQRGR GMAAFTKGDM DGDSGATTNA
TGGPKKRVGK
