PABP_USTMA
ID PABP_USTMA Reviewed; 651 AA.
AC Q4P8R9; A0A0D1CP36;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Polyadenylate-binding protein 1 {ECO:0000303|PubMed:19494833};
DE Short=PABP {ECO:0000250|UniProtKB:P04147};
DE AltName: Full=RNA-binding protein RRM12 {ECO:0000303|PubMed:15643068};
GN Name=PAB1 {ECO:0000303|PubMed:19494833};
GN Synonyms=RRM12 {ECO:0000303|PubMed:15643068}; ORFNames=UMAG_03494;
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021;
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021;
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=15643068; DOI=10.1128/ec.4.1.121-133.2005;
RA Becht P., Vollmeister E., Feldbruegge M.;
RT "Role for RNA-binding proteins implicated in pathogenic development of
RT Ustilago maydis.";
RL Eukaryot. Cell 4:121-133(2005).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19494833; DOI=10.1038/emboj.2009.145;
RA Koenig J., Baumann S., Koepke J., Pohlmann T., Zarnack K., Feldbruegge M.;
RT "The fungal RNA-binding protein Rrm4 mediates long-distance transport of
RT ubi1 and rho3 mRNAs.";
RL EMBO J. 28:1855-1866(2009).
RN [5]
RP FUNCTION, DOMAIN, SUBUNIT, INTERACTION WITH UPA1, AND SUBCELLULAR LOCATION.
RX PubMed=25985087; DOI=10.7554/elife.06041;
RA Pohlmann T., Baumann S., Haag C., Albrecht M., Feldbruegge M.;
RT "A FYVE zinc finger domain protein specifically links mRNA transport to
RT endosome trafficking.";
RL Elife 4:0-0(2015).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=28422978; DOI=10.1371/journal.pgen.1006734;
RA Haag C., Pohlmann T., Feldbruegge M.;
RT "The ESCRT regulator Did2 maintains the balance between long-distance
RT endosomal transport and endocytic trafficking.";
RL PLoS Genet. 13:e1006734-e1006734(2017).
RN [7]
RP FUNCTION, DOMAIN, SUBUNIT, INTERACTION WITH UPA2, AND SUBCELLULAR LOCATION.
RX PubMed=31338952; DOI=10.15252/embr.201847381;
RA Jankowski S., Pohlmann T., Baumann S., Muentjes K., Devan S.K., Zander S.,
RA Feldbruegge M.;
RT "The multi PAM2 protein Upa2 functions as novel core component of endosomal
RT mRNA transport.";
RL EMBO Rep. 20:e47381-e47381(2019).
CC -!- FUNCTION: RNA-binding protein involved in the formation of polar-
CC growing hyphae which is essential for infection by the plant pathogen
CC (PubMed:15643068). Component of endosomal mRNA transport that regulates
CC polarity of the infectious hyphae by transporting a broad spectrum of
CC cargo mRNAs from the nucleus to cell poles (PubMed:19494833,
CC PubMed:25985087, PubMed:31338952). {ECO:0000269|PubMed:15643068,
CC ECO:0000269|PubMed:19494833, ECO:0000269|PubMed:25985087,
CC ECO:0000269|PubMed:31338952}.
CC -!- SUBUNIT: Part of large ribonucleoprotein complexes (mRNPs) containing
CC RNA-binding proteins RRM4 and PAB1, endosome-binding protein UPA1, core
CC scaffold protein UPA2 and associated factor GRP1 (PubMed:25985087,
CC PubMed:31338952). Interacts (via PABC domain) with UPA1 (via PAM2
CC domain) (PubMed:25985087). Interacts (via PABC domain) with UPA2 (via
CC PAM2 domains) (PubMed:31338952). {ECO:0000269|PubMed:25985087,
CC ECO:0000269|PubMed:31338952}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19494833, ECO:0000269|PubMed:25985087,
CC ECO:0000269|PubMed:28422978}. Endosome {ECO:0000269|PubMed:19494833,
CC ECO:0000269|PubMed:25985087, ECO:0000269|PubMed:31338952}. Cytoplasm
CC {ECO:0000269|PubMed:31338952}. Note=Shuttles with endosomes along
CC microtubules. {ECO:0000269|PubMed:19494833,
CC ECO:0000269|PubMed:25985087, ECO:0000269|PubMed:28422978,
CC ECO:0000269|PubMed:31338952}.
CC -!- DOMAIN: The C-terminal PABC domain is involved in the interaction with
CC UPA1 and UPA2. {ECO:0000269|PubMed:25985087,
CC ECO:0000269|PubMed:31338952}.
CC -!- SIMILARITY: Belongs to the polyadenylate-binding protein type-1 family.
CC {ECO:0000305}.
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DR EMBL; CM003148; KIS68403.1; -; Genomic_DNA.
DR RefSeq; XP_011389943.1; XM_011391641.1.
DR AlphaFoldDB; Q4P8R9; -.
DR SMR; Q4P8R9; -.
DR IntAct; Q4P8R9; 1.
DR MINT; Q4P8R9; -.
DR STRING; 5270.UM03494P0; -.
DR PRIDE; Q4P8R9; -.
DR EnsemblFungi; KIS68403; KIS68403; UMAG_03494.
DR GeneID; 23563930; -.
DR KEGG; uma:UMAG_03494; -.
DR VEuPathDB; FungiDB:UMAG_03494; -.
DR eggNOG; KOG0123; Eukaryota.
DR HOGENOM; CLU_012062_22_4_1; -.
DR InParanoid; Q4P8R9; -.
DR OMA; ASPMEQK; -.
DR OrthoDB; 1027234at2759; -.
DR Proteomes; UP000000561; Chromosome 9.
DR GO; GO:0010494; C:cytoplasmic stress granule; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR006515; PABP_1234.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 4.
DR SUPFAM; SSF54928; SSF54928; 2.
DR SUPFAM; SSF63570; SSF63570; 1.
DR TIGRFAMs; TIGR01628; PABP-1234; 1.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 1: Evidence at protein level;
KW Cytoplasm; Cytoskeleton; Endosome; mRNA transport; Reference proteome;
KW Repeat; RNA-binding; Translation regulation; Transport.
FT CHAIN 1..651
FT /note="Polyadenylate-binding protein 1"
FT /id="PRO_0000295400"
FT DOMAIN 47..125
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 135..211
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 227..304
FT /note="RRM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 330..407
FT /note="RRM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 555..632
FT /note="PABC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00641"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..519
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 70488 MW; D33154CAAB235D83 CRC64;
MSSTESPVPA AAAPAEAVPA STPAPAAEQP AVGNGEQRNN ADAANNTSLY VGELDPSVTE
AMLFEIFSMI GTVASIRVCR DAVTRRSLGY AYVNFLNAAD GERAMEQLNY SLIRNRPCRI
MWSQRDPALR RTGQGNIFIK NLDAGIDNKA LHDTFAAFGN ILSCKVATNE TGSLGYGFVH
YETAEAAEAA IKHVNGMLLN DKKVYVGHHI PRKERQAKIE ETRANFTNVY AKNVDPEVTD
DEFEKLFTKF GKITSCVLQR DEDGKSKGFG FVNFEDHNEA QKAVDELHDS DFKGQKLFVA
RAQKKSEREE ELRRSYEAAK NEKLAKFQGV NLYLKNIPES YDDERLREEF APFGAITSCK
IMRAPSGVSR GFGFVCYSAP EEANKAVSEM NGKMLDNRPL YVALAQRKDV RRQQLEAQIM
QRNQLRLQQQ AAAQGMGYPG PGMYYPQPGA FPGQPGGMVP RPRYAPAGMM PQGMPMAPYG
QPGQFPAGMM PQGYRPARPP RGAPNAAGGP APPAGARPPT GVNGAPRPAG QPVPGQPMPR
GPAARPAGRP EADQPGALTA AALAKASPEE QKQMLGEAIY PKVAASQPEL AGKLTGMILE
LPVTELLHLL EESEALDAKV NEALEVLKEY QQNDSAGAEA EANAEAPKTE A
