ID   UPA2_USTMA              Reviewed;        2121 AA.
AC   A0A0D1DRJ3;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2015, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=PAM2 domain-containing protein UPA2 {ECO:0000303|PubMed:31338952};
GN   Name=UPA2 {ECO:0000303|PubMed:31338952}; ORFNames=UMAG_10350;
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, DOMAIN, INTERACTION WITH PAB1, DISRUPTION PHENOTYPE, SUBCELLULAR
RP   LOCATION, AND MUTAGENESIS OF 2118-GLY--TRP-2120.
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: Core component of endosomal mRNA transport and appears to
CC       carry out crucial scaffolding functions (PubMed:31338952). The
CC       endosomal mRNA transport regulates polarity of the infectious hyphae by
CC       transporting a broad spectrum of cargo mRNAs from the nucleus to cell
CC       poles (PubMed:31338952). {ECO:0000269|PubMed:31338952}.
CC   -!- SUBUNIT: Might form homodimers via its C-terminal coiled-coil domain
CC       (Probable). Part of large ribonucleoprotein complexes (mRNPs)
CC       containing RNA-binding proteins RRM4 and PAB1, endosome-binding protein
CC       UPA1, core scaffold protein UPA2 and associated factor GRP1
CC       (PubMed:31338952). Interacts (via PAM2 motifs) with PAB1
CC       (PubMed:31338952). {ECO:0000269|PubMed:31338952,
CC       ECO:0000305|PubMed:31338952}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000269|PubMed:31338952}. Endosome {ECO:0000269|PubMed:31338952}.
CC       Note=Shuttles with RRM4-positive transport endosomes along microtubules
CC       (PubMed:31338952). Rhe endosomal localization depends on the RNA-
CC       binding capacity of RRM4 (PubMed:31338952).
CC       {ECO:0000269|PubMed:31338952}.
CC   -!- DOMAIN: The PAM2 motifs are involved in the binding to PAB1.
CC       {ECO:0000269|PubMed:31338952}.
CC   -!- DOMAIN: The effector domain (residues 339 to 599) is important for
CC       endosomal mRNA transport. {ECO:0000269|PubMed:31338952}.
CC   -!- DOMAIN: The C-terminal coiled-coil domain might be involved in
CC       dimerization. {ECO:0000305|PubMed:31338952}.
CC   -!- DOMAIN: the conserved C-terminal GWW motif is essential for endosomal
CC       localization andwhich in turn is important for the function of the
CC       protein. {ECO:0000269|PubMed:31338952}.
CC   -!- DISRUPTION PHENOTYPE: Causes defects in the formation of endosomal
CC       mRNPs and exhibits a bipolar growth phenotype.
CC       {ECO:0000269|PubMed:31338952}.
CC   -!- SIMILARITY: Belongs to the UPA1 PAM2 domain-binding protein family.
CC       {ECO:0000305}.
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DR   EMBL; CM003157; KIS66526.1; -; Genomic_DNA.
DR   RefSeq; XP_011391917.1; XM_011393615.1.
DR   SMR; A0A0D1DRJ3; -.
DR   EnsemblFungi; KIS66526; KIS66526; UMAG_10350.
DR   GeneID; 23566393; -.
DR   KEGG; uma:UMAG_10350; -.
DR   VEuPathDB; FungiDB:UMAG_10350; -.
DR   eggNOG; ENOG502SDVW; Eukaryota.
DR   OrthoDB; 105076at2759; -.
DR   Proteomes; UP000000561; Chromosome 18.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Cytoskeleton; Endosome; mRNA transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..2121
FT                   /note="PAM2 domain-containing protein UPA2"
FT                   /id="PRO_0000454341"
FT   REGION          14..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..302
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          339..599
FT                   /note="Effector domain"
FT                   /evidence="ECO:0000269|PubMed:31338952"
FT   REGION          375..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          475..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..543
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..819
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          950..1012
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1076..1096
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1119..1261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1337..1369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2099..2121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1783..2054
FT                   /evidence="ECO:0000305|PubMed:31338952"
FT   MOTIF           1..17
FT                   /note="PAM2 1"
FT                   /evidence="ECO:0000303|PubMed:31338952"
FT   MOTIF           858..874
FT                   /note="PAM2 2"
FT                   /evidence="ECO:0000303|PubMed:31338952"
FT   MOTIF           920..937
FT                   /note="PAM2 3"
FT                   /evidence="ECO:0000303|PubMed:31338952"
FT   MOTIF           1046..1063
FT                   /note="PAM2 4"
FT                   /evidence="ECO:0000303|PubMed:31338952"
FT   MOTIF           2118..2120
FT                   /note="GWW"
FT                   /evidence="ECO:0000269|PubMed:31338952"
FT   COMPBIAS        266..280
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        598..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..648
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        657..690
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        691..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        712..728
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        770..789
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        966..992
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1092
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1129..1146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1157..1185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1196..1210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1225..1248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1341..1367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         2118..2120
FT                   /note="GWW->AAA: Resulted in loss of shuttling."
FT                   /evidence="ECO:0000269|PubMed:31338952"
SQ   SEQUENCE   2121 AA;  231852 MW;  2C117BEC8AC11A1F CRC64;
     MEGSSLNVAA PVFKPSGAAN SFTPAPSQPA PPTLLSSSGP DAAVHAPDHL SPSTMLSQIQ
     NQMASGGGVP GGMIHMNASS RPFVPGTAVK PSIVEPPTPI PYHPPLSSFA NASRSPVPQH
     RLGHALNPGS VQLTGLPTFL ATPPVINHMP HMSRSPSYTG PPSPISPNFS GAASPFVMPP
     AQMSYGLPLP AGLMNGNMKP RRAKGLPPVT PLKTTGHNST PSISMNPAAF AANLAALKAR
     KKVVVCLPAE QLLPDDEALL AQPEDESLGE EVKSDVDGVE TGARASEPGS AKSRHARASA
     LTRSRWVQRQ PLSSDKHDLV PFFEAPREEI VTCDIHPEPW PYSLGLPDTI EIYLPGMSAW
     DEYLELRYEE QQMEAATTDH EPRSPLAHQG IPLPPSTAGF TFDRRGRSLS ISTPADPGMV
     TFKLNRFLES QQQQLSQYDS DQVCGLDSAQ NFGDADKPFG RFQTDLPNRL REAFARRRGD
     SSDLNLRPSL KTTHNHTMSL GLPSSGGPFG PEVFSALDMI RANSDEGPSK PPSEAQDLPQ
     KPLSDTEAFA GKSEIYLSNI AEEDGEQEPS AELAVEGHTR VGSWKDLGRG FGYEPQSPNA
     APNGTTSKHV RQASRFSVNT SRHDGEENDE LGFDGEEAEI RTNPSEDADA SDFEEEPNEY
     GADHWRSRHN SVHLSAFGDG HDRYADDNQS HASNDDSLQD SLTPSDEQFS NPSDEEAARE
     ERILRRQHRA AERAARRERK QRQRGRAYSD NTLPSSSIGE ADIHHNGVYG QDEQQRNPRN
     GNTISNPSEQ EHCDIDDDSQ TFGHNDRSNM PDQGPQFSRD FRFPPLNPCT VDVDPQVQSS
     SVHSGNCPPM SGTLGRASGI SLLNPDAKEF KFGGTSASTR SVSAPQPSMQ TAPEAAGAHF
     RLPSIKTSSF GSSALGDAPT NAAHLNVGAA PFTPGLFTFK AIQRLQVPEN SLSASPSIAV
     TSADGGADHR ETENRDMQGR EKRTRYGPID YDSQDERSSV YSPSPPRPKA SAATIEGPLR
     IFSSLARNSP QPFLPVGYSQ QQRAVSHESR LTADAPSFVP TWAKSSQLLG GSTSFKRPSL
     PDWDQQGQQA VDKDLPSILD PTFFSRDVES KAIPVGRASK DDVRGAARPS LSSASTLASV
     DKQANKSAVE PSRAADVDSG QETSETHQAP FAWQPSASNR LAPRTQPMHI PSGPRSCHSP
     SISQTSDAGH VPSIRWGDRR TSSRMSMSSL DRRFRRSCRG KKGPDDVGGN DEDDYEDEEE
     SVTDIIEEIV ERMDKVLEGW AGKILDEVTI MGQVRPHPRN LASVSDFPLD QEKLVQDMFK
     RMEEALDSRL TPALFASHAR RASDETQSTI RPLRQRNSSS DVKTANSSLA DAPGEWDFDY
     VQDILDVKLG EFRNQIESTL AQVMAALDKN GHLGAAVKPN GNDKYTNDSG PLVDFAEVVT
     ARLMTQLEST LQLHLHAAKE FQSASDVELQ KAMQSKLDEN LFLLSEKGAT DRSSIQHMLE
     SEMHGLERSF SKIVSSVEEH IRSALMLHLP PLLADKASSD GTLADRLTNQ LGSALGPVLS
     EERRCMLEEH QRSRDLLLEA LPSSTQIAQS TIKLVEPLVK SLKSEPIDSD ALVKRLAEVI
     GKQSIEHLVD LNPVLALIEP LIVKHEEARA FSKKILQRQE DTERTLCELP GAINAKTEIF
     LSSANDTSER QGLILEKIAE IKAEIKDSSS TLSNAASLNT DALHRRLEDL AKDKILTRET
     AEKTLSELAS VYQVLDSSYQ ALSRLEAQHT SSEESHRDAT AWLEKQAQAN ADLAKELREA
     EARAARAEAG QAEAEAKLSS LGRESDSLRD QLAQLTAEFA SFKAERTKEQ EASEKAVADA
     MARVDRAEAA SVETQDRMSR LLEQANVAER EAYDSAKSVL ERASKAEGQV AALEKRIAEQ
     DNKIGNLQQL SATQKQKAAQ SHQKLAEGEK RVKELEGKAE ELAEAAIRLR LLEEKANELE
     DVRRQLHDSV EREALMKKEL TKYDDRFSEM ETELVEIKDS FVERSVHEEV QRKYTESQKL
     VEQLEAKLQT LTASPLTFDG WEAVEKQKTG AWASMHAPRV HIEDVELVGR SSRSIRSVSF
     ASTAGSQGKK EVEVDEGGWW S