UPA1_USTMA
ID UPA1_USTMA Reviewed; 1287 AA.
AC A0A0D1E015;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2015, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=FYVE zinc finger domain protein UPA1 {ECO:0000303|PubMed:25985087};
DE AltName: Full=PAM2 domain-containing protein UPA1 {ECO:0000303|PubMed:25985087};
GN Name=UPA1 {ECO:0000303|PubMed:25985087}; ORFNames=UMAG_12183;
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, DISRUPTION PHENOTYPE, DOMAIN, SUBUNIT, INTERACTION WITH PAB1 AND
RP RRM4, 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 [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
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).
CC -!- FUNCTION: FYVE zinc finger domain protein that functions in endosomal
CC targeting and transport of mRNAs, as well as associated ribosomes
CC (PubMed:25985087, PubMed:28422978). The endosomal mRNA transport
CC regulates polarity of the infectious hyphae by transporting a broad
CC spectrum of cargo mRNAs from the nucleus to cell poles
CC (PubMed:25985087). Involved in chitinase CTS1 secretion
CC (PubMed:25985087). Dispensable for general endosomal functions but
CC crucial for endosomal recruitment of RRM4 (PubMed:25985087).
CC {ECO:0000269|PubMed:25985087, ECO:0000269|PubMed:28422978}.
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 Interacts (via PAM2 motif) with PAB1 (via PABC domain)
CC (PubMed:25985087). Interacts (via PAM2L motifs) with RRM4
CC (PubMed:25985087). {ECO:0000269|PubMed:25985087}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:25985087}. Endosome {ECO:0000269|PubMed:25985087}.
CC Note=Shuttles with endosomes along microtubules (PubMed:25985087). the
CC FYVE domain mediates endosomal localization and endosomal targeting is
CC crucial for its function during polar growth and CTS1 secretion
CC (PubMed:25985087). {ECO:0000269|PubMed:25985087}.
CC -!- DOMAIN: The FYVE domain is sufficient for endosome interaction.
CC {ECO:0000269|PubMed:25985087}.
CC -!- DOMAIN: The PAM2 motif interacts specifically with the PABC domain of
CC PAB1, wheareas the 2 PAM2L motifs are involved in the interaction with
CC RRM4. {ECO:0000269|PubMed:25985087}.
CC -!- DISRUPTION PHENOTYPE: Causes defects in hyphal growth and secretion of
CC chitinase CTS1, 2 cellular processes that are regulated by RRM4-
CC mediated endosomal mRNA transport. {ECO:0000269|PubMed:25985087,
CC ECO:0000269|PubMed:28422978}.
CC -!- SIMILARITY: Belongs to the UPA1 PAM2 domain-binding protein family.
CC {ECO:0000305}.
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DR EMBL; CM003144; KIS69564.1; -; Genomic_DNA.
DR RefSeq; XP_011388912.1; XM_011390610.1.
DR STRING; 5270.UM02100P0; -.
DR EnsemblFungi; KIS69564; KIS69564; UMAG_12183.
DR GeneID; 23567936; -.
DR KEGG; uma:UMAG_12183; -.
DR VEuPathDB; FungiDB:UMAG_12183; -.
DR eggNOG; KOG1729; Eukaryota.
DR eggNOG; KOG4177; Eukaryota.
DR OrthoDB; 922362at2759; -.
DR Proteomes; UP000000561; Chromosome 5.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.20; -; 2.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Cytoskeleton; Endosome; Metal-binding;
KW mRNA transport; Reference proteome; Repeat; Transferase; Transport;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1287
FT /note="FYVE zinc finger domain protein UPA1"
FT /id="PRO_0000454340"
FT REPEAT 366..395
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 400..429
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 433..463
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 468..497
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT ZN_FING 1055..1129
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT ZN_FING 1243..1283
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 934..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 128..144
FT /note="PAM2"
FT /evidence="ECO:0000269|PubMed:25985087"
FT MOTIF 239..253
FT /note="PAM2L 1"
FT /evidence="ECO:0000269|PubMed:25985087"
FT MOTIF 941..960
FT /note="PAM2L 2"
FT /evidence="ECO:0000269|PubMed:25985087"
FT COMPBIAS 64..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..697
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..957
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1061
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1064
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1077
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1080
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1085
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1088
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1121
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 1124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
SQ SEQUENCE 1287 AA; 138533 MW; 2796105F5E9FBEEC CRC64;
MTIPDPANII HNDAGTASPH HIWADVGDST SSSQHEATRS RSDDANGGAS ASMHAPQHVK
ANRAAQPTYD SSDLPSFGLS ARLTRDSSSF GSKPSSSASD SRRPKFAPYE AENLWATSST
TSHPSKASQS TLSPNASVFK PSRSLQPNHF EPHAVANVHD FDDPLNSAYS SDTVSPRPDH
APLDHEQPQQ PSALDPVAVS KVEEQRGDHS IPHQNGLVSA QAQTASDAVS TSKYTTEAAD
QEEDQDDFVY PGADSPSSGQ AAVQDEQQAV TDSQTTKSLT KQESDPEASS TSLSAPAEAE
HIVVGSAAEQ SLTSSAPAET AVHIDYDTLA QLCSRGPLSD LQSFFHTAQE SGLSMFSLSN
DPNPGNGLVP LHFAAKDGKT DIVRWLITQA GAIVEMEDRE GETALHKAAM AGKLSVASLL
LSHGADANAQ DADGWTALHN ACSRGYLDLV RLLVDRGHAQ IDVQGGRGAW TPLMNAASKG
HLPVVRHLTA KYHADPFVRN AAGETAFDVA AATFEVYICE ILERYEAERW NASKFTTSSP
SRSGAIVPGR GPYEPLALHT TIPVILHENQ RLDTRLQTLA LNGGKPRWSS SSAARAHKPD
RRSPSSMPPG PLAPSRTRHV PMRQDDVGLP TRSLPYKLRL RSRVGPAAAR RRAAALAAQH
TPNPQDCHDD DLASTPTPES VLQARRGTSS VNGASAQHAD AESSHFWLCE WQLDTTHPLV
DVEHGWQYAQ SFDALDDKWS SQPPPPLERL LEGRGLSASV TRAITGGAGF ANAQAEQEIS
SSSWVRRRRW IRVLRRRLDI EFGDDLEACE GATGAGAEHL VLSSESQSNG DGSHGLSTAA
IMAAQEAAKS ECSQLGPDAD YVSRAKALAG PSAASGATPA DAMGADRDEL ARRIARLVMA
NTELRAAFED DDVERRSRAE ELRKEYALQL GQLREAAGLD EDEDEDAADD DDDEFIYPNS
YKDDGASVFT RLVNGETSGT LSRPSLSQRQ SSAASMLRNS VAPSEAGTSL AAARSADLAA
NREFRVPTNE APNKVVLRHG PTMREQNLQP QWQRDEEAKD CIGCGRHFTF FLRKHHCRRC
GRIFCDACSS KRAQLRMAEL VVDPSLPSMA ASEVLAPTRV CNGCHAELQL PPQLQNMRGA
DAMMAASRSR GADEVSGRSI LETQLEDGAF RSTLAPPSDV SSRASELTEC PVCSTTLSAL
GGSEEQEAHV RNCLENGGGG SMQGGRYLVY KLPEDSPIVG KECSICMEDF VANSTIARLP
CLCYFHRGCI DSWFKRGREC PVHARDW
