ID   PRM1_USTMA              Reviewed;         983 AA.
AC   Q4P996; A0A0D1DYN3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Plasma membrane fusion protein PRM1;
GN   Name=PRM1; ORFNames=UMAG_03317;
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.
CC   -!- FUNCTION: Involved in cell fusion during mating by stabilizing the
CC       plasma membrane fusion event. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PRM1 family. {ECO:0000305}.
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DR   EMBL; CM003147; KIS68751.1; -; Genomic_DNA.
DR   RefSeq; XP_011389721.1; XM_011391419.1.
DR   AlphaFoldDB; Q4P996; -.
DR   STRING; 5270.UM03317P0; -.
DR   EnsemblFungi; KIS68751; KIS68751; UMAG_03317.
DR   GeneID; 23563809; -.
DR   KEGG; uma:UMAG_03317; -.
DR   VEuPathDB; FungiDB:UMAG_03317; -.
DR   eggNOG; ENOG502QRP5; Eukaryota.
DR   HOGENOM; CLU_010191_0_0_1; -.
DR   InParanoid; Q4P996; -.
DR   OMA; QTYLCLF; -.
DR   OrthoDB; 607383at2759; -.
DR   Proteomes; UP000000561; Chromosome 8.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043332; C:mating projection tip; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032220; P:plasma membrane fusion involved in cytogamy; IBA:GO_Central.
DR   InterPro; IPR026777; PRM1.
DR   PANTHER; PTHR31030; PTHR31030; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Conjugation; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..983
FT                   /note="Plasma membrane fusion protein PRM1"
FT                   /id="PRO_0000337291"
FT   TOPO_DOM        1..57
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..159
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        181..332
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        333..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        354..440
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        441..461
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        462..641
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        642..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        663..983
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          674..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..976
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        674..693
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        765..813
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        939..956
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        35
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        242
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        306
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        529
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        585
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   983 AA;  107499 MW;  D8A0C87BA49F2058 CRC64;
     MSFHPNAVDA PPSYLHQHQA GSPLYTQNTI RPNANSTDLN SPHKPPILQP WLGLQARLFL
     APISIPLISL LFVAARMLSS SNEATDSISS AKGKLLSACS AAEGTASLAA SFPHFLAAST
     NVQLALSVTA TVHSAARVFD LSMTAIQKIL TYIVNSYKSL FMCFMELLVR GALAVLITAV
     EFISQAITAA TLGIRSAIQE SITGVNTLLA TAVGAINDVI GVFGQHVNPP HIAVPSLTSL
     ENITLPHEIQ DGLVKLNATL PTLQQLKQSM DALIETPFEE MKREVNATLA SFQFNHSVFP
     VPEMQNVTFC DRIDTSPLDE LGNALKNVAR WGLVALLLIA IVVMLIGVAW EWWKWQKEVK
     AVERTRSLWL AQRSSAHSDG NDKFCDNILK TENLMSLLTI SQHPLISFCS LNYCKRLGIR
     TRRAQDRCAW LLSFLMHPAS LACLFTGVLG LISVLMQAIL VHSLSHHYVS SIDTSLAHLS
     SDIVNLVHDH TRNASVAFST SANTVILQVE AELNDHVFRW VDTTTSTMNS TLNQFVDGLT
     ETLTSTFGGT PFNAPLQTFV QCILGQKVQG IEKALTWIHE NAYVNFSVVP ADVLMLRPEQ
     QEAVLRPVRE AMLGSRDDQG GGNGVVGHVI SRYMEHLHQE KILFTALIGV YAIILLIGLL
     AVLYATLAER RMHDDDETRK KVSRDESEEK LRSDLQAGPG GAGIARLWSR RPKLNAGCFR
     AFSHPPVPVS AQNPSSKIDH AARFPSSAHS SRPDPIHVTK DSISYPFQMH HSLNTSPSTR
     PTQPTPLQQT SNPDRDTVQS LHHASTTHNQ TASTRTKEYD SWLCFLASYH DGEATVPAKA
     PEAVEGAQDR FHRLFGCSLR ASPTVATFNH HVSAPAVSSD RAEIEVEDAR FRETLDLGSM
     QDWIGSKSPI PPPAGRGGSH SPRNTADQLP EVQLTRSGGC VGPHSSDSTQ ETYAFTDSVR
     LPPGPQPQQK RVVSSQSISF FAW