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PRM1_CRYNJ
ID   PRM1_CRYNJ              Reviewed;        1076 AA.
AC   P0CQ04; Q55QH3; Q5KFP3;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   25-MAY-2022, entry version 32.
DE   RecName: Full=Plasma membrane fusion protein PRM1;
GN   Name=PRM1; OrderedLocusNames=CNF01070;
OS   Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC
OS   MYA-565) (Filobasidiella neoformans).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Cryptococcus;
OC   Cryptococcus neoformans species complex.
OX   NCBI_TaxID=214684;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JEC21 / ATCC MYA-565;
RX   PubMed=15653466; DOI=10.1126/science.1103773;
RA   Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA   Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA   Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA   Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA   Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA   Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA   Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA   Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA   Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA   Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT   "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT   neoformans.";
RL   Science 307:1321-1324(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAW44262.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AE017346; AAW44262.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_571569.1; XM_571569.1.
DR   AlphaFoldDB; P0CQ04; -.
DR   STRING; 5207.AAW44262; -.
DR   EnsemblFungi; AAW44262; AAW44262; CNF01070.
DR   GeneID; 3258038; -.
DR   VEuPathDB; FungiDB:CNF01070; -.
DR   eggNOG; ENOG502QRP5; Eukaryota.
DR   InParanoid; P0CQ04; -.
DR   OrthoDB; 306736at2759; -.
DR   Proteomes; UP000002149; Chromosome 6.
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..1076
FT                   /note="Plasma membrane fusion protein PRM1"
FT                   /id="PRO_0000337279"
FT   TOPO_DOM        1..66
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        67..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        88..138
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        160..350
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        372..432
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        433..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        456..646
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        647..667
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        668..1076
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          796..834
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          874..899
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          963..1020
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1057..1076
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        814..834
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        987..1009
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        235
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        251
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        266
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        476
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        496
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        526
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        533
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        548
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        602
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1076 AA;  117355 MW;  8EA83F133888336E CRC64;
     MSYPQAPSKF VNPDEIIPLS PPTKPPFAQY AASPLPATPH TPYSPPSPSR LSETIPLRPY
     LSLLPRILLT FFSPCLLPMI LTIAHLIQNR SSTASLATSL KSSVLSACSG LAKAAASIKT
     LPRYLAMQTN QEAIRATQAS ILAIGTMLMD AITIIEAVVN FIVDTYRSLL LCTIELAVRG
     TLEILISAVQ TISDAVTDTL NSVRSNIQDD IGDANDIIQT AVSAINRVTT LVNLNISVPE
     FSIPALSFLQ NVTIPTTFED GLITLNSSLP TLTDLKKKMD EIIDTPFEAL ISEINSTRLE
     MAASFNSSIL SVPSLSSLSA NSANDLSNDL CSDLDTSLID DTAKALHKLS SIAIGLMFLL
     LFLIWAALAV WEWRKWKLMK DTVDAVNEEW DRDGKSDAWR MVAIVEHPVL ERYSGTFLGK
     IAKMPRTRTN LRWFLSYLAH PTCLALLFIS LFGFLSIQFQ LVALNALKAH AQSSANSTVT
     ASTNSLVTKL NAAALNSSQE YADSYNEAIA GYQDRINNEL FGSWVNTTAV TLNSTLVEFY
     DEVEKALNAS FGGTILYNPI NTFMYCILGS KITNLEKGLT WISEHAFVDL PTFPSDILLL
     SNDSMNEIAT PIAAAAVGSG DGGDDDDGVV GTLISHFESA LKVERTFYGI MLGVWLALFL
     IGLAVVIWNS GGREKFMALR GVPSSSSPPG YGPPESKHPR WKAWLTNNHP IYDSYAEKQF
     RGTTPTNCLE SYTHADVPNV NNGNDDHEKS FFKMRDSHAA GPFGSHATSA VRSTIASLAA
     PGQSFLKLSG RKLTDTTTPY DDKVPLAPVQ TSEKYSRDHA NSPFPRPSSE SSESSAAQPF
     WVDKFYGAFE GVKSFFPTRS QRLGAALARK ASQRTEGSFG ASQVPTARTP GHDWIGGHQC
     LPEKKAEPEW SMVDPRMLGR ALEDDKGRYP RVLPPSEMAA ANYNPHPVYP RPMSRASTLG
     EGMVIPSTTS HPDPFQDMPP LPPKHKRASM DYVEEYESSH SRSSREDSRH GGVTSPASSS
     VSYFAAEPQL VSASKVQVGV AQKGGQATRA LAEIVKELQE KRERKDPFGD DYERGL
 
 
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