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PRM1_LACBS
ID   PRM1_LACBS              Reviewed;        1026 AA.
AC   B0D0P0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=Plasma membrane fusion protein PRM1;
GN   Name=PRM1; ORFNames=LACBIDRAFT_231982;
OS   Laccaria bicolor (strain S238N-H82 / ATCC MYA-4686) (Bicoloured deceiver)
OS   (Laccaria laccata var. bicolor).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Tricholomataceae; Laccaria.
OX   NCBI_TaxID=486041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 / ATCC MYA-4686;
RX   PubMed=18322534; DOI=10.1038/nature06556;
RA   Martin F., Aerts A., Ahren D., Brun A., Danchin E.G.J., Duchaussoy F.,
RA   Gibon J., Kohler A., Lindquist E., Pereda V., Salamov A., Shapiro H.J.,
RA   Wuyts J., Blaudez D., Buee M., Brokstein P., Canbaeck B., Cohen D.,
RA   Courty P.E., Coutinho P.M., Delaruelle C., Detter J.C., Deveau A.,
RA   DiFazio S., Duplessis S., Fraissinet-Tachet L., Lucic E., Frey-Klett P.,
RA   Fourrey C., Feussner I., Gay G., Grimwood J., Hoegger P.J., Jain P.,
RA   Kilaru S., Labbe J., Lin Y.C., Legue V., Le Tacon F., Marmeisse R.,
RA   Melayah D., Montanini B., Muratet M., Nehls U., Niculita-Hirzel H.,
RA   Oudot-Le Secq M.P., Peter M., Quesneville H., Rajashekar B., Reich M.,
RA   Rouhier N., Schmutz J., Yin T., Chalot M., Henrissat B., Kuees U.,
RA   Lucas S., Van de Peer Y., Podila G.K., Polle A., Pukkila P.J.,
RA   Richardson P.M., Rouze P., Sanders I.R., Stajich J.E., Tunlid A.,
RA   Tuskan G., Grigoriev I.V.;
RT   "The genome of Laccaria bicolor provides insights into mycorrhizal
RT   symbiosis.";
RL   Nature 452:88-92(2008).
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; DS547095; EDR11496.1; ALT_TERM; Genomic_DNA.
DR   RefSeq; XP_001877393.1; XM_001877358.1.
DR   AlphaFoldDB; B0D0P0; -.
DR   STRING; 486041.B0D0P0; -.
DR   EnsemblFungi; EDR11496; EDR11496; LACBIDRAFT_231982.
DR   GeneID; 6073481; -.
DR   KEGG; lbc:LACBIDRAFT_231982; -.
DR   HOGENOM; CLU_010191_2_0_1; -.
DR   InParanoid; B0D0P0; -.
DR   OrthoDB; 1333210at2759; -.
DR   Proteomes; UP000001194; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043332; C:mating projection tip; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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..1026
FT                   /note="Plasma membrane fusion protein PRM1"
FT                   /id="PRO_0000337283"
FT   TOPO_DOM        1..26
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        48..108
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..300
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        301..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        322..403
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        404..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        425..611
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        612..632
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        633..1026
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   REGION          693..777
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          793..812
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          818..879
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          904..952
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        696..715
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        760..777
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..874
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        265
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        463
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        492
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        499
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        518
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        560
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1026 AA;  112212 MW;  4058390602A4E239 CRC64;
     MSTLAQPPTY DATTTADTQL TPYLQLSHLL SLTWLAYPIL SLIFVAFRLQ LSMTSLENSI
     LSVKSDILSS CKAAEHAATA AASMPRYMAL ATNEQFADAV NGSLHAARVA LVVSLTAMEA
     IINFIIDTYR STFFCFLELV VTGGLAVLIS AVQGINTVLQ SVTGSLRTSI QSDIASANSV
     IQNAINAINK VNPFGNINAP QIAVPSLDAL QNVTLPASFQ DALTSLNASI PTVADLKGAL
     ESIIDTPFEL LKTDINDTFT GLSFNSSILP VPEQNRLSFC NDVDLSVIDE IGRDFIKIAK
     IGVVIIILLA LLLIGFNCLL TWYKWRCMKR HLEYTRQAWN TDPTMIHTKT SSSSPPQVIL
     TDHNLMILHA NSAHPLITRI MNQLSARLRF SPSHHTNLRW FLHYIFHAPA LACFLIGFFG
     LLSVEIQLLA MGPIVHKFED SAAAAVSDFS NVIAASINDS MFNQSALYAN DINSRVDVIQ
     STINNGVFGW VNSTTFTLNA TINAFYTDIQ KAVSTVFNGT VLESPANDFI KCFIGGKVDA
     IENALTFLHD NLQIDIPRVN DSILVLSPAS VHEATAPIAA AAIGGGPNDK EGLIGRLVKA
     YTATLKKERV MFGLFLALWG IVVLMGVCIL IWNTYGQALL KKRRRRRYEL EQRSGINGIV
     VPFRSGVESE NEKGAVLDLP SFTPLPSPRR SAFKPFWGSR SNSPMGNQPS GSAESFAIQK
     EEWDDFPPKP IESTVKKPSR LMAIGRKAMG KERVKADGGE ESTSSSSEKS PSDEGIRSTT
     WVGKFTTLWT KKEPVPQSSE FWDQPSRGRP KLQINVHRDS ADAGPNLYSS HTMQSRWSAS
     PDATQTSWGK VMSPSKKTST TTTATFQTPF GYSTRKSGVP IHDLDQSYDS LSSKSGAPAS
     LPLPLYHGFS GSQSRPSARA EATTTERKDT SPPPPFAPYR TNKLPNPPYD EQRRTSTLRV
     MNPTFKSSDH TVAMPASRLL TTMDARHSSA INPFITPFDD EHRVTIDNNP VYVRQSIPTN
     PFGVAL
 
 
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