PRM1_COPC7
ID PRM1_COPC7 Reviewed; 1062 AA.
AC A8N5E6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 54.
DE RecName: Full=Plasma membrane fusion protein PRM1;
GN Name=PRM1; ORFNames=CC1G_04524;
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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; AACS02000003; EAU91756.1; -; Genomic_DNA.
DR RefSeq; XP_001830091.1; XM_001830039.1.
DR AlphaFoldDB; A8N5E6; -.
DR STRING; 5346.XP_001830091.1; -.
DR EnsemblFungi; EAU91756; EAU91756; CC1G_04524.
DR GeneID; 6006529; -.
DR KEGG; cci:CC1G_04524; -.
DR VEuPathDB; FungiDB:CC1G_04524; -.
DR eggNOG; ENOG502QRP5; Eukaryota.
DR HOGENOM; CLU_010191_0_0_1; -.
DR InParanoid; A8N5E6; -.
DR OMA; HSYGRDM; -.
DR OrthoDB; 1333210at2759; -.
DR Proteomes; UP000001861; 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..1062
FT /note="Plasma membrane fusion protein PRM1"
FT /id="PRO_0000337278"
FT TOPO_DOM 1..20
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..294
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 295..315
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 316..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 397..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..604
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 605..625
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 626..1062
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT REGION 652..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 965..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 250
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 456
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 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1062 AA; 114986 MW; 2D0EFB633BD9F3B6 CRC64;
MSFLTTPPNE HTTLTSYLQL PHLLSLTWLA YPILSLIFVA FRLQASLASS EDAISSAKSN
LLASCKAAEE AATSTASLPR YMAIATNQQV ADAVNATLRG ARAALILTLT VMEAIINFII
DLYRSIFLCF LELVVRGGIA ILVGAVEEIN NVLATVTSGL RTQIQASVGT LNNALRETIE
GINRINPFGD IPVPTFDPPN LDGLDNVSLP DSFQESLLRL NDTIPTVSTI KEKLQDIIGT
PFELVKRDIN DTFAAVSFSA DTLPVPEQNK VSFCSDLDLS VVDDVGNDIV KSAKIGIVIL
LVIALVLIGL NCLFTWYKWR CMQAHLEYTR QAWNTDPTMQ TKGSISATPQ IALSNHNLMV
LQANSEHPLV TRITNQLSQK LRLSPRTHTH MQWFFNYIFH PPAAACLLIG VFGLLLIEIQ
LLAMGPLVNK YQEQAAETTK DFSLLIANSI NESMLNQSTI YAAEINGRVD SVQTTINDGL
FGWVDGTIVP LNTTINEFYD DIQNAVQTVF GGTILETAAT EFIRCLIGSK VDAVENALTF
LHENLRVDMP RVNDTALMLS PESVNEASAP IAAAAMGGGT DDDQGLIGRL VNSYADSLRK
ERVTFGIFLA LWGVVVLMGL FVLFWHSTGK PLLEKRRRRK YEKSKGMLPE GGFVVPYRDG
SAPPSRDEKN LGGGGNGGVG LAMTGDELPQ FTPLPSPRRS AFKPFWNPAK PDASGEAKDV
EKEPSPMAQV AADEVSKLKA FRLKLMGKST ESLDADSKAS DNPPGLFGKV KGVFGKKDAD
QAPDYWTSYN ASSDTVNANT ARPNIRVIVD TDQDREDTYG NSFRHSADIE GADIYTPPPN
SRWSTSPGPT KTSWNLKKLT LLSPKSSNNK KLPAVSGSSS IGPIPPSMSA AASGLKRQPS
VPTDIGASFD DPFMASVSVP RKPSPIVPGI YPVPLHAAAP AINNNPYQRA PSPPKRFVAP
YLNDPSALSR NTSGSSASKT HRRSSSHPAA VWRVTNAAST DRLTASPMSS QVSLPARMLT
SENPFITPFD DEHRVEVVNP SRGEVRKSMA VNPFSNAAAV AI
