ID W6R5M2_PENRF Unreviewed; 626 AA.
AC W6R5M2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Exocyst complex protein EXO70 {ECO:0000256|RuleBase:RU365026};
GN Name=exo70 {ECO:0000313|EMBL:CDM37112.1};
GN ORFNames=PROQFM164_S06g000072 {ECO:0000313|EMBL:CDM37112.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM37112.1};
RN [1] {ECO:0000313|EMBL:CDM37112.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM37112.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- FUNCTION: Involved in the secretory pathway as part of the exocyst
CC complex which tethers secretory vesicles to the sites of exocytosis.
CC Also plays a role in the assembly of the exocyst.
CC {ECO:0000256|RuleBase:RU365026}.
CC -!- SUBCELLULAR LOCATION: Bud {ECO:0000256|RuleBase:RU365026}. Bud neck
CC {ECO:0000256|RuleBase:RU365026}.
CC -!- SIMILARITY: Belongs to the EXO70 family.
CC {ECO:0000256|ARBA:ARBA00006756, ECO:0000256|RuleBase:RU365026}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG792020; CDM37112.1; -; Genomic_DNA.
DR AlphaFoldDB; W6R5M2; -.
DR STRING; 1365484.W6R5M2; -.
DR OMA; GIIRAGP; -.
DR OrthoDB; 460764at2759; -.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0000145; C:exocyst; IEA:InterPro.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1280.170; Exocyst complex component Exo70; 1.
DR InterPro; IPR016159; Cullin_repeat-like_dom_sf.
DR InterPro; IPR004140; Exo70.
DR InterPro; IPR046364; Exo70_C.
DR PANTHER; PTHR12542:SF41; EXOCYST COMPLEX COMPONENT 7; 1.
DR PANTHER; PTHR12542; EXOCYST COMPLEX PROTEIN EXO70; 1.
DR Pfam; PF03081; Exo70_C; 1.
DR Pfam; PF20669; Exo70_N; 1.
DR SUPFAM; SSF74788; Cullin repeat-like; 1.
PE 3: Inferred from homology;
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483, ECO:0000256|RuleBase:RU365026};
KW Protein transport {ECO:0000256|RuleBase:RU365026};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365026}.
FT DOMAIN 246..623
FT /note="Exocyst complex subunit Exo70 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03081"
SQ SEQUENCE 626 AA; 68795 MW; 7B31973EDD4D7584 CRC64;
MVAPRNTAYA EESAEVEVLY ANLEKLNRLT KKIQGSMVRL ETGGKVVKEA IGPIYSNTQS
LQITNSNIDK VNDAIDRLRQ PLDAKNREDG IIRAGPQSSG LTHYLGAMKR VEKALVDLNT
TNLRSNQNAI ADFNSLLNTG STKLQEVLRG ELSQHSTPVE PLHYLTKDLP FPSIPEDTVT
HMAPLCSAVG SASVHGSQRG KGDNPALKAY AEVRGPYIAS SLENLAIASL NTVKRRPTDG
PYKQGTNGIG IYSNALEAFI TTEHGIIVEM FTGDQQGLAL QATFFPAMGE YSKTLRELNQ
YIKTNLMTDC FLAFEIIEIV TAMSYRIDSK AAELKSLLIE ALRPVRETAK SSLSELLEET
KRKAANTTLP PDGGSVPLVE EVMSSLATLT GYSGPLASIL TSLGDGNWRA KSNTAGSAPL
DVGPDSSTLL SHFILDMIEA LMTSLEGRGR AFHRSKAALG VFLSNVFCVV DRSIRQSPEL
ARYLGNPDSI ARIDTFRKRA TSTYLDAWKE TSQYLLDVQY TSRGAQRNSS GNVDSSAIVK
SLSSKDKDAI KDKFKAFNAS FEDMVSRHKT LHMEREVRSL LTRELQTVLE PLYARFYDRY
VEIDKGRGKY IKYDKASLSV QLAQLA
//
