ID A0A1W5D9K5_9LECA Unreviewed; 782 AA.
AC A0A1W5D9K5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Exocyst complex protein EXO70 {ECO:0000256|RuleBase:RU365026};
OS Lasallia pustulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC OSLEUM clade; Umbilicariomycetidae; Umbilicariales; Umbilicariaceae;
OC Lasallia.
OX NCBI_TaxID=136370 {ECO:0000313|EMBL:SLM39721.1, ECO:0000313|Proteomes:UP000192927};
RN [1] {ECO:0000313|Proteomes:UP000192927}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sharma R., Thines M.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FWEW01003541; SLM39721.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W5D9K5; -.
DR OrthoDB; 460764at2759; -.
DR Proteomes; UP000192927; Unassembled WGS sequence.
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 391..777
FT /note="Exocyst complex subunit Exo70 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03081"
FT REGION 1..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..89
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 782 AA; 86556 MW; 8B4DD83EFD76C4B2 CRC64;
MLFRIRNPSA SSTESLSSLA PPENPFEDSA EYDYALPDVY SSQSESVDSS DENYFSDLDS
SDQNDSSGLD ENDSSDLDFS DNENDSSDLD SSDEHDHHVL SPDVTFGIRL EIDLLELTKR
EIVDLVAPYA ERLAALIESL VEFRLMMASQ RNVAHAEESA EVAVFYATLE KLKSLTKKIQ
GSLTRLEANG RVVSEAVGPV HDNTQSSQTL IQNLERISSA IDQLQKPLEG KAREEKIIYA
GPNEVGVQEY MASLKRIDQA LANMNATNLR VNQQTVGDLK NLLSHGTRQL HAVFRSILNE
DLQPVEPLHY ITKHLPFPTL PEDKTAILRS IELCLSWSAS HGESTDRESL TIQTYSAMRG
LYIANSLHNL ATASIITARK KSPDENYRQN TNGIGTYATG LEKMLLAEYQ SIVAVFSQAN
WAAVFKLTYI RPLVDFEKTL RDLNSHINSN ITTDCFLAYE LIDIVTPISV RLEDWAGARK
PALADALKQI RGTAKFSLGE LLEEVRKRIQ NMQVLPGDGA AIPLTTAIMT RLQTMILYPL
PLYSIMTEMG DGNWLSASSA SSSSASMSSA HSVDLVADGR QLLAHYVNDT IDTLLQSLDS
RARVLLKSKS IPGVFLANNI AVINRMIHSS DLASVLSVSP SPPKWDIWRK KGNSAYLDSW
KEACSALLDV QYTSRGARPP SGSQGMIDSA AVIKGLGSKE KDAIKEKFKT FNTIFDELSA
KHMGLAMERE VRSQLSREVA AMIEPLYGRF WDRYHEIDKG KGKYVKYDKG GLSGQLAQLA
LI
//
