ID J8Q3E6_SACAR Unreviewed; 623 AA.
AC J8Q3E6;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Exocyst complex protein EXO70 {ECO:0000256|RuleBase:RU365026};
GN ORFNames=SU7_1761 {ECO:0000313|EMBL:EJS43146.1};
OS Saccharomyces arboricola (strain H-6 / AS 2.3317 / CBS 10644) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=1160507 {ECO:0000313|EMBL:EJS43146.1, ECO:0000313|Proteomes:UP000006968};
RN [1] {ECO:0000313|EMBL:EJS43146.1, ECO:0000313|Proteomes:UP000006968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H-6 / AS 2.3317 / CBS 10644
RC {ECO:0000313|Proteomes:UP000006968};
RX PubMed=23368932; DOI=10.1186/1471-2164-14-69;
RA Liti G., Nguyen Ba A.N., Blythe M., Mueller C.A., Bergstroem A.,
RA Cubillos F.A., Dafhnis-Calas F., Khoshraftar S., Malla S., Mehta N.,
RA Siow C.C., Warringer J., Moses A.M., Louis E.J., Nieduszynski C.A.;
RT "High quality de novo sequencing and assembly of the Saccharomyces
RT arboricolus genome.";
RL BMC Genomics 14:69-69(2013).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJS43146.1}.
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DR EMBL; ALIE01000112; EJS43146.1; -; Genomic_DNA.
DR AlphaFoldDB; J8Q3E6; -.
DR HOGENOM; CLU_010236_4_1_1; -.
DR OrthoDB; 460764at2759; -.
DR Proteomes; UP000006968; Chromosome X.
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; 1.10.357.60; -; 1.
DR Gene3D; 1.20.1310.30; -; 1.
DR Gene3D; 1.20.58.1150; -; 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000006968};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365026}.
FT DOMAIN 237..620
FT /note="Exocyst complex subunit Exo70 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03081"
SQ SEQUENCE 623 AA; 71159 MW; 961C5D70D4CF7562 CRC64;
MPAEIDIDEA DVLVLSQGLQ KTSKLTFQIN KSLQKIAATS TQSSQLFTPI LARNNVLTTL
QRNIESTLNS VASVKDLANE ASKYEIILQK GINQVGLKQY TQVIHKLDDM LEDIQSGQSN
REESSEFHGI LTHLEELIKS SEAQLRVYFI SIINIIKPFD PQINITKKMP FPYYEDQQLG
ALSWILDYFH GNSQSSTLQD IFVGERSKLI LKCMAFLEPF AKEVTTAKNA PYEKGSSGMN
SYTEALLGFI ANEKSLVDDL YSQYTENKPQ VLSQILSPLI SAYAKLFNAN LKIVRSNLEN
VGFFSFELVE SINGVKKSLR GKELQNYKSL LDCTQEVRQV TQSLFRDAID RIVKKANSIS
TIPSNNGVTE ATVDTMSRLR KFSEYKNGCL GAMDNITREN WLPSNYKEKE YTLQNEPLNW
EDRNVLLSCF ISDCIDTLAV NLERKAQLTL MPNQEPDVAN PNSPRNKHKQ RIGFFILMNL
TLVEQIVEKS ELNSMIAGEG HSRLKRLKKR YVSYMVSDWR DLTANLMDAV FIDSSGKKSK
DKEQIKEKFR KFNEGFEDLV SKTKQYKLSD PSLKVILKSE IISLVMPMYE RFHSRYKDSF
KNPRKHIKYT PDELTAVLNQ LVR
//
