ID A0A0C9MLP4_9FUNG Unreviewed; 813 AA.
AC A0A0C9MLP4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Exocyst complex protein EXO70 {ECO:0000256|RuleBase:RU365026};
GN ORFNames=MAM1_0206d07981 {ECO:0000313|EMBL:GAN08469.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN08469.1};
RN [1] {ECO:0000313|EMBL:GAN08469.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN08469.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) 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; DF836495; GAN08469.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9MLP4; -.
DR STRING; 91626.A0A0C9MLP4; -.
DR OrthoDB; 460764at2759; -.
DR Proteomes; UP000053815; 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 Reference proteome {ECO:0000313|Proteomes:UP000053815};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365026}.
FT DOMAIN 246..613
FT /note="Exocyst complex subunit Exo70 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03081"
FT REGION 690..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 92056 MW; E483D19F4CDD3A4A CRC64;
MPRQTYSQIA TNGKLDEDTA DLDALQKQLG RMNGLSDKLV NILDSFDGRL LKLEASILPI
HKSTQNLTKL ANNIDATLKE TENIVDCLNM PSKEEAYILK GPDENNVLPY LKAMGRLKDG
VDAIEKSQLR SCEKTTYQMK QLLKAGMLHL ETLFRKWLSA VSNPVDVNTM LNSNSEMMTT
ASMKQLSQLS TYISSSEKEI GYSVDFTKPY IDIRSSFLQR SLHPLSQSVQ LSEKHQGSSY
ERGSSEFLKY TECYTKMLES EYKFAQQIMG NEQRRAAALK GTIVPATVEY VAAGKQLNAV
AKRLNYTETT FVFDIIEKFD RECISYVEAL SHVVSLHDIQ DMMNSFKLTV LRNFYEFMED
VRGRKEVSQP INLSSDGTVH EMTSNTLNYF KRLYIWRDTV EPLLVLIGDG GWNNMPSPQI
MNDTSRMQQG ESAIGAALLQ KFFVDALDQM TVALQLKSRG YKKQTLATLF LLNNYNHILR
QIRSPPLNAI FDDGSEMKFG KLVKKQLDAY QESWKPCVEN LMDVTYVRGG AIKNSMGSQE
RQLIKERFKN FNTEFEEIAR AQQTYAIPDT ELRNQVIRDV KNVLVPMYGR FLDKYQNTDF
TKNPAKYIRY DKDKGLYKKN IQSKQVLQVS STKNLKYELN YYSHQPTATS TLRYGEQSLQ
PSDSLLFNGR QRSSDGLKLH RALHQRMSRR YQPYSTTLNN NNNNNDTIQD GPLFGPIPCL
SSASPSSSSS SLASSPSLSF AAASSSSITS LNNASILEDS EIFDEFDDFI STPASNYLAS
PPASPLLSPS NSSFNNDNND EDDFDFSDFP LFS
//