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Database: UniProt
Entry: H6C4P1_EXODN
LinkDB: H6C4P1_EXODN
Original site: H6C4P1_EXODN 
ID   H6C4P1_EXODN            Unreviewed;      1035 AA.
AC   H6C4P1;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Exocyst complex component SEC5 {ECO:0000256|RuleBase:RU365069};
GN   ORFNames=HMPREF1120_05691 {ECO:0000313|EMBL:EHY57662.1};
OS   Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS   yeast) (Wangiella dermatitidis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY57662.1, ECO:0000313|Proteomes:UP000007304};
RN   [1] {ECO:0000313|EMBL:EHY57662.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY57662.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL   Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the exocyst complex involved in the docking of
CC       exocytic vesicles with fusion sites on the plasma membrane.
CC       {ECO:0000256|RuleBase:RU365069}.
CC   -!- SUBUNIT: Component of the exocyst complex.
CC       {ECO:0000256|RuleBase:RU365069}.
CC   -!- SIMILARITY: Belongs to the SEC5 family. {ECO:0000256|ARBA:ARBA00010578,
CC       ECO:0000256|RuleBase:RU365069}.
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DR   EMBL; JH226134; EHY57662.1; -; Genomic_DNA.
DR   RefSeq; XP_009158123.1; XM_009159875.1.
DR   AlphaFoldDB; H6C4P1; -.
DR   STRING; 858893.H6C4P1; -.
DR   GeneID; 20310330; -.
DR   VEuPathDB; FungiDB:HMPREF1120_05691; -.
DR   eggNOG; KOG2347; Eukaryota.
DR   HOGENOM; CLU_011308_0_0_1; -.
DR   InParanoid; H6C4P1; -.
DR   OMA; RMWMDVD; -.
DR   OrthoDB; 37589at2759; -.
DR   Proteomes; UP000007304; Unassembled WGS sequence.
DR   GO; GO:0000145; C:exocyst; IEA:UniProtKB-UniRule.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006893; P:Golgi to plasma membrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR029175; EXOC2/Sec5.
DR   InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR   PANTHER; PTHR13043:SF1; EXOCYST COMPLEX COMPONENT 2; 1.
DR   PANTHER; PTHR13043; EXOCYST COMPLEX COMPONENT SEC5; 1.
DR   Pfam; PF15469; Sec5; 1.
PE   3: Inferred from homology;
KW   Exocytosis {ECO:0000256|ARBA:ARBA00022483, ECO:0000256|RuleBase:RU365069};
KW   Protein transport {ECO:0000256|RuleBase:RU365069};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007304};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365069}.
FT   DOMAIN          81..1015
FT                   /note="Exocyst complex component EXOC2/Sec5 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF15469"
FT   REGION          16..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1035 AA;  114522 MW;  FCB0DFA98A732731 CRC64;
     MSADQERTIV THYNLTNPFP TEWPAELDES DEDEVPDAVG IRRSRSRYSA LERSASERKS
     LVPGSERTGD GRANLVQKDE PDPLGVHPSV VNVLRNSGVP VEHDSRARNK FMLSSTTFSP
     GVFLSHVHAN ATTDDLLRGL QYLSRSIDQK SASLKVLVET NFERFVRAKA TIDNVYTEMR
     NQGMDSKAGS PPSPRHSRRS SAVHFRNVSN GAAPAVQTPS KNALRKETDY GVQGIKGPLL
     EVSQKAEEVW GPALGGKERE ANLKAIVEAI AQDRGLYELG SNLSHAITQK DYGTAIGLYH
     AALRYVAEAR SLSDMAVQQG RTLSNEEVQK VIAIGRMWDD AHEQIKSLKR DIWRRLANIP
     ATSPLPGAAQ SDDYMELINV LLQLGVEESP IWVYLLSRYD ALKNKIAAVV ERSKIEIEIL
     RRRLASADSP SSATVAAFLR QASRDRPEAL DSDDVVDFWN CILTYITKLL SLSSGLLGEI
     VDFWETAQSF IDGTRQKALS VGFEGESSKH HQLSESDVSG LRSGAIELVS QIRDAVLSLF
     ADAPTEDISS LFSPAPGSAE TPTTPLTGAA FSPTDGRIGV LDPQNLPTFA AKRGEPWEDF
     AFWPPHSNAL SAVHYLEKIL MLVGTAAGEM VALGPVSSNN TMHEKIKTMV GGARERSMRA
     ICEAWSKDAE SCKSLEDWVR APEKRDQTRM PLYFEAYERQ ILLGMQQVLY FSDTTAKPGT
     REIITPPPSK LLQMVRTQFV SSIYKAVSGM LENAEASTQG NEDDWVLVTS LSSIVDGASP
     TEFITQDAIN ASSRNVRMLL TMSNLKALRN DYVPSLIQVF ESSFSVKLAD ESKTIRDVFG
     QIDAKLFHSY TRPTVAQLTK IIRDGINSPT WAPTTSRPDQ VRPYVYATLM TLVMVHTEVS
     TTVSNAESSS PLLSEILSYL LENVSQALLD GFKERKPNTY SLPALMQATL DTEFIAQTMN
     QYATSKAGEI QGQIYTELDK RTTNEARARL QQELGDMRVV LKKLREGSRN TFSCFKRARP
     AEKDRTRPER KMTGT
//
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