ID A0A0V1D4Z2_TRIBR Unreviewed; 918 AA.
AC A0A0V1D4Z2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Exocyst complex component 2 {ECO:0000256|ARBA:ARBA00017526, ECO:0000256|RuleBase:RU365069};
GN Name=sec-5 {ECO:0000313|EMBL:KRY56601.1};
GN ORFNames=T03_577 {ECO:0000313|EMBL:KRY56601.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY56601.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY56601.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY56601.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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|ARBA:ARBA00002660, 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}.
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:KRY56601.1}.
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DR EMBL; JYDI01000041; KRY56601.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1D4Z2; -.
DR STRING; 45882.A0A0V1D4Z2; -.
DR Proteomes; UP000054653; 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 CDD; cd00603; IPT_PCSR; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR029175; EXOC2/Sec5.
DR InterPro; IPR039481; EXOC2/Sec5_N_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR PANTHER; PTHR13043:SF1; EXOCYST COMPLEX COMPONENT 2; 1.
DR PANTHER; PTHR13043; EXOCYST COMPLEX COMPONENT SEC5; 1.
DR Pfam; PF15469; Sec5; 1.
DR Pfam; PF01833; TIG; 1.
DR SUPFAM; SSF81296; E set domains; 1.
PE 3: Inferred from homology;
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483, ECO:0000256|RuleBase:RU365069};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365069};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365069}.
FT DOMAIN 6..88
FT /note="IPT/TIG"
FT /evidence="ECO:0000259|Pfam:PF01833"
FT DOMAIN 129..892
FT /note="Exocyst complex component EXOC2/Sec5 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF15469"
SQ SEQUENCE 918 AA; 104570 MW; 2E5766ACE86531C4 CRC64;
MKGPAPVVTG LSPKDGVPGT QIVIRGEHLG LSQSDVIGLT VCNADCMQSL KWESSHKIIT
RVSHCKAGTG EVIVTTKSGG RGSCTVQFRI FHALIGPLQP TAVWVDESRM IETFRRDPKE
AAAIVDDCPL GFSVETNVTP IYHWSSELFP ESSSNMRLEN FHPVRYLVEN CRIVSFENLK
AGLEFMRSQV IVSKKGPKEF MKSNLSCILD CIDAMSGKLK LCNFSFLGVL NLDLRLHVEQ
DCCVNPTEMA EQFQTKIDHC IQTGEDVFVD VLKRKEQSDA IRNALSLLQR FRFMFYLPQL
MKVYTEKVAI INFVCPYQSG EYALVLSEYS RAKSLLSETE VPLFKEAFAE AEIQMEEFKS
TLHRQLVDHK VPLSEQKRII RYLTSVDSEV DAGWICLESQ CQWLKALIID CQKIHFSIGK
EKTFDDSEND FSDKLVSQIP QSFRFSESVC TILDTKVQDF VKLSQEYIAG QLTSHSIIHT
KQVEVHIFNL SAALVFNAIF PVNKIPSELV DSYDDAFLQW NVSSMEPAYL LQLLKSLRST
VAGFLDLECE ERYLQYWMDL CVEIRLHCLA CFVEQTESSI SALASKEIWK LLVCNEEMSK
TALPDLFESI IHELLPIFKQ LLCYNNYRKE VDFLSSESHK DGLLKRFERL LCSFKLTMLK
LIGFEQQQQL DDDVVSGGGM SKGSSTFEFD YPKGRAKKSS RITDKKLLIV LANCDYLLRY
CLPRLIDRLS RNGMWLTEPL QQRCVVCYGS FRTFLLKLYI SSKSSMLNTI FEISTDSWQK
LQGVSNYIKD LILRIVSVQA ELFLISPALY STVIGFVIRS YCDRIIQCAK ANISSFNQSQ
HTQLLLDFTA FEESVQPLLS DETKSMIKEF KLEIHSTWNY ELQEMLNAYL QGAEILLTSL
KQPMPVNNNN NNNANNNA
//