ID A0A0V1CIQ4_TRIBR Unreviewed; 1051 AA.
AC A0A0V1CIQ4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Exocyst complex component 5 {ECO:0000256|ARBA:ARBA00017524};
DE AltName: Full=Exocyst complex component Sec10 {ECO:0000256|ARBA:ARBA00031471};
GN Name=EXOC5 {ECO:0000313|EMBL:KRY48627.1};
GN ORFNames=T03_921 {ECO:0000313|EMBL:KRY48627.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY48627.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY48627.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY48627.1};
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SEC10 family.
CC {ECO:0000256|ARBA:ARBA00006572}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000256|ARBA:ARBA00006666,
CC ECO:0000256|RuleBase:RU003857}.
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:KRY48627.1}.
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DR EMBL; JYDI01000201; KRY48627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CIQ4; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005267; F:potassium channel activity; IEA:InterPro.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd07978; TAF13; 1.
DR Gene3D; 1.10.287.70; -; 1.
DR Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR009976; Sec10-like.
DR InterPro; IPR048627; Sec10_HB.
DR InterPro; IPR048625; Sec10_N.
DR InterPro; IPR003195; TFIID_TAF13.
DR PANTHER; PTHR12100:SF0; EXOCYST COMPLEX COMPONENT 5; 1.
DR PANTHER; PTHR12100; SEC10; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR Pfam; PF07393; Sec10_HB; 2.
DR Pfam; PF20667; Sec10_N; 1.
DR Pfam; PF02269; TFIID-18kDa; 1.
DR PRINTS; PR01333; 2POREKCHANEL.
DR SUPFAM; SSF47113; Histone-fold; 1.
DR SUPFAM; SSF81324; Voltage-gated potassium channels; 2.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Exocytosis {ECO:0000256|ARBA:ARBA00022483};
KW Ion channel {ECO:0000256|RuleBase:RU003857};
KW Ion transport {ECO:0000256|RuleBase:RU003857};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU003857};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003857}.
FT TRANSMEM 527..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 636..654
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 720..743
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 749..768
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 775..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..70
FT /note="Exocyst complex component Sec10 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20667"
FT DOMAIN 98..176
FT /note="Exocyst complex component Sec10-like alpha-helical
FT bundle"
FT /evidence="ECO:0000259|Pfam:PF07393"
FT DOMAIN 182..453
FT /note="Exocyst complex component Sec10-like alpha-helical
FT bundle"
FT /evidence="ECO:0000259|Pfam:PF07393"
FT DOMAIN 636..691
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT DOMAIN 730..800
FT /note="Potassium channel"
FT /evidence="ECO:0000259|Pfam:PF07885"
FT REGION 894..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1051 AA; 120302 MW; 0E2504216075BCA8 CRC64;
MLRTYAEDLE SIADGKLKTL NERVNSVAAR VVHLGDQLQS VTAPRARAFE AYQLMVHFNE
FLSDQPLESE TFTDPDKGYS QAIDAYVEQC QWQSFRGGDI FTDIWNMLQK HDPVINDVFP
NPQQVMSKLV LNIYHGKLQG YVRSKLLNAS DPELYLSSLY DLFQKIQDLK RDLQARLMQD
TRTNYSLLSE EVAINILQET KLAFHRCGVL SSANDLSENV RQILDILMQY LCREHLEYAV
DLAVNAIQSN ENQGVKDFLN ILRQTAAISH LLEKQIDDSV SALLKNSSQS TSCLEHAKSL
LETIEAKLDK GVDKMLTTIV GHVRFILTTE QKKQEFKPEE DDNNGGEIPL CSNQIAIMNE
SLDGSNLENT LTELVVRFHR VIVDHIYQFQ YNSQGAMLLL CDVSEYRKVV SELNIPIAKK
LFVTLHALCN LLIVSSDHLL SACSSNTLKG MKNTNDEIME TKSIFEEHSS AFSRWLTSRS
ERVRSAGGRW VIPNFGHCST ATVQLRKCIF TRAIRLIDAL LVWSVKWHLI PFLILVGYSL
LGGCLFHILE GGPTIPKLAN RSTRPYILRA RVHTAADYQK EATLQLWRIL GKDVNDTERW
QQVQDTWIWY NSKALVPEAA APCPEFQLPK PPKLELNFWT SVYYAVTVYT TIGYGDIVPR
TTGGKIFTMI YCLFGIPLLF YILEELGTML LKMLHCILRW LKLAFNRPVL HRYDHCLAEV
PLSVALLLQI IWLCTSAALF LLWEDEWDYF TSFYFFFISF TTIGLGDVVP KYPSYTLMCS
ILVLLGLALV SMTVSVVQQK IDLLFQLLMN DIEHEYRKRQ VDPGTSKLSF GKRDDMLDEL
RYLCDGKPLQ SRILFKVMGK SKRDLLLQSY VKKASTRNIA VQTVHSKFKS VSCQTPRQTA
EPKSKTNRKY VFKNSTDPCL PHSPKSEMKD SSVNDSEPSV ESSVPEPGSS TETGEPKKRY
LTKELRCMLY GFGDSKQPFA ETVDLLEDIV MEFIKSFTLK SMEVRKTGRI TLEDIWYLIR
RDPKKYSRVK DLLTMNEELR KARKAFDEAK Y
//
