ID A0A1B1DZ33_9APIC Unreviewed; 759 AA.
AC A0A1B1DZ33;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ANQ07865.1};
GN ORFNames=PCOAH_00021450 {ECO:0000313|EMBL:ANQ07865.1};
OS Plasmodium coatneyi.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium.
OX NCBI_TaxID=208452 {ECO:0000313|EMBL:ANQ07865.1, ECO:0000313|Proteomes:UP000092716};
RN [1] {ECO:0000313|Proteomes:UP000092716}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hackeri {ECO:0000313|Proteomes:UP000092716};
RA Chien J.-T., Pakala S.B., Geraldo J.A., Lapp S.A., Barnwell J.W.,
RA Kissinger J.C., Galinski M.R., Humphrey J.C.;
RT "First high quality genome sequence of Plasmodium coatneyi using continuous
RT long reads from single molecule, real-time sequencing.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004163}. Membrane
CC {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004211}.
CC -!- SIMILARITY: Belongs to the synaptobrevin family.
CC {ECO:0000256|ARBA:ARBA00008025}.
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DR EMBL; CP016246; ANQ07865.1; -; Genomic_DNA.
DR RefSeq; XP_019914560.1; XM_020058952.1.
DR AlphaFoldDB; A0A1B1DZ33; -.
DR EnsemblProtists; ANQ07865; ANQ07865; PCOAH_00021450.
DR GeneID; 30908871; -.
DR VEuPathDB; PlasmoDB:PCOAH_00021450; -.
DR OrthoDB; 238575at2759; -.
DR Proteomes; UP000092716; Chromosome 8.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:InterPro.
DR CDD; cd14824; Longin; 1.
DR CDD; cd15866; R-SNARE_SEC22; 1.
DR Gene3D; 1.20.5.110; -; 1.
DR Gene3D; 3.30.450.50; Longin domain; 1.
DR InterPro; IPR006387; CPW_WPC_dom.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR InterPro; IPR010908; Longin_dom.
DR InterPro; IPR044565; Sec22.
DR InterPro; IPR042855; V_SNARE_CC.
DR NCBIfam; TIGR01492; CPW_WPC; 5.
DR PANTHER; PTHR45837; VESICLE-TRAFFICKING PROTEIN SEC22B; 1.
DR PANTHER; PTHR45837:SF3; VESICLE-TRAFFICKING PROTEIN SEC22B; 1.
DR Pfam; PF09717; CPW_WPC; 5.
DR Pfam; PF13774; Longin; 1.
DR Pfam; PF00957; Synaptobrevin; 1.
DR SMART; SM01099; CPW_WPC; 5.
DR SMART; SM01270; Longin; 1.
DR SUPFAM; SSF58038; SNARE fusion complex; 1.
DR SUPFAM; SSF64356; SNARE-like; 1.
DR PROSITE; PS50859; LONGIN; 1.
DR PROSITE; PS50892; V_SNARE; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU00290};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 6..124
FT /note="Longin"
FT /evidence="ECO:0000259|PROSITE:PS50859"
FT DOMAIN 139..199
FT /note="V-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50892"
FT REGION 227..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 266..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 87264 MW; E25E605BE8A324CF CRC64;
MCDVVLLCRV SDGMTLVETN SESKNIAHKI ELKKLCKRLQ SFPSLSTVTS NQFNYHFLIE
NGIAYIAVFP VTYPKKLAFL FLNDICKQFN EELMIQYGTH SIDYRSIIET IEKPYSFIKF
DRKISKIKQE YKDPRSNIAI KKLNESLNEV SSIMRKNIDD ILLRGENLED VGRKAFNLKY
ESEKFKKVSR VLSLRYTLYQ YGILIFENVQ LELLHIDATT NCSGEVNAGG KNELSHRSEQ
NEEVPKRGDR KIHKYNFGSL KKKLHIESKE QGTDVGGVEP SDQKEDNKNE EGTEVSTGKT
NGGKENLSPE EEYTKCIGMI EKELKGEEDA KIREELENLC SKKREQDEAE KAAVQAKEAK
SKLNEKAQLE THPHGGDTHN DCKRHIISQL GLSTKLDVPL EVLKESLSEV KNCVRDYTQK
CPLNWKVSET NEAFCVGPES YIGPCAKEIK NDLNEDEKMQ MEKKCSLFWK CDYKCVQDYE
GSVCPIDWVM EKEEEYDGYC ISPDGYTGKC MRKIKFSTMT SKEKAIYSNL CDIKWPCRKK
CTHDYSVLCP SGWIEGADGY CLATSSYSGN CEKKMYLKHL DEVMKQTYEH KCQFNYPCVH
SCEKNYSDVC PNLWIPVNEK ECTPSENYNG RCKHNYIFKG NILEEEKKNF EKMCHVSYPC
VKDCKRDYSF NCPIGWKETL SFCLAPTSYR HSCEKMMKKN MNEREKIQVS AKCLVFWPCS
NYEVVLKNLL HSNISPADYL SVVNGPVDDV TGAVLRLTG
//
