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Database: UniProt
Entry: G8B9K2_CANPC
LinkDB: G8B9K2_CANPC
Original site: G8B9K2_CANPC 
ID   G8B9K2_CANPC            Unreviewed;       230 AA.
AC   G8B9K2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=t-SNARE coiled-coil homology domain-containing protein {ECO:0000259|PROSITE:PS50192};
GN   OrderedLocusNames=CPAR2_302920 {ECO:0000313|CGD:CAL0000145497,
GN   ECO:0000313|EMBL:CCE41303.1};
OS   Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia
OS   parapsilosis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=578454 {ECO:0000313|EMBL:CCE41303.1, ECO:0000313|Proteomes:UP000005221};
RN   [1] {ECO:0000313|Proteomes:UP000005221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
RN   [2] {ECO:0000313|Proteomes:UP000005221}
RP   GENOME REANNOTATION.
RC   STRAIN=CDC 317 / ATCC MYA-4646 {ECO:0000313|Proteomes:UP000005221};
RX   PubMed=22192698; DOI=10.1186/1471-2164-12-628;
RA   Guida A., Lindstaedt C., Maguire S.L., Ding C., Higgins D.G., Corton N.J.,
RA   Berriman M., Butler G.;
RT   "Using RNA-seq to determine the transcriptional landscape and the hypoxic
RT   response of the pathogenic yeast Candida parapsilosis.";
RL   BMC Genomics 12:628-628(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-
CC       pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000256|ARBA:ARBA00009063}.
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DR   EMBL; HE605204; CCE41303.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8B9K2; -.
DR   STRING; 578454.G8B9K2; -.
DR   EnsemblFungi; CPAR2_302920-T; CPAR2_302920-T-p1; CPAR2_302920.
DR   CGD; CAL0000145497; CPAR2_302920.
DR   VEuPathDB; FungiDB:CPAR2_302920; -.
DR   eggNOG; KOG3202; Eukaryota.
DR   Proteomes; UP000005221; Chromosome 3.
DR   GO; GO:0005768; C:endosome; IEA:EnsemblFungi.
DR   GO; GO:0031090; C:organelle membrane; IEA:UniProt.
DR   GO; GO:0031201; C:SNARE complex; IEA:EnsemblFungi.
DR   GO; GO:0005802; C:trans-Golgi network; IEA:EnsemblFungi.
DR   GO; GO:0005484; F:SNAP receptor activity; IEA:EnsemblFungi.
DR   GO; GO:0006897; P:endocytosis; IEA:EnsemblFungi.
DR   GO; GO:0048193; P:Golgi vesicle transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0006906; P:vesicle fusion; IEA:EnsemblFungi.
DR   CDD; cd21444; SNARE_NTD_Tlg1p-like; 1.
DR   CDD; cd15851; SNARE_Syntaxin6; 1.
DR   Gene3D; 1.20.5.110; -; 1.
DR   Gene3D; 1.20.58.90; -; 1.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR015260; Syntaxin-6_N.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   InterPro; IPR048036; Tlg1p-like_N.
DR   PANTHER; PTHR19957:SF224; HL02043P; 1.
DR   PANTHER; PTHR19957; SYNTAXIN; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF09177; Syntaxin-6_N; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   SUPFAM; SSF47661; t-snare proteins; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005221};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        208..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          138..200
FT                   /note="T-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000259|PROSITE:PS50192"
FT   REGION          110..132
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          36..63
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   230 AA;  26354 MW;  399B71AD270BBE1C CRC64;
     MDPFNEVKDD AYSVIDRLES LIAQRISGRP PSTEQSQDFD NNYEELQEMR DDLQSALEQS
     AKDPSQFNLT SDDISQRQAI LQDLNRQISH LLQSWDNKKL RDVTTMSNRI SQDDENPFNI
     DTDSGGGGTT NMTSYQQQEL IQEQDVQLDD IHKTMMNLNQ QATMMGDELE DQGFMLDELD
     YEMDHVGSKL DRGMKRLNIF IERNKEKASN WCIGILAVVL CVLLVLLIVA
//
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