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SSO2_CANAL
ID   SSO2_CANAL              Reviewed;         295 AA.
AC   Q59YF0; A0A1D8PIJ6;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Protein transport protein SSO2 {ECO:0000305};
GN   Name=SSO2; OrderedLocusNames=CAALFM_C209740WA;
GN   ORFNames=CaO19.1376, CaO19.8956;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=24911595; DOI=10.1111/1567-1364.12165;
RA   Bernardo S.M., Rane H.S., Chavez-Dozal A., Lee S.A.;
RT   "Secretion and filamentation are mediated by the Candida albicans t-SNAREs
RT   Sso2p and Sec9p.";
RL   FEMS Yeast Res. 14:762-775(2014).
CC   -!- FUNCTION: Late secretory t-SNARE protein required for secretion and
CC       proper cytokinesis. Plays an important role in the secretion of
CC       virulence-associated extracellular enzymes and vesicle-mediated
CC       polarized hyphal growth. {ECO:0000269|PubMed:24911595}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type IV
CC       membrane protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Leads to defects in secretion of degradative
CC       enzymes and defects in hyphal extension. Leads also to the
CC       Spitzenkoerper dissipation and accumulation of secretory vesicles.
CC       {ECO:0000269|PubMed:24911595}.
CC   -!- SIMILARITY: Belongs to the syntaxin family.
CC       {ECO:0000255|RuleBase:RU003858}.
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DR   EMBL; CP017624; AOW27952.1; -; Genomic_DNA.
DR   RefSeq; XP_714550.1; XM_709457.1.
DR   AlphaFoldDB; Q59YF0; -.
DR   SMR; Q59YF0; -.
DR   STRING; 237561.Q59YF0; -.
DR   PRIDE; Q59YF0; -.
DR   GeneID; 3643809; -.
DR   KEGG; cal:CAALFM_C209740WA; -.
DR   CGD; CAL0000181188; SSO2.
DR   VEuPathDB; FungiDB:C2_09740W_A; -.
DR   eggNOG; KOG0810; Eukaryota.
DR   HOGENOM; CLU_042423_0_1_1; -.
DR   InParanoid; Q59YF0; -.
DR   OMA; RWICFIL; -.
DR   OrthoDB; 1033833at2759; -.
DR   PRO; PR:Q59YF0; -.
DR   Proteomes; UP000000559; Chromosome 2.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:1903561; C:extracellular vesicle; IDA:CGD.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0030448; P:hyphal growth; IMP:CGD.
DR   GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0009306; P:protein secretion; IMP:CGD.
DR   GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR   GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR   InterPro; IPR010989; SNARE.
DR   InterPro; IPR045242; Syntaxin.
DR   InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR   InterPro; IPR006011; Syntaxin_N.
DR   InterPro; IPR000727; T_SNARE_dom.
DR   PANTHER; PTHR19957; PTHR19957; 1.
DR   Pfam; PF05739; SNARE; 1.
DR   Pfam; PF00804; Syntaxin; 1.
DR   SMART; SM00397; t_SNARE; 1.
DR   SUPFAM; SSF47661; SSF47661; 1.
DR   PROSITE; PS00914; SYNTAXIN; 1.
DR   PROSITE; PS50192; T_SNARE; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Membrane; Protein transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Virulence.
FT   CHAIN           1..295
FT                   /note="Protein transport protein SSO2"
FT                   /id="PRO_0000431520"
FT   TOPO_DOM        1..270
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        271..291
FT                   /note="Helical; Anchor for type IV membrane protein"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        292..295
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          196..258
FT                   /note="t-SNARE coiled-coil homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          33..110
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   295 AA;  34308 MW;  A581E7789494B544 CRC64;
     MSNPYQNSQN GYQQNNSYEL NNYPNKQYSS SNEDDFVQFM NEIQDINSQL DNYSNIINLI
     DNKQKNFLHG LDLNDEDTDY DSKQIENLVN EAQSLQLDLK NRIKNVQTQA VHSRDQTKVD
     QAETCRKRFL DLIQDYRLVE ARNKESTKEQ AARQYQIIKP DATDEEIKAV VEDGSQQYFQ
     QALMQSNRRG EARSVLNEVQ VRHRELLKLE KTMAELTQLF HDMEELVIEQ DQPIQQIEEQ
     VGTAQHDIEQ GVGHTNKAVK SAKSARKKKL WCFFICLLIV IILAVILGAY FGTRK
 
 
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