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