SEC9_CANAL
ID SEC9_CANAL Reviewed; 530 AA.
AC Q59XP0; A0A1D8PPI9; Q59WT5;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Protein transport protein SEC9 {ECO:0000305};
GN Name=SEC9; OrderedLocusNames=CAALFM_C601100WA;
GN ORFNames=CaO19.117, CaO19.7764;
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:0000305}; Peripheral membrane
CC protein {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Leads to defects in secretion of degradative
CC enzymes and defects in hyphal extension. {ECO:0000269|PubMed:24911595}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; CP017628; AOW30056.1; -; Genomic_DNA.
DR RefSeq; XP_714323.2; XM_709230.2.
DR AlphaFoldDB; Q59XP0; -.
DR SMR; Q59XP0; -.
DR STRING; 237561.Q59XP0; -.
DR PRIDE; Q59XP0; -.
DR GeneID; 3644052; -.
DR KEGG; cal:CAALFM_C601100WA; -.
DR CGD; CAL0000200439; SEC9.
DR VEuPathDB; FungiDB:C6_01100W_A; -.
DR HOGENOM; CLU_020823_1_0_1; -.
DR InParanoid; Q59XP0; -.
DR OrthoDB; 1358184at2759; -.
DR PRO; PR:Q59XP0; -.
DR Proteomes; UP000000559; Chromosome 6.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:EnsemblFungi.
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:0019905; F:syntaxin 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:0009306; P:protein secretion; IMP:CGD.
DR GO; GO:0035493; P:SNARE complex assembly; IEA:EnsemblFungi.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR InterPro; IPR000727; T_SNARE_dom.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Membrane; Protein transport; Reference proteome; Transport; Virulence.
FT CHAIN 1..530
FT /note="Protein transport protein SEC9"
FT /id="PRO_0000431521"
FT DOMAIN 313..375
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 467..529
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 58712 MW; E779837A1C25D669 CRC64;
MGIKKMFQKK EPTEQEIREE LSRVGISTRS NNTRQEKFGA FKNYAQERAN MKPQLGPVGG
NPYANINPGT NNNNNNPYAN DNGNNSTGNP NNNSNSNNGG NPYGGGVTNN NPYGGSGGNG
RGSSPSPYAP TTSTTTRSSN PYGNNNGSRS SQNTSSPYAK STNNSSYSNS PYSGSTVNNG
NRGGHSNNSN SSAGGNPYAA GGRSSQSQNS RDNVYTAPAT RTSTRQTQGY GGGDTDSTLD
LNAIPSHQMF DNKKPIKRNQ QSSQQPANDY NLDLNDEYGE EEDLNLDISE VPEEQQQINS
EDEEVEAIKQ DIKFVKQESV QSTRNTLRMA QEADASGTNT LGMLGSQSER LYNAEQNLLL
AETQTQIADE KVKELKRLNR SIFIPANGNP FNKKSRLRQQ EEKIKNQKLQ EKYIRENNRQ
EMFASEQRIK QGITNNSTNN DVYNKYQDEK NLSAAKRYQF ENDSEDDDME KEIASNLNQI
DQYAKKLKGL ANTMGTEVDN QNTRLKKIEE SADKLDINVH MNTTRLNNIR
