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Database: UniProt
Entry: C5MA77_CANTT
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Original site: C5MA77_CANTT 
ID   C5MA77_CANTT            Unreviewed;       857 AA.
AC   C5MA77;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN   ORFNames=CTRG_02389 {ECO:0000313|EMBL:EER33571.1};
OS   Candida tropicalis (strain ATCC MYA-3404 / T1) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=294747 {ECO:0000313|EMBL:EER33571.1, ECO:0000313|Proteomes:UP000002037};
RN   [1] {ECO:0000313|EMBL:EER33571.1, ECO:0000313|Proteomes:UP000002037}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-3404 / T1 {ECO:0000313|Proteomes:UP000002037};
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).
CC   -!- FUNCTION: Component of the coat protein complex II (COPII) which
CC       promotes the formation of transport vesicles from the endoplasmic
CC       reticulum (ER). The coat has two main functions, the physical
CC       deformation of the endoplasmic reticulum membrane into vesicles and the
CC       selection of cargo molecules. {ECO:0000256|RuleBase:RU365030}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365030}.
CC       Cytoplasmic vesicle, COPII-coated vesicle membrane
CC       {ECO:0000256|ARBA:ARBA00004299, ECO:0000256|RuleBase:RU365030};
CC       Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299,
CC       ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004299, ECO:0000256|RuleBase:RU365030}.
CC       Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397,
CC       ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397, ECO:0000256|RuleBase:RU365030};
CC       Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397,
CC       ECO:0000256|RuleBase:RU365030}. Golgi apparatus membrane
CC       {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC       {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC       {ECO:0000256|RuleBase:RU365030}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004287}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC       {ECO:0000256|ARBA:ARBA00009210, ECO:0000256|RuleBase:RU365030}.
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DR   EMBL; GG692397; EER33571.1; -; Genomic_DNA.
DR   RefSeq; XP_002548092.1; XM_002548046.1.
DR   AlphaFoldDB; C5MA77; -.
DR   STRING; 294747.C5MA77; -.
DR   EnsemblFungi; CTRG_02389-t43_1; CTRG_02389-t43_1-p1; CTRG_02389.
DR   GeneID; 8301680; -.
DR   KEGG; ctp:CTRG_02389; -.
DR   VEuPathDB; FungiDB:CTRG_02389; -.
DR   eggNOG; KOG1986; Eukaryota.
DR   HOGENOM; CLU_333436_0_0_1; -.
DR   OrthoDB; 2046817at2759; -.
DR   Proteomes; UP000002037; Unassembled WGS sequence.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR   Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR   Gene3D; 3.40.20.10; Severin; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR   InterPro; IPR036180; Gelsolin-like_dom_sf.
DR   InterPro; IPR037364; Sec23.
DR   InterPro; IPR006900; Sec23/24_helical_dom.
DR   InterPro; IPR036175; Sec23/24_helical_dom_sf.
DR   InterPro; IPR006896; Sec23/24_trunk_dom.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR11141; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR   PANTHER; PTHR11141:SF0; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR   Pfam; PF04815; Sec23_helical; 1.
DR   Pfam; PF04811; Sec23_trunk; 1.
DR   Pfam; PF04810; zf-Sec23_Sec24; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR   SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|RuleBase:RU365030};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW   ECO:0000256|RuleBase:RU365030};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW   ECO:0000256|RuleBase:RU365030};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW   ECO:0000256|RuleBase:RU365030};
KW   Golgi apparatus {ECO:0000256|RuleBase:RU365030};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365030};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU365030};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|RuleBase:RU365030};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002037};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT   DOMAIN          55..91
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          133..344
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          578..693
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
SQ   SEQUENCE   857 AA;  98702 MW;  E0B4594DFE7D5F26 CRC64;
     MMSNQGEPHT ATIQFNWNVL PVTRLEESQI VAPLGCLYSP FSNETEAIPH TTNLPITCSS
     CQTYLNPFIK LDRKNGMWWC PFCEKRSYLP EYLPIPEAIN SVNDWPIEMR ETSSTIDYHL
     PEDITTPTND NIPLVYYIVI DTYQQFADLS FKSLIKSIIQ ILHKLPFGSL IGLMTFNKSV
     QIHNMVKNEM IDVSIGDILT STSYTKLFQE ETITCLLRKL NLSPRVMDSN ENKLLDAGYL
     IELNPSSIGF ITDYIRNLNG LYTESFKPPR CTGFAHYVYS IMFSQLGFRN FMGKVLFFTS
     GPCTEFPGKI VGEKDQMRTH KDIYALEADN FTASSKYYTL LSYIACGQSV KKSLEIYKSS
     SLKTTKYDID PIAPVWSVNL IVGSLDQVGA YEMKPLIGNS SGIVYLLETF DSYLLPQMIS
     SCIDSTKRKV TLEVSTSNGL KTSKLISNGN YALPSSYHRA SKFHHLYHDK IDDELGEFDS
     PQFKGGFTNK WKFNELSQDD TLSLFFKMET IRSNSELTKS GISQVYIQFK IKYWDPEERK
     WILRITTLRK PTTLAYLNID SNRKSEIYKD HKFLLGFNQK VWVVLLARLI INKIDTNLGY
     SSFDKVVHLI DRTMIKLLYH FGGISVNSNQ PQSSNPYYRL RTMYEINENF RALPSLIYNL
     KRNLNLIKIF NSSPDETAFC HLWFLRMNSE LSLTVIEPVL CNVEGEKVTR LPLDSSCLES
     AKSESFLVLD SGFLLVVYYQ YSQDDKLPLH PSNNDAMIED RNELLPWKFI SDLLKDRKIV
     TKVVFTQRNH SQARFLLSRL GPVEEDIPNM NQLDINKSSS YWSFLKPSKN KTRVITDDLT
     LKQYYDNLVK QVKNYHV
//
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