ID A0A2H1A7A7_CANAR Unreviewed; 798 AA.
AC A0A2H1A7A7;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN ORFNames=B9J08_000206 {ECO:0000313|EMBL:PIS58756.1};
OS Candida auris (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=498019 {ECO:0000313|EMBL:PIS58756.1, ECO:0000313|Proteomes:UP000230249};
RN [1] {ECO:0000313|EMBL:PIS58756.1, ECO:0000313|Proteomes:UP000230249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B8441 {ECO:0000313|EMBL:PIS58756.1,
RC ECO:0000313|Proteomes:UP000230249};
RX PubMed=27988485; DOI=.1093/cid/ciw691;
RA Lockhart S.R., Etienne K.A., Vallabhaneni S., Farooqi J., Chowdhary A.,
RA Govender N.P., Colombo A.L., Calvo B., Cuomo C.A., Desjardins C.A.,
RA Berkow E.L., Castanheira M., Magobo R.E., Jabeen K., Asghar R.J.,
RA Meis J.F., Jackson B., Chiller T., Litvintseva A.P.;
RT "Simultaneous emergence of multidrug-resistant Candida auris on 3
RT continents confirmed by whole-genome sequencing and epidemiological
RT analyses.";
RL Clin. Infect. Dis. 64:134-140(2017).
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|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU365030}. Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
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}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000256|ARBA:ARBA00009210, ECO:0000256|RuleBase:RU365030}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIS58756.1}.
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DR EMBL; PEKT02000001; PIS58756.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H1A7A7; -.
DR STRING; 498019.A0A2H1A7A7; -.
DR EnsemblFungi; B9J08_000206-t37_1; B9J08_000206-t37_1-p1; B9J08_000206.
DR VEuPathDB; FungiDB:B9J08_000206; -.
DR VEuPathDB; FungiDB:CJI96_0000934; -.
DR VEuPathDB; FungiDB:CJI97_000209; -.
DR VEuPathDB; FungiDB:CJJ07_001158; -.
DR VEuPathDB; FungiDB:CJJ09_001824; -.
DR VEuPathDB; FungiDB:QG37_02593; -.
DR OMA; AHYIYSI; -.
DR Proteomes; UP000230249; 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 InterPro; IPR029006; ADF-H/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; 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; 2.
DR SUPFAM; SSF81995; beta-sandwich 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|RuleBase:RU365030};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU365030};
KW ER-Golgi transport {ECO:0000256|RuleBase:RU365030};
KW Golgi apparatus {ECO:0000256|RuleBase:RU365030};
KW Membrane {ECO:0000256|RuleBase:RU365030};
KW Metal-binding {ECO:0000256|RuleBase:RU365030};
KW Protein transport {ECO:0000256|RuleBase:RU365030};
KW Reference proteome {ECO:0000313|Proteomes:UP000230249};
KW Transport {ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|RuleBase:RU365030}.
FT DOMAIN 114..317
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 340..394
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 552..664
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT REGION 765..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 768..783
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 89376 MW; B05CBF733944AE5C CRC64;
MEVKFNWDAL PSTKLEASRL STPLGCLIRK NSAKVPTLTS FPTKCSNCGA FTSIYTKYDT
TSDTIFCPFC QSNSKLETGT YPQEIDFQSI GESDDTFDYV LPTDIAQPIV SRGPVVLFVV
DTYQHVECPK EMAALKKRLI ECISEIPPET PVGLITFNRD VTLHSKISDI DISVDDFPST
SDLNDILGNK PMLAHILLKI ANNSKNNIWK GQNLLQSGYF FSPSELIQRV NELSSMPTRS
FKSERASGLA LLVASLLLSS ASSSSLLGKV MFFSSGPCTI GPGLVVKSAE NIRTHDDIAN
MKARHFADSS KFYRALSYVA CGYTLSQAND AAFSLNVSLT DFAVKPSAPK FSINLFFGAL
DQVGLYEMSP MSSGTGGSII FSDSFESHSF GSKLMAITPT LSDQDNCITV MTSTGLKVSY
SLNYGTPYQS SYQYGNASNF HHQRISDTIT GFESSLRKRY FTNRWYLGDL RDSVSCVLFE
VDPLALNGKD VYIQFQLEWW SHELQKRVIR SSTLRKQTTL STFLGKVGEF SKITKKVSES
ARHKALLSSF NPDTWITILT RLLINKIDTT LGFESFEEVI DIMDSTLIRI TNLFGNIQKE
ASVSENPFEK LKTLYSIDEH FKSLPIYGYY LRRNPQLVSI FNSSPDETAY FHHIFMGLGV
EESCIFIQPK LYEVCGRALS PRPLLTTSIQ SKDDGIFYVL DTYHTIIIYL HCNKNKLRLH
SSDNDDIIYG RKLEKINRIL DIVESELTTS RTFVPKLVLT QTGHSQASGW KEDKEEMVAT
RETPEANNER GYQLGEVS
//
