ID K1V5N5_TRIAC Unreviewed; 763 AA.
AC K1V5N5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 28-JUN-2023, entry version 43.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN ORFNames=A1Q2_06499 {ECO:0000313|EMBL:EKC99299.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC99299.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC99299.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC99299.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
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}.
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:EKC99299.1}.
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DR EMBL; AMBO01000373; EKC99299.1; -; Genomic_DNA.
DR AlphaFoldDB; K1V5N5; -.
DR STRING; 1220162.K1V5N5; -.
DR eggNOG; KOG1986; Eukaryota.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; K1V5N5; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 5474700at2759; -.
DR Proteomes; UP000006757; 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:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd01478; Sec23-like; 1.
DR CDD; cd11287; Sec23_C; 1.
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; IPR007123; Gelsolin-like_dom.
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; IPR012990; Sec23_24_beta_S.
DR InterPro; IPR037550; Sec23_C.
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; PF00626; Gelsolin; 1.
DR Pfam; PF08033; Sec23_BS; 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:UP000006757};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT DOMAIN 56..95
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 123..388
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 399..501
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 514..612
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 626..714
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
SQ SEQUENCE 763 AA; 85238 MW; 07595483C1D530D0 CRC64;
MNGANFEDVE DRDGVRFSWN AWPSSRIEAT RTVVPISALY TPLKERDDLP PVHYEPVTCK
APCKAILNPY CQIDVRGKMW ICPFCLQRNP FPPHYKDISQ TNLPAELLPK YTTIEYTLTR
PVPVPPIFLY VVDTCVDEDE LTALKETLMV SINLLPANAL VGLITFGTMA MVHELAYAEC
PKSYVFRGSK EYQPKQIADM LGLNPSNRPM AGMRPGQPMP APAASRFLMP QQACEFQLNN
ILENLQRDPW PVADNRRPLR CTGVALGVAT SLLESAFPNT GARIMLFSGG PCTEGPGMVV
GPELREPIRS HHDIERDSVK HFKKATKYYE GLSKRASVNG HAVDIYAGCL DQVGLLEMKS
LPNSTNGFMV ISDSFMTAIF KQSFLRTFNK DDQGFLKMGF NGTFDVQTTK ELKISGVIGH
VISANKKSPC VGETEIGIGG TSAWKICSLT DKTSLGVYFE VVTPAGQPLQ PNQNGLIQFV
THYQHSSGFY RLRVTTVART FHEGGHPNIA AQFDQEAAAV LMARIATFKA EIDDAPDVLR
WLDRMLIRLC QKFADYRKED PSSFQLSPNF SIYPQFMFHL RRSQFLQVFN NSPDETAFYR
HVLNDADVNN SLIMIQPTLM SYTFDQEPHP VLLDSVSIRP DVILLLDTFF HILIFHGETI
AQWRKANYQD QEDYANFKEL LEAPVADAQE LLEDRLPIPR YVVCDQGGSQ ARFLMAKLNP
STTHTSGTGY GAGAGGQAIF TDDVSLQVFM EHLKRLAVGA STS
//
