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Database: UniProt
Entry: A0A2J6T557_9HELO
LinkDB: A0A2J6T557_9HELO
Original site: A0A2J6T557_9HELO 
ID   A0A2J6T557_9HELO        Unreviewed;       774 AA.
AC   A0A2J6T557;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Protein transport protein SEC23 {ECO:0000256|ARBA:ARBA00021212, ECO:0000256|RuleBase:RU365030};
GN   ORFNames=K444DRAFT_614413 {ECO:0000313|EMBL:PMD58154.1};
OS   Hyaloscypha bicolor E.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Hyaloscyphaceae; Hyaloscypha; Hyaloscypha bicolor.
OX   NCBI_TaxID=1095630 {ECO:0000313|EMBL:PMD58154.1, ECO:0000313|Proteomes:UP000235371};
RN   [1] {ECO:0000313|EMBL:PMD58154.1, ECO:0000313|Proteomes:UP000235371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E {ECO:0000313|EMBL:PMD58154.1,
RC   ECO:0000313|Proteomes:UP000235371};
RG   DOE Joint Genome Institute;
RA   Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA   Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA   Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA   Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA   Martin F., Perotto S.;
RT   "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025471,
CC       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; KZ613828; PMD58154.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2J6T557; -.
DR   STRING; 1095630.A0A2J6T557; -.
DR   InParanoid; A0A2J6T557; -.
DR   OrthoDB; 5474700at2759; -.
DR   Proteomes; UP000235371; 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|ARBA:ARBA00023034,
KW   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:UP000235371};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT   DOMAIN          60..99
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          127..395
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          406..510
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          524..622
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          639..725
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
SQ   SEQUENCE   774 AA;  86329 MW;  FE11CAD16B991443 CRC64;
     MDIEALKEQW SEVEDRDGVR LSWNVFPSSR MEASRLVVPI GALYTPLKEK PDTPLLQFEP
     VICKQPCRSV LNPFCQVDVR ARLWICPFCL SRNPLPPHYK DITANAIPPE LHPSNTTIEY
     RLSRPAPSPP IFLYVVDTCQ EEDSLSALKE SLILSLSLLP ENALVGLVTF GTMAQVHEIG
     YTECPKSYVF RGSKDYSAKQ VQEMLGLTSP GLRPGMQQQQ PGRPMPPMGP AARFLLPVQQ
     CEFQLTKALE QLQKDPWPVA SDRRNLRCTG VALSVAVGLL ESSFQNAGGR IMLFAGGPAT
     EGPGLVVGPE LREPIRSHHD IDRDNIKYYK KALKFYDNLA KRTAHNGHII DIFAGCLDQV
     GLLEMKGLSN STGGHMVLTD SFTASMFKQS FVRIFEKDAD DNLLMGFNAS LEVLTTKELK
     VTGLIGHAVS MNKKSTSVGE TECGIGNTCS WKMCGIDPSA SYGIYFEIAS QGGPTQHQQT
     PQKGMMQFLT YYQHSSGQFH LRVTTVSRNL SGPAGDPAIA QSFDQEAAAV LMSRIAVFKA
     EVDDGPDVLR WVDRMLIRLC SRFADYRKDD PSSFRLEKNF TLYPQFMFHL RRSQFLQVFN
     NSPDETAFYR HVLNHEDVSN SLIMIQPTLD SYTFDQDGSQ PVLLDSTSIQ PTHILLLDTF
     FHILIFHGET VAEWRKAGYQ EQEGYENFAS LLEQPKEDAR DLITDRFPLP RFIVCDAGGS
     QARFLLSKLN PSTTHTTGAW GGVGAQTAQT IFTDDVSLQT FMDHLMKLAV SGTN
//
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