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Database: UniProt
Entry: A0A1Y2WTK1_9PEZI
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ID   A0A1Y2WTK1_9PEZI        Unreviewed;       955 AA.
AC   A0A1Y2WTK1;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Protein transport protein SEC24 {ECO:0000256|ARBA:ARBA00021213};
DE   AltName: Full=Protein transport protein sec24 {ECO:0000256|ARBA:ARBA00013453};
GN   ORFNames=K445DRAFT_66235 {ECO:0000313|EMBL:OTB12507.1};
OS   Daldinia sp. EC12.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Hypoxylaceae; Daldinia.
OX   NCBI_TaxID=1001832 {ECO:0000313|EMBL:OTB12507.1, ECO:0000313|Proteomes:UP000243732};
RN   [1] {ECO:0000313|EMBL:OTB12507.1, ECO:0000313|Proteomes:UP000243732}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC12 {ECO:0000313|EMBL:OTB12507.1,
RC   ECO:0000313|Proteomes:UP000243732};
RX   PubMed=28078400; DOI=10.1007/s00253-017-8091-1;
RA   Wu W., Davis R.W., Tran-Gyamfi M.B., Kuo A., LaButti K., Mihaltcheva S.,
RA   Hundley H., Chovatia M., Lindquist E., Barry K., Grigoriev I.V.,
RA   Henrissat B., Gladden J.M.;
RT   "Characterization of four endophytic fungi as potential consolidated
RT   bioprocessing hosts for conversion of lignocellulose into advanced
RT   biofuels.";
RL   Appl. Microbiol. Biotechnol. 101:2603-2618(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|ARBA:ARBA00025471}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC       membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC       {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC       {ECO:0000256|ARBA:ARBA00004255}.
CC   -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008334}.
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DR   EMBL; KZ112954; OTB12507.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2WTK1; -.
DR   STRING; 1001832.A0A1Y2WTK1; -.
DR   OrthoDB; 977017at2759; -.
DR   Proteomes; UP000243732; 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   CDD; cd01479; Sec24-like; 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; 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; IPR041742; Sec24-like_trunk_dom.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   InterPro; IPR006895; Znf_Sec23_Sec24.
DR   InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR   PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
DR   PANTHER; PTHR13803:SF39; SECRETORY 24AB, ISOFORM A; 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|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243732};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          276..313
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          350..591
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          597..680
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          691..793
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          820..892
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   955 AA;  103988 MW;  0872E8311B01FF48 CRC64;
     MAAPNDGYGQ YPPQEYGQEA PYSDQPPAGY EGQTSPPPQA ASHHDGKKKK RGYATQAFEF
     GSGANAGATV PTPGGITPGY GGPVPGPQPS PGYAGGGAYP TPDFQQGGYG SPAPGQVPYG
     APQQPGVPQP GLGGYQAPDP YYQPGVGQPP PGVAGITQGM AGMNMGPGPQ PAVQQPGQQA
     RIALNQLYPT DLLNQPFNVS ELDLPPPPCI LPPNASVTQS PDANCPPKYI RSTLNAVPTT
     HSLLKKSKLP FALVIQPYAA LHDIDDPVPV VQDQVIARCR RCRTYINPYV IFLDQGHRWR
     CNMCNLTNDV PQAFDWDAAA QKSVNRWDRH ELNHAVVEFV APQEYMVRPP QPLVYLFLFD
     VSYAAVSTGL LATSARTILD SLNRIPNADR RTRLGFIAVD SSLHYFSVPK DDEENAETSM
     LVISDLDEPF LPVPHDLLVP LIESRNSIEN FLTKLPDMFQ NNQSNGSCMG SALRAGHKLI
     SPLGGKIVVL SASLPNLGVG KLDMREDKKL LGTSKESGLL QTANSFYKSF AVECSKNQVS
     IDMFLFSSQY QDVASLSNLP RYTGGQTWFY PGWNAGRAED AVKFASEFSD YLSSEIGLEA
     VLRVRATTGL RMSTFYGNFF NRSSDLCAFP AFPRDQCYVV EVAIDETLQK NYVCLQAGVL
     YTTCNGERRI RVMTLAIPTT TNLADVYASA DQCAITTYFT HKAVERALSS GLDAARDALQ
     SKLIELLQTF KKELGGGSMG GGGLQFPANL RGLPVLFLGL IKHVGLRKSA QIPSDLRSAA
     LCLLSTLPLP LLMQYIYPRL YSLHDMPDNA GVPDPETSQI VLPPPLNLSS ERFVSYGLYL
     IDDGQTQFLW VGRDAVPQLL TDVFGVADRT QLRVGKGSIP ELDNDFNERV RAVIQKSRDH
     LSRGVGSIIV PHLYIVREDG EPSLKLWAQT LLVEDRADQG MSFGQWMGTL REKVS
//
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