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Database: UniProt
Entry: A0A369GJ36_9HYPO
LinkDB: A0A369GJ36_9HYPO
Original site: A0A369GJ36_9HYPO 
ID   A0A369GJ36_9HYPO        Unreviewed;       952 AA.
AC   A0A369GJ36;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Protein transport protein SEC24 {ECO:0000256|ARBA:ARBA00021213};
DE   AltName: Full=Protein transport protein sec24 {ECO:0000256|ARBA:ARBA00013453};
GN   ORFNames=CP532_0948 {ECO:0000313|EMBL:RDA82852.1};
OS   Ophiocordyceps camponoti-leonardi (nom. inval.).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX   NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA82852.1, ECO:0000313|Proteomes:UP000252748};
RN   [1] {ECO:0000313|EMBL:RDA82852.1, ECO:0000313|Proteomes:UP000252748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA82852.1,
RC   ECO:0000313|Proteomes:UP000252748};
RA   Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA   Luangsa-Ard J.-J., Giraud T.;
RT   "A genome scan of diversifying selection in the zombie-ant fungus
RT   Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT   coevolution and host-specificity.";
RL   Submitted (OCT-2017) 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   -!- 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}.
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:RDA82852.1}.
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DR   EMBL; PDHP01000247; RDA82852.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A369GJ36; -.
DR   STRING; 2039875.A0A369GJ36; -.
DR   Proteomes; UP000252748; 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:UP000252748};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          274..311
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          348..589
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          595..678
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          689..791
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          818..889
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..136
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   952 AA;  104509 MW;  B27014D1659554D7 CRC64;
     MSAPPNDGYG QFPGQQHLQQ PQQHLDQAGN PVQPDAGAPA VVQGKKKKRG YAAQAFDVGS
     GPNAAQMPGL GQPQLQPQYG IPPAHQQAQG YVGYSQPDAQ QQQQQQQAYQ QGYGAPQPGF
     QQQQQQQPQP QPSYGGYQAP DQGYPTPGAA GITQGMAGMH LGGQQQQQQP QMGQQAPRAG
     PLNHLYPTDL TNQPFSVAEL DIPPPPIVLP PNTSVTSSPN ANCPPRYVRS TLNAVPTTNS
     LLKKSKLPFA LVVQPYGALH DDEDPVPVVQ DQIISRCRRC RTYINPFVTF LDHGHRWRCN
     MCNLSNDVPQ AFDWDAAAQQ AADRWQRYEL NHSVVEFVAP QEYMVRPPQP LVYLFLFDVS
     YAAASNGLLA TSARTILDSL SRIPNADRRT RLGFLAVDAS LHYFSIPKDE DENGDTNMLV
     VSDLDEPFLP VPHDLLVPLT ESRQSIERFL QKLPDMFQHN QSNGSCMGSA LRAGHKLISA
     LGGKIVVLTA SLPNIGAGKL EMREDKKLLG SSKEGGLLQT GSSFYKSFAV ECSKNQVSID
     MFLFSSQYQD VASLSNLPRY TGGQTWFYPG WHASRPEDAL KFASELSDYL SSEIGLEAVL
     RVRATTGLRM NTFYGNFFNR SSDLCAFPAF PRDQCYVVEV AIDENINKNF VCLQTAVLHT
     TCNGERRIRV LTLALPTTTN LSDMYASADQ CAITTYFSHK AVERTLSSGL EAARDALQAK
     LTELLQTFKK ELGGGSMGGG GLQFPANLRG LPVLFLGLIK NVGLRKSTQI PSDIRSAALC
     LLSTLPVPLL MRYIYPRLYS LHDMPDSAGV PDGETGQIVL PPPVNLTSER LAPHGLYLID
     DGQTQFLWVG RDAVPQLVAD VFGVEDRTQV QVGKTRVPEL ATDFNERVRA VIQKSRDHRS
     LGVGSITVPH LYVVREDGEP SLKLWAQTLL VEDRADQSVS AAQWLGVLRE KV
//
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