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Database: UniProt
Entry: J4KQV9_BEAB2
LinkDB: J4KQV9_BEAB2
Original site: J4KQV9_BEAB2 
ID   J4KQV9_BEAB2            Unreviewed;      1018 AA.
AC   J4KQV9;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Transport protein sec24 {ECO:0000313|EMBL:EJP69884.1};
GN   ORFNames=BBA_00753 {ECO:0000313|EMBL:EJP69884.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP69884.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP69884.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP69884.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(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|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; JH725151; EJP69884.1; -; Genomic_DNA.
DR   RefSeq; XP_008594072.1; XM_008595850.1.
DR   AlphaFoldDB; J4KQV9; -.
DR   STRING; 655819.J4KQV9; -.
DR   GeneID; 19883765; -.
DR   HOGENOM; CLU_004589_1_0_1; -.
DR   InParanoid; J4KQV9; -.
DR   OrthoDB; 977017at2759; -.
DR   Proteomes; UP000002762; 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   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; 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:SF4; SECRETORY 24CD, ISOFORM C; 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   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          293..331
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          371..614
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          621..705
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          727..828
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          857..902
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..77
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          98..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          153..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1018 AA;  110478 MW;  640E743BCB39994A CRC64;
     MADYNQFHAL GHGEQYDPND PNKTTAPAAQ QFMPPVAPNP YQQQQQYGAP PYHGGQAPPM
     SGLPSPGFQG GAPPPQQDAL AAQMGGMSLG GDVQGTVRRK KKDRHAYHTV EPTGSSQAFN
     GMPTAGVGAS QFLNNSGSPS IPAFGNQFDS QGAPHTQYGA PAASPLGGPI NPITGSTSGD
     AAASVPASGQ GKVSADDLPS VPAARDAIQQ YFLNNIYPTF EKHVPPPASV SFVAHDQGNS
     SPKYARLTMN NVPATPDGLQ ATGIPLGLLL QPLAPLQAGE AEIPVLDFGE AGPPRCRRCR
     AYINPLMMFR SGGNKFVCNL CTYPNDTPPE YFCATSPQGV RVDRDQRPEL HRGTVEFVVP
     KEYWTRPPVG LRFLFLIDVT QESFNKGFLE SFCDGIQAAL YGGEIGEDGE PKRRIPEGAK
     VGFVTYDQDI HFYNINPGLD QAHMLIMPDL EDPFLPLGEG LFVDPYECKS TITSLLNRLP
     EMFSTVKNPE PAMLAALSSG LAALEATGGK VICSCAALPT WGPGRLFLRD DGSHPGGESD
     KKLYTTEHPG WKKVSEKMAA SGVGVDFFLA APSGGYLDIG TIGHVAATTG GETFYYPNFI
     APRDSPRLST EIAHAVTRET GFQALMKVRC SNGLQIAAYH GNFVQHTFGA DLEIGVIDAD
     KALGVSFSYD GKLDAKLDAH FQSALLYTTA SGQRRVRCSN IIASVSDTSK EAGVREQGIR
     ACMKFVDQDA VIALLAKEAS TKLSTTSSSL KDTRNWLTER TIDIMSCYRK HSAQQHPPGQ
     LVMPERLKEF CMYMLGLLKC RAYKGGIENT DRRVYEMRLV RSMGALELSL YLYPRMIPLH
     NLNPEDGFAD AETGHLKMPP CVRASFSRVE PGGVYLVDNG QQCLIWFHAQ TSPNLISDLF
     GEGKDTLKSL DAYTSSLPVL DTHLNAQARN IIEFLKTQRG SKGMNIQLAR QGIDGAEFEF
     ARLLVEDRNN EAQSYVDWLV HVHKGVQLEL SGQRKRETEA DNAANSLTNF AGLRPSYW
//
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