ID A0A167CUZ3_9HYPO Unreviewed; 925 AA.
AC A0A167CUZ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Protein transport protein SEC24 {ECO:0000256|ARBA:ARBA00021213};
DE AltName: Full=Protein transport protein sec24 {ECO:0000256|ARBA:ARBA00013453};
GN ORFNames=BBO_05597 {ECO:0000313|EMBL:OAA41611.1};
OS Beauveria brongniartii RCEF 3172.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria;
OC Beauveria brongniartii.
OX NCBI_TaxID=1081107 {ECO:0000313|EMBL:OAA41611.1, ECO:0000313|Proteomes:UP000076863};
RN [1] {ECO:0000313|EMBL:OAA41611.1, ECO:0000313|Proteomes:UP000076863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCEF 3172 {ECO:0000313|EMBL:OAA41611.1,
RC ECO:0000313|Proteomes:UP000076863};
RX PubMed=27071652; DOI=10.1093/gbe/evw082;
RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.;
RT "Divergent and convergent evolution of fungal pathogenicity.";
RL Genome Biol. Evol. 8:1374-1387(2016).
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:OAA41611.1}.
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DR EMBL; AZHA01000016; OAA41611.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A167CUZ3; -.
DR OrthoDB; 977017at2759; -.
DR Proteomes; UP000076863; 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 Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 246..283
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 320..561
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 567..650
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 661..762
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 789..859
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 1..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 925 AA; 101069 MW; 13CDAAD8763A2AFE CRC64;
MSAPTGDGFG QFQGQPQHQQ PDAQVDAGAA GAAPKKKKRG YAAGAFDVAT GANAGGQMPG
AAPPAPQYGG YPQVDMQQQQ QQQAAGGYQY GQTYGPPQPG APQQGYGGYP APDQAAQIGG
QDVAGITQGV AGLNMGAQQP PSMPMAPQAR QATLNQLYPS DLLSQPFNVA ELDLAPPPIN
LPPNSSVTRS ETANCPPKYI RSTLNAVPTT NSLLKKSKLP LSLVIQPYGS LHDDEDNVPV
VQDQVISRCR RCRTYINPYV TFMDHGHRWR CNMCNLTNDV PQAFDWDSAT QKTVDRWQRP
ELNHAVVEFV APQEYMVRPP QPLVYLFLFD VSYAAISSGL LATSARTILD SLNRIPNADR
RTRIGFMAVD ASLHYFSIPK DEDENAETNM LVVSDLEEPF LPVPHDLLVP LSESRQSVER
FLQKLPEMFQ NNQSNSSCMG PALRAGHKLI SSLGGKIIVL TASLPNVGAG KLEMREDKKV
LGTSKEGALL QTGNSFYKSF AVECSKNQVS VDMFLFSSQY QDVASLSNLP RYTGGQTWFY
PGWHASRPED ALKFASEFSD HLSSEIGLEA VLRVRATTGL RMNTFYGNFF NRSSDLCSFP
AFPRDQCYVV EVAIDENLTK NVVCFQAAIL HTTCNGERRI RVLTVALPTT TNLSDVYASA
DQCAITTYFT HKAVERVLSS GLDAARDALQ AKVTELLQTF RKELAGGSMG GGLQFPANLR
GLPILFLGLM KNVGLRKSAQ IPTDIRSAAL CLLSTLPVPL LMRYIYPRLY SLHDMPDTAG
VTDGETGQIV LPPPLNLTSE RLASHGLYLI DDGQTQFLWV GRDAVPQLVA DVFGVDDRTS
IHVGKGRVPE LEGDFNERVR AVVQKSRDHR SLGVGSITVP HLYIVREDGE PSLKLWAQTL
LVEDRADQSV SAAQWLGILR EKVVQ
//
