ID A0A093XGZ3_9PEZI Unreviewed; 948 AA.
AC A0A093XGZ3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Protein transport protein SEC24 {ECO:0000256|ARBA:ARBA00021213};
DE AltName: Full=Protein transport protein sec24 {ECO:0000256|ARBA:ARBA00013453};
GN ORFNames=V490_05620 {ECO:0000313|EMBL:KFX91975.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX91975.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX91975.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX91975.1,
RC ECO:0000313|Proteomes:UP000029320};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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:KFX91975.1}.
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DR EMBL; JPJS01001621; KFX91975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093XGZ3; -.
DR STRING; 1437433.A0A093XGZ3; -.
DR HOGENOM; CLU_004589_2_1_1; -.
DR Proteomes; UP000029320; 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:UP000029320};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 268..304
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 342..583
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 589..672
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 683..785
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 812..885
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 1..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 948 AA; 103629 MW; 1CC903F3E0CACF08 CRC64;
MSAPQEGYPP QGYPQQEQYG EQQPQPGFGA AAPAPAEEHQ DSHGGKKKKR GYAAQAYDFG
AGGNAALGGQ PPNPENFAPV GAPAYGGYPA PGDQPAYTGN QPYTDSPQPP AASTFGQSAL
SGLGGYQAPQ QAQTGYPGPG APPGGDVGGI TQGMGQMGIA PQAAQAGAGA IPRVALNQLY
PTDLLNQPFN VAELELPPPP IILPPNSSVT PSPDSNCSHK FIRSTLNAVP TTNNLLKKSK
LPFALVIQPY TSLHDADDPV PVIQDQIISR CRRCRSYINP YVTFLDHGHR WRCNMCNLTN
DVPQGFDWDA ATQQSVDRWQ RAELNHAVVE FVAPQEYMVR PPQPLVYLFL FDVSYNAVNN
GLLATSARTI LDSLNRIPNA DRRTRLGFMA VDSSLHYFTI PKDTEENGET NMLVVSDLDE
PFLPIPQELL VPLSESRTNI EAFLTKLPSM FQNNVITTSC MGSALRAGHK LISPLGGKLV
VLTATLPNVG YGKLDLREDP KALGTSKEGA LLQTQNSFYK SFAVECSKNQ VSIDMFLFSS
QYQDVASLSN LPRYTGGQTY FYPGWSAVRS EDAIKFASEF SDYLSSEIGL EAVLRVRATT
GLRMNTFYGN FFNRSSDLCA FPAFPRDQAY VVEVAIDESL TKNFICMQAA VLHTTSNGER
RIRVMTLSLP TTTILADLYA SADQCAITTY FSHKAVERAL SNGLESARES LQSKLIELLQ
TFKKELAGGN MGGGGLQFPA NLRGLPTLFL GLIKNLGLRK SAQIPSDLRS AALCLLSTLP
LPLMMQYIYP RLYSLHDMPD NVGIPDPETS EIVLPAPLSL SSERLVPYGL YLITDGQTQF
LWVGRDAVPQ LLEDVFGVPD RTQVKVGKSS LPELDNDFNE RIRAVMLKCK DYRSRGVGSI
IQPHLYIVKE DGDPSLKLWA QTMLLEDRAD QGMSFQQWMG TLREKVMQ
//
