ID A0A094EM44_9PEZI Unreviewed; 774 AA.
AC A0A094EM44;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|ARBA:ARBA00021212, ECO:0000256|RuleBase:RU365030};
GN ORFNames=V498_09316 {ECO:0000313|EMBL:KFY77488.1};
OS Pseudogymnoascus sp. VKM F-4517 (FW-2822).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420911 {ECO:0000313|EMBL:KFY77488.1, ECO:0000313|Proteomes:UP000029270};
RN [1] {ECO:0000313|EMBL:KFY77488.1, ECO:0000313|Proteomes:UP000029270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4517 (FW-2822) {ECO:0000313|Proteomes:UP000029270};
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 ECO:0000256|RuleBase:RU365030}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365030}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004299, ECO:0000256|RuleBase:RU365030};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004299,
CC ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299, ECO:0000256|RuleBase:RU365030}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397,
CC ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397, ECO:0000256|RuleBase:RU365030};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397,
CC ECO:0000256|RuleBase:RU365030}. Golgi apparatus membrane
CC {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU365030}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000256|ARBA:ARBA00009210, ECO:0000256|RuleBase:RU365030}.
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:KFY77488.1}.
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DR EMBL; JPKA01004060; KFY77488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EM44; -.
DR HOGENOM; CLU_008658_3_0_1; -.
DR Proteomes; UP000029270; 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:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd01478; Sec23-like; 1.
DR CDD; cd11287; Sec23_C; 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; IPR037364; Sec23.
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; IPR037550; Sec23_C.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR11141; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR PANTHER; PTHR11141:SF0; PROTEIN TRANSPORT PROTEIN SEC23; 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|RuleBase:RU365030};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|RuleBase:RU365030};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365030};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU365030};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|RuleBase:RU365030};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365030};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365030};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365030};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT DOMAIN 60..99
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 127..395
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 406..510
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 524..622
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 639..725
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
SQ SEQUENCE 774 AA; 86392 MW; 7569C7D87AAA4D50 CRC64;
MDHEALKEQW GEMEDRDGIR LSWNVFPSSR MEASRLVVPI GALYTPLKEK PDTPLLQFEP
VTCKPPCRAV LNPFCQVDVR ARLWICPFCL SRNALPPHYK DITQNAIPPE LHLTNTTIEY
RLSRPAPSPP VFLYVVDTCQ EEDSLSALKE SLIMSLSLLP ENALVGLITY GTMAQVHEIG
YTECAKSYVF RGSKDYSAKQ VQDMLGLSSA GLRPAMQQPQ QPGRPAPMGP ASRFLQPVQQ
CEFQLVKALE QLQKDPWPVS SDRRNLRCTG VALSVAVGLM ESSFQNAGGR IMLFAGGPAT
EGPGLVVGPE LREPIRSHHD IDRDQIKYYK KALKFYDNLA KRTAHNGHVI DIFAGCLDQV
GLLEMKGLAN STGGYMILTD SFTSSMFKQS FVRVFEKDAN DNLLMGFNAS LEVLTTKELK
VTGLIGHAVS MNKKSTSVGE TECGIGNTCS WKMCSIDPSS SYGIYFEIAS QGGPAQHQQT
PQKGMLQFLT YYQHSSGQFH LRVTTVARNL SGPAGDPAIA QSFDQETAAV LMSRIAVFKA
EVDDGPDVLR WVDRMLIRLC SRFADYRKDD PSSFRLEKNF TLYPQFMFHL RRSQFLQVFN
NSPDETAFYR HVLNQEDVSN SLIMIQPTLD SYTFDQEGSQ PVLLDSTSIQ PTHILLLDTF
FHILIFHGET IAEWRKAGYQ DQEGYENFAT LLEEPKEDAR ELITDRFPLP RFIVCDAGGS
QARFLLSKLN PSTTHTTGSY GGVGATNAQT IFTDDVSLQT FMDHLMKLAV SGTN
//
