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Entry: A0A094C9K1_9PEZI
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ID   A0A094C9K1_9PEZI        Unreviewed;       944 AA.
AC   A0A094C9K1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=Protein transport protein SEC24 {ECO:0000256|ARBA:ARBA00021213};
DE   AltName: Full=Protein transport protein sec24 {ECO:0000256|ARBA:ARBA00013453};
GN   ORFNames=V494_01616 {ECO:0000313|EMBL:KFY44130.1};
OS   Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY44130.1, ECO:0000313|Proteomes:UP000029288};
RN   [1] {ECO:0000313|EMBL:KFY44130.1, ECO:0000313|Proteomes:UP000029288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
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:KFY44130.1}.
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DR   EMBL; JPJW01000541; KFY44130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094C9K1; -.
DR   STRING; 1420907.A0A094C9K1; -.
DR   HOGENOM; CLU_004589_2_1_1; -.
DR   OrthoDB; 977017at2759; -.
DR   Proteomes; UP000029288; 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:UP000029288};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          264..300
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          338..579
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          585..668
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          679..781
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          808..880
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          1..82
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"
SQ   SEQUENCE   944 AA;  103060 MW;  24D5C03EA3E1FA5C CRC64;
     MSAPQEGYPP QGYPQQEQYG EQQPQPGFGA AAPPPAEEHH DTHGGKKKKR GYAAQAYDFG
     AGGNAALGGQ PPNPENFAPV GAPAYGGYPA PAEQPAYGAN QPYTDAPQPA AAYGQSALGG
     LGGYQAPQQA GYPAPGAPPG GDVGGITQGM GQMGIAPQAA APGAGGAPKV ALNQLYPTDL
     LNQPFNVAEL ELPPPPIILP PNSSVTPSPD ANSSHKYVRS TLNAVPTTNN LLKKSKLPFA
     LVIQPYSSLH DADDTVPVIQ DQIISRCRRC RTYINPYVTF LDHGHRWRCN MCNLTNDVPQ
     GFDWDAATQQ SVDRWQRAEL NHAVVEFVAP QEYMVRPPQP LVYLFLFDVS YNAVNNGLLA
     TSARTILDSL NRIPNADRRT RLGFMAVDSS LHYFTVPKDG EENGETNMLV VSDLDEPFLP
     IPQELLVPLS ESRANIETFL TKLPGMFQNN VITTSCMGSA LRAGHKLISP LGGKLVVLTA
     TLPNVGYGKL DLREDPKALG TSKENALLQT QNSFYKSFAV ECSKNQVSID MFLFSSQYQD
     VASLSNLPRY TGGQTYFYPG WSAVRSEDAI KFASEFSDYL SSEIGLEAVL RVRATTGLRM
     NTFYGNFFNR SSDLCAFPAF PRDQAYVVEV AIDETLTKNF ICMQAAVLHT TSNGERRIRV
     LTLSLPTTTI LADLYASADQ CAITTYFSHK AVERALSNGL ESARESLQSK LIELLQTFKK
     ELAGGNMGGG GLQFPANLRG LPTLFLGLIK NLGLRKSAQI PSDLRSAALC LLSTLPLPLM
     MQYIYPRLYS LHDMPDNVGI PDPETNEIVL PSPLNLSSER LVPYGLYLIT DGQTQFLWVG
     RDAVPQLLED VFGVPDRTQV KVGKSSLPEL DNDFNERIRA VLLKCKDYRS RGVGSIIQPH
     LYIVKEDGDP SLKLWAQTML IEDRADQGVS FQQWMGTLRE KVMQ
//
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