SC241_NAUCC
ID SC241_NAUCC Reviewed; 911 AA.
AC Q875V8; G0VIG4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Protein transport protein SEC24-1;
GN Name=SEC241; OrderedLocusNames=NCAS_0G03120;
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
RX PubMed=12594514; DOI=10.1038/nature01419;
RA Langkjaer R.B., Cliften P.F., Johnston M., Piskur J.;
RT "Yeast genome duplication was followed by asynchronous differentiation of
RT duplicated genes.";
RL Nature 421:848-852(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (JUL-2011) 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: The COPII coat is composed of at least 5 proteins: the
CC SEC23/24 complex, the SEC13/31 complex, and the protein SAR1. Golgi
CC apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle,
CC COPII-coated vesicle membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endoplasmic
CC reticulum membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY144961; AAO32524.1; -; Genomic_DNA.
DR EMBL; HE576758; CCC71199.1; -; Genomic_DNA.
DR RefSeq; XP_003677551.1; XM_003677503.1.
DR AlphaFoldDB; Q875V8; -.
DR SMR; Q875V8; -.
DR STRING; 1064592.Q875V8; -.
DR PRIDE; Q875V8; -.
DR EnsemblFungi; CCC71199; CCC71199; NCAS_0G03120.
DR GeneID; 11528713; -.
DR KEGG; ncs:NCAS_0G03120; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q875V8; -.
DR OMA; TFPRDQS; -.
DR OrthoDB; 330236at2759; -.
DR Proteomes; UP000001640; Chromosome 7.
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; 3.40.20.10; -; 1.
DR Gene3D; 3.40.50.410; -; 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 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; SSF53300; SSF53300; 1.
DR SUPFAM; SSF81811; SSF81811; 1.
DR SUPFAM; SSF82754; SSF82754; 1.
DR SUPFAM; SSF82919; SSF82919; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Golgi apparatus; Membrane; Metal-binding; Protein transport;
KW Reference proteome; Transport; Zinc.
FT CHAIN 1..911
FT /note="Protein transport protein SEC24-1"
FT /id="PRO_0000295500"
FT REGION 108..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..251
FT /note="Zinc finger-like"
FT COMPBIAS 108..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 226
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 911 AA; 102400 MW; B993B091CB0985EB CRC64;
MSHKKRVYPT AQLQYGQTNI YEQHGVPQDA GAPQGQPLQS DIPYMNAQPG VIPGQGAPMM
MDNGAMPQQQ MFTPAQQQLN QQIDQTTAAM GNMQFNPAAN ESNMYYQQPL PQQQQQQQQQ
QGPAKPPKPM NQLYPIDLLV AFPPPISDLS LPPPPILFPL DTIPVPSEDA LAPSNYIRST
LNAVPKSNSL LKKTKLPFSL VITPYQHLHD DINPPPLNED GTIVRCRRCR SYMNPFVHFN
QDGRRWKCNI CNLFNEVPSF LDRMPNDTMS NRYMRNELRY SVVEYLAPKE YSLRQPPPST
YTFIIDVSQN AMKNGLLGTT TRTLLDNLDS LPNHDGRTRI SILCVDNGLH YFAIPSDDQE
GQQVEMMDVC DLDDAFIPRP DSMVVNLVQC RNNIETLLTK IPQIFQNNII NKFALGPALQ
AAYNLTRNEG GKIIVVSATL PNIGVGQLKK RVEEANVGTP KESQQLLTCQ DPFYKTFTIQ
CNKVQISIDM FLASEEYMDV ATLANLGHFS GGQTHFYPGF SAQRITDATK FSMEFAKHLS
MDTSNEVVMR ARGSTGIRTT GFHGHFFNRS SDLCAFSIMN RDQSYVFDIT LDENIAAEYC
YVQVAILLSL NTSQRRIRVI TLALPTTDSI AEVYASVDQL AVTAAFTQKA IDKAQDTSLE
EARRFINQSV EDVLTTYKKE LVVQNTGAGG MPLRLCANMK IFPLLMHALT KNLAFRPGRV
PSDHRAAALN YMESVPLKYL LKCIYPTIYS LHDMPDEVGL PDENNEIILP EPINASYSSF
ETYGLYLIDN GIDLFLWMGG EALPQLVEDA FGVPNILEMP IGKQEVPVVP ESPFNERIRN
IINRLRNHDD VITYQSLYIL RSASNSDPVQ ANAKELSSLR MWASTHLVED KIMGSEGYRD
FLQMMKNKTS K
