SC242_NAUCC
ID SC242_NAUCC Reviewed; 912 AA.
AC Q875V7; G0V9V5;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein transport protein SEC24-2;
GN Name=SEC242; OrderedLocusNames=NCAS_0B06380;
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; AY144962; AAO32525.1; -; Genomic_DNA.
DR EMBL; HE576753; CCC68722.1; -; Genomic_DNA.
DR RefSeq; XP_003675093.1; XM_003675045.1.
DR AlphaFoldDB; Q875V7; -.
DR SMR; Q875V7; -.
DR STRING; 1064592.Q875V7; -.
DR PRIDE; Q875V7; -.
DR EnsemblFungi; CCC68722; CCC68722; NCAS_0B06380.
DR GeneID; 11526168; -.
DR KEGG; ncs:NCAS_0B06380; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q875V7; -.
DR OMA; MSAYNPN; -.
DR OrthoDB; 330236at2759; -.
DR Proteomes; UP000001640; Chromosome 2.
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..912
FT /note="Protein transport protein SEC24-2"
FT /id="PRO_0000295501"
FT REGION 1..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..251
FT /note="Zinc finger-like"
FT COMPBIAS 17..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..129
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 912 AA; 102066 MW; FE9D4A18A69C1A1B CRC64;
MSNPSRPKKR VYPTAQYVAP SSPSMPFQGG AFSGQTMQSQ VSGSASPYMA PSGQFTQPMN
ASDAQNQPQF MTPAQQQLKQ QISQATTSMN DMHLHNVPVI DPNAYYQPNN GNNIQPTGEN
KPSLTPGRPT NNLYPVDILT ELPPKINDLN LLPPPILLEP EISTKFSESV YASPDYIRST
LNAVPQSNAL LKKSKLPFAL IIKPFKHLHD MNAPLPCNED EFVIRCRRCR GYLNPFVKIL
QVESKWRCNF CGCINGFPDG SEHFQLPNLY NRNELTYSSM DFLPSSSYSQ QVKEEPPAVY
TFVIDVSINT IKNGYLFSVA NALVNSLDLI PNHDNKTLIS LICADSSLHY FSVPLDTEDG
PKESSMFDIS DLDEPFLPTS NSLLVSLSQC RNNLEHLLLK IPEIFKSTTI QSFALGPALQ
NASELVKDKG GKVIVCSSTL PNMGIGKLNP RDERGISNTS KESKDLLSCQ DAFYRSFTVE
CNKLQITIDL FIASGNYMDI ATLSNLSKYT GGQTHFYPQF LGSVAADFTK FSKEFSRHLS
MDLSFRTVMR PRCSIGLRIE DSYGHLFNRS TDLCSFPAMP RDQSYVVELS IEDKLTADYC
YAQIAFLYST GTGKRKIRVL TLALPTTTIL HNVFASADQL AIATYFARIA TEKVMKNSFD
HARSFLNTSL EEILINYRKE IVVENNAGGV TLRFSTNLKM LPLLVHMLLK NIAFRKGVIP
SDLRAIALNN MESLPLKYLI KNAYPTVYSL HDIPDEAGLP DENGVIVMPP PMNDTISSFE
KYGLYLINTP NELILWVGGN AIPELVSDVF GLQDVFQVPN GKNELPELPE SEFNQRLRSI
IENIRANDDE QITYQTLYIV RGNSQNEPAN SSQNKEIVPL RNWAVSFLVE DNVVGCESYR
EFLQNLKTRL NK
