SC242_CANGA
ID SC242_CANGA Reviewed; 906 AA.
AC Q6FWD3;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Protein transport protein SEC24-2;
GN Name=SEC242; OrderedLocusNames=CAGL0D01078g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; CR380950; CAG58372.1; -; Genomic_DNA.
DR RefSeq; XP_445461.1; XM_445461.1.
DR AlphaFoldDB; Q6FWD3; -.
DR SMR; Q6FWD3; -.
DR STRING; 5478.XP_445461.1; -.
DR EnsemblFungi; CAG58372; CAG58372; CAGL0D01078g.
DR GeneID; 2886987; -.
DR KEGG; cgr:CAGL0D01078g; -.
DR CGD; CAL0128245; CAGL0D01078g.
DR VEuPathDB; FungiDB:CAGL0D01078g; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q6FWD3; -.
DR OMA; TFPRDQS; -.
DR Proteomes; UP000002428; Chromosome D.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:EnsemblFungi.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005048; F:signal sequence binding; IEA:EnsemblFungi.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IEA:EnsemblFungi.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0016236; P:macroautophagy; IEA:EnsemblFungi.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IEA:EnsemblFungi.
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..906
FT /note="Protein transport protein SEC24-2"
FT /id="PRO_0000295483"
FT REGION 222..247
FT /note="Zinc finger-like"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 906 AA; 101317 MW; 9F7F30DAD60C1909 CRC64;
MSHHKKRVYP QAQFQYGAGV PPAGIPVSDA SIIPPQVQSP QVGATDNMIP PYNQTPTMNQ
MEQAPQAQMF TPAQQQLNQQ INSVTTNMGA MNIGTPMMEQ MPQQMTPQPQ MYGQSQGLMG
HSNKPMNQLY PVDLLTELPP PIHDLMLPPP PLMVSPDKML VPSETANASS DYLRCTLNAM
PKNGSLLKKS KLPLALVIRP YQHLHDEVNP PPLNEDGLVV RCRRCRSYMN PFVTFIEQGR
RWRCNFCRLA NDVPMQLDQS FEGAPANRYE RNEIKHSVME YLAPKEYTVR QPPPSTYIFV
LDVSQNAVKN GLLATTARSI LDTLEFLPNH DNRTRVSILA VDNSLHYFSI PLDEESDQIR
MMDISDIDEP FLPKPHSMIV PLNECRNNLE KLLTQLPEIF QFNIMSKFAL GPALKAAQNM
ISNLGGKIVV VSATLPNIGI GKLQRRNESG VANTPKESTQ LLSCQDAFYK NFTITCSKSQ
VSVDLFLASE DYMDVASLSN LGRFTGGQTH FYPGFTAANI ADVTKFTKEF SKFLSMDLST
ETVMRARGST GIRMSAFYGH FFNRSSDLCA FSTMPRDQSY VFEMSIDENI GTEYCYVQIA
VLLSLNTSQR RIRIITVAIP TTESLSEVYA SADQLAIADF FTKKAVEKAM NSSLQDARDL
LNKSLQDILA TYKKEIVVSN TAGGAPLRFC ANLRMLPLLV HALSKHTAFR AGIVPSDHRA
AALNNLESMP LKYLVKSAYA RVYSLHDMVD EAGYPDENGE IVLPEPINAS ASLFERYGLY
LIDNSSELFL WVGGDAVPEL VNDVFGLQDI FQIPNGKHEL AIVEGSEFNE RVRNIIQKVR
EHDDVITYQT LYIVRGPSVS EPVGHAAGRE LQPLRMWATS NLVEDKVLGT ESYREFLQTL
KNKLNK
