SC241_CANGA
ID SC241_CANGA Reviewed; 897 AA.
AC Q6FX11;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Protein transport protein SEC24-1;
GN Name=SEC241; OrderedLocusNames=CAGL0C01353g;
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; CR380949; CAG58139.1; -; Genomic_DNA.
DR RefSeq; XP_445233.1; XM_445233.1.
DR AlphaFoldDB; Q6FX11; -.
DR SMR; Q6FX11; -.
DR STRING; 5478.XP_445233.1; -.
DR EnsemblFungi; CAG58139; CAG58139; CAGL0C01353g.
DR GeneID; 2886812; -.
DR KEGG; cgr:CAGL0C01353g; -.
DR CGD; CAL0127234; CAGL0C01353g.
DR VEuPathDB; FungiDB:CAGL0C01353g; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q6FX11; -.
DR OMA; MSAYNPN; -.
DR Proteomes; UP000002428; Chromosome C.
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: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 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..897
FT /note="Protein transport protein SEC24-1"
FT /id="PRO_0000295482"
FT REGION 213..238
FT /note="Zinc finger-like"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 897 AA; 100099 MW; 17285F3617634720 CRC64;
MSHHKRRVYP QAQFGLAQAG QTGYQDVQQP GVLPSQANYQ EPVPLVTPIQ EVLNNQIDQT
ADSLHNMQLH NVPDFNQPLQ GQLNGPQSPA LYQNYNENGM NNYNAAFGNG GTSVKQVNQL
YPIDLLSDLP PPIKDLGLPP PPINLSPDIM SVPSDKSNAS PDYIRSTLNA VPKTNSLLKK
TKLPFALVIK PYQHLNDDVN APPLNEECLI VRCRRCRSYI NPFAKFIEQG RRWRCNFCRL
ANDLPMQFDQ SSIDTNIVNR LDRTEIKNAV MEYVAPKEYT VRPPPPSIYT FIIDVSQNAI
KNGLFVSTIE TLKQQLEYLP NRDNRTKISI ILVDHALHIL SIPADDVSNK FRILDVADID
EPYIPLPNSL VVSLSRCKQN VQLALEKIKQ LFEINVSTKF ALGPALRTAQ KLIGGVGGKL
IVISASLPNA GIGSLQRRNE SGVSGTTKES SQLLSCQDSF YKTFTVECSK TQITIDLFLA
SDDYVDVATL SNLPRYTAGQ THFYPGYNAS NISDFNKFTT EFSKHITMDI SFETVMRARG
STGLKTSAFY GHFFNRSSDL CAFSTMPRDQ SYVFDISIED TITTDYCYFQ VAVLLSLNNG
QRRIRVITLA LPTTQSISEV FACVDQQAVA AQITQRAVQK ANSSSIDDAR DLIQKTTLDI
LSTYKKELVV TNTGGVVPLK LSTNLRILPL LMHALMKHMA FRAGVVPSDH RAYSLNVLES
VPIKSLITSI YPSIYSMHDM GDDCGYTDET GNVILPECIN DTAILMEKYG LYLIDNGSEL
FLWVGGEAVP ELLSDVFGVP EMSQVPVGKH DLFRVEGSQF NERVCNIIDQ LRTSDDTTVY
KTLYIVSGPT INDSFSQGTR ELASLRMWAA TAFVEDNIMK TLSYREFLEK MKKEVSK
