SEC24_YARLI
ID SEC24_YARLI Reviewed; 934 AA.
AC Q6C2T4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Protein transport protein SEC24;
GN Name=SEC24; OrderedLocusNames=YALI0F05324g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382132; CAG77835.1; -; Genomic_DNA.
DR RefSeq; XP_505028.1; XM_505028.1.
DR AlphaFoldDB; Q6C2T4; -.
DR SMR; Q6C2T4; -.
DR STRING; 4952.CAG77835; -.
DR EnsemblFungi; CAG77835; CAG77835; YALI0_F05324g.
DR GeneID; 2908193; -.
DR KEGG; yli:YALI0F05324g; -.
DR VEuPathDB; FungiDB:YALI0_F05324g; -.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q6C2T4; -.
DR OMA; TFPRDQS; -.
DR Proteomes; UP000001300; Chromosome F.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
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..934
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295504"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..272
FT /note="Zinc finger-like"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 250
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 934 AA; 101900 MW; 56BAA7B0934A217D CRC64;
MSQEHPEQGS SSKRRVYPQQ QYDFAAAQPA GYSMPDPTQP YGASASPSAA MYGGAHAIPS
PAAFQPHTAN VQSGAFAPPP GTPGSAVDPP VAPGVAGGMA YGAPQAAGAA YGYQGLTNQM
GNLNIGGGGA YQGGAPPGAA GGAHMAAPTQ LNQIYNTDLL QNFPPPISDL TLPPPPVILP
PGSSVTGNPD PNADSEFMRC TLNTVPTSSS LLKKSKLPFA LVIRPYTALR DADENVPTVA
DTTIARCRRC RSYINPYVVF LEGGARWRCN MCNLTNDVPS GFDYDAVANK PRDRWSRAEL
NHSVVEFVAP AEYMVRPPQP LVYVFVLDVS VHSVKNGLLA TAARTIKESL SRIPNVDNRT
RVGFLAVDSS LHYFAIPRKE DVAEGEGEEG EENEWPEPRM MVVSDIDDPF LPMPTDLLVN
LSQCKGGIEK LLDSLQSMFA HTVNPASALG SAVVAAHKLI ANIGGKIVCL TSTLPNVGQG
KLEVRDDKKA LGTSREGQML QTASTFYKSF AVECSKTQVT VDMFLFSSHY QDVASLSNLP
RFSAGQTYFY PGWIASNPED ANKFALEFSE YLSQELATEA VLRVRSCDGI RMSAFYGNFF
SRSSDLCSFS TFPRDQSYVI EVNIEETIVK PWVTFQAAIL HSTASGERRI RVITRAFPTS
ALLQDIYASA DQIAITTYLA NKAVEKALQK GPQDARDLLM NRLNEMFTCY KKDLMTTNVG
ASAPLQFCTN LRMLPLLVNA LIKHIGFRKT SQIPSDLRSA ALCLLSTLPD KYLIQYIYPN
FYNLIFMPDE AGLPDAETGQ IVMPPCTNLS GEHLISHGLF LIDDGQVMFL WVGRDAQPAL
LQDVFGVSSI TEVPTGKTEL PVLDNQFNER IRNIISKARE KTDAITYQHL YVVREDGEPA
LRLWATTHLV EDRVEQSGVT YHQFLTSIRE KLNS
