SEC24_DEBHA
ID SEC24_DEBHA Reviewed; 924 AA.
AC Q6BT80;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Protein transport protein SEC24;
GN Name=SEC24; OrderedLocusNames=DEHA2D02838g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382136; CAG86725.2; -; Genomic_DNA.
DR RefSeq; XP_458590.2; XM_458590.1.
DR AlphaFoldDB; Q6BT80; -.
DR SMR; Q6BT80; -.
DR STRING; 4959.XP_458590.2; -.
DR PRIDE; Q6BT80; -.
DR EnsemblFungi; CAG86725; CAG86725; DEHA2D02838g.
DR GeneID; 2901563; -.
DR KEGG; dha:DEHA2D02838g; -.
DR VEuPathDB; FungiDB:DEHA2D02838g; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q6BT80; -.
DR OMA; TFPRDQS; -.
DR OrthoDB; 330236at2759; -.
DR Proteomes; UP000000599; Chromosome D.
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 Gene3D; 3.40.20.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
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; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
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..924
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295487"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..249
FT /note="Zinc finger-like"
FT COMPBIAS 23..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 224
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 227
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 249
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 924 AA; 102437 MW; B68FE20B404CACCA CRC64;
MSSRRRAYPQ PQYAATPAVP AADPQLQQFQ PQQAQGQAQQ AQGYGAGSPA YGVDQVNQQF
QNMNVGGGVA GQPMANQYSG QYQPPPSQAN PQAPYQAPGA DSFGSQFAQH PQYAQPGMVG
GAAALPLNQL YTTDLSRELP PSITDLSLPP PPIVLPANSV VVPTSEDSNA PPEYFRSTLN
VLPANNSLLK KSKLPLALVV RPYNTLHIDS ENIPVTSDTI ISRCRRCRGY INPFVTLTEQ
GRRWRCNFCN LQNDIPSAFD YDELTGTAKN KFERVELNHS VVEFVAPKEY MARTPQPIVY
TFIIDVSIDA VNSGLTSTIT RTILESLDRI PNDNKTARVA FIGVDSNLHY FKFNEGLDGT
DLLIVSDIDE PFLPSPDGLL INLNENRSTI EKLLIDFPTY FEGTANDRFA LGPALRAGHK
MISNIGGKLI CFTATLPNIG EGKLTLRDEA SHSGKPKESQ MLLSNADKFY KSFAVECNSA
QVTVDLFLTS AKYQDVASLA NLPRFTAGQT HFYPAWSCAK AEDVTKLSRE VSEHLSMDIA
LEAVLRVRGS TGIRMSSFYG NFFNRSSDLC SFPTFPRDQS YCIEMSIEET IHKSVVYFQA
AVLHSTCFGE RRIRVMNLAI PTSTKLDDIF ASADQLAVAN YFTHRSVEKA FSSSLPDARD
YLVKSIVDIL NVYKKELVAG NVSGSSPLQL STNLRMLPLL LFSLTKHLAL RQERVPSDHR
AAALNLLSSL PIPHLIKYIY PTVYSLHNMG DECGLPEQIV QVDEETGEEE TVNSTEILLP
EPLNDTKASW ENYGLYLIDN STELFLWVSG DVVPGLVYDL FGTDNLYSVP TGKTELPEFS
FEESEFNYKV RQIIGKIREQ KDSVTWKNLY VVIGGSSNEP IEISQQRDLM ALRMWALSCL
VEDKTASEPG YREFLTSLKS KITQ
