ID   SEC24_PICPA             Reviewed;         960 AA.
AC   Q0PVD8;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Protein transport protein SEC24;
GN   Name=SEC24;
OS   Komagataella pastoris (Yeast) (Pichia pastoris).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Komagataella.
OX   NCBI_TaxID=4922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16962585; DOI=10.1016/j.febslet.2006.08.058;
RA   Esaki M., Liu Y., Glick B.S.;
RT   "The budding yeast Pichia pastoris has a novel Sec23p homolog.";
RL   FEBS Lett. 580:5215-5221(2006).
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; DQ683203; ABG81279.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0PVD8; -.
DR   SMR; Q0PVD8; -.
DR   IntAct; Q0PVD8; 2.
DR   MINT; Q0PVD8; -.
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; 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; 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; Transport;
KW   Zinc.
FT   CHAIN           1..960
FT                   /note="Protein transport protein SEC24"
FT                   /id="PRO_0000295495"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..279
FT                   /note="Zinc finger-like"
FT   COMPBIAS        75..104
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         254
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         257
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         276
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         279
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   960 AA;  106081 MW;  0B47A40FC5498D13 CRC64;
     MSGKRRAYPS MQYPATEPVA TGGSFGYGQQ PGAQAYGQQF TPGAGIAGQQ LPGATQPNLN
     GQGAPYGAPG GDQLAQGMSS LNIQPNQQPQ PVHQFPSQQQ GYINPGAGLG VPPTQAAGPY
     GVPAAVAPQQ QSAQLGYAGP PYGNTYDQQQ PQQAAFPFNQ LYTADLLKEL PPPISDLELP
     PPPIVLPQGA SLTGKPESNA SPEYFRCTLN VIPNNNSLLK KSKLPLAVVV NPYQCLRDED
     EPVPVVEDTL ISRCRRCRSY INPLITFVDR NTKWRCNLCN LTNDVPSGFD FDKDTQQRVD
     RMARVELNYS VVEFVAPKEY MVRLPQPLVY LFVLDVSTHA IQNGYLATVA RTILDSLDQI
     PNKDGRARVG FIGVDSSLHF FTIPQDSEDE NDAQETSMLV VSDLDDVIVP AAENLLAPLQ
     QSRQNIENLL NNFHSYFENN VNPNFALGPA LKAGHRLINN IGGKMIVFTS TLPNKGIGAL
     SIRDEEAHSG KAKESSALLS PNDSFYKSFA VECNKSQVTV DMFLASSSYQ DVATLSNLPR
     YTAGQTHFYP AWTAAREEDI TKLSKEISNH LSMNINLEAV LRVRGSAGLR MNAFYGNFFN
     RSSDLCSFPT FPRDQSYLIE ISIDEHITKP LAAFQAAVLH TTSFGERRIR VMTLEVPIGK
     ELNQIYASAD QLAITNYFTH KAVEKALSSS LIDAREYLNR SLLDIFQVFK KELVAGNLGS
     SSPLQLCNNL KMLPLLLHSL TKYIAFRPGK VPSDHRAYAL NLLASSPIQR LIKFIYPTIY
     SLHDMADECG LPEELEETYV NEAGEEVTEP IDGDIVLPEP INDTSTLLAP YGLYLIDSGT
     DLFLYVGGES VPQLLLDVFG VDNPGYIKYG KSELPELNNE FNERLRNVIN RVREGKDRIT
     YQNLQIVIGQ SKQRTGVPDR IQEDLTPLRL WCFSHLVEDR VGGGTAYREY LNQIREKLSS