ID   SEC24_COCIM             Reviewed;         932 AA.
AC   Q1E6U9; J3KK44;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Protein transport protein SEC24;
GN   Name=SEC24; ORFNames=CIMG_01714;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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; GG704911; EAS36360.3; -; Genomic_DNA.
DR   RefSeq; XP_001247943.2; XM_001247942.2.
DR   AlphaFoldDB; Q1E6U9; -.
DR   SMR; Q1E6U9; -.
DR   STRING; 246410.Q1E6U9; -.
DR   EnsemblFungi; EAS36360; EAS36360; CIMG_01714.
DR   GeneID; 4566953; -.
DR   KEGG; cim:CIMG_01714; -.
DR   VEuPathDB; FungiDB:CIMG_01714; -.
DR   InParanoid; Q1E6U9; -.
DR   OMA; TFPRDQS; -.
DR   OrthoDB; 330236at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
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; 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..932
FT                   /note="Protein transport protein SEC24"
FT                   /id="PRO_0000295485"
FT   REGION          1..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..280
FT                   /note="Zinc finger-like"
FT   COMPBIAS        29..43
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..105
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         255
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         277
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         280
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   932 AA;  101401 MW;  A9FDF28382136155 CRC64;
     MAAPQEGYPP PHSDGQQGYG QPYGAPPAEA DQPVAPPPAG APATGGPTHG GRKKRAYAGQ
     AFEFGSGANA ALGGQLPGGG TYGGYPAPPQ PQGYPPVPYP GQPAQPAPET YAAGEQLGAG
     GYQPPGPGYP AADVSQITQQ MGQMSMGGQM PGRAPGATSL NQLYPTDLLA QSFNVAELDF
     PPPPVILPPN ASVTPSPTAN CSAKFVRSTL NAVPTTNSLL KKSRLPFALV IQPFTSLHDS
     EDPVPIVSDQ IISRCRRCRS YINPFVTFLD HGHRWRCNMC NLTNDVPQGF DWDATAQQAL
     DRWQRPELNH AVVEFVAPQE YMVRPPQPLV YLFLIDVSYS SVTTGLLATA ARCIKESLDR
     IPNTDRRTRL GFIAVDSSLH YFTIPRDGSE SSDPSMLVVS DLDEPFLPIP GDLLVTLTEC
     RENIEIFLDK LQEMFQNTQN GGSAMGSALR AGHKLIGPVG GKLTVLTASL PNIGYGSLEM
     REDKKVLGTS KESSLLQTGN SFYKSFAVEC SKQQISVDMF LFSSQYQDVA SLSNLPRYTG
     GQTYFYPGWN AARSEDAIKF AKEFSDYLSS EIGLEAVLRV RATTGLRMST FYGNFFNRSS
     DLCAFPAFPR DQAYVVEVAI DETVTKSVVC LQTAVLHTTC NGERRIRVLT LALPTTQSLA
     DVYASADQTA IATYFSHKAV ERTLGSGLEQ ARDALQAKII ELLSTYRKEL AGGSVTGGGL
     QFPSNLRGLP LLFLALIKNL GLRKSAQIPT DMRSAALCLL STLPLPLLIQ YIYPKMYSLH
     DMPDDAGVPD PATGEIVLPP LCNLTSERLV PYGLYLIDDG QTQFLWVGRD AVPQLVQDVF
     GFPDKSQLRV GKQFLPELDN DFNERVRAVI QKSRDFRSRG VGSIIVPQLY VVKEDGEPGL
     RLWAQSMLVE DRADQGVSLQ QWMSLLREKV IQ