SEC24_CANAL
ID SEC24_CANAL Reviewed; 928 AA.
AC Q5AQ76; A0A1D8PEG4; Q5APN4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Protein transport protein SEC24;
GN Name=SEC24; OrderedLocusNames=CAALFM_C108740CA;
GN ORFNames=CaO19.12194, CaO19.4732;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017623; AOW26511.1; -; Genomic_DNA.
DR RefSeq; XP_723419.2; XM_718326.2.
DR AlphaFoldDB; Q5AQ76; -.
DR SMR; Q5AQ76; -.
DR BioGRID; 1218033; 1.
DR STRING; 237561.Q5AQ76; -.
DR PRIDE; Q5AQ76; -.
DR GeneID; 3634939; -.
DR KEGG; cal:CAALFM_C108740CA; -.
DR CGD; CAL0000196446; SEC24.
DR VEuPathDB; FungiDB:C1_08740C_A; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q5AQ76; -.
DR OrthoDB; 330236at2759; -.
DR PRO; PR:Q5AQ76; -.
DR Proteomes; UP000000559; Chromosome 1.
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 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; 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..928
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295481"
FT REGION 1..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..256
FT /note="Zinc finger-like"
FT COMPBIAS 24..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 253
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 928 AA; 102062 MW; 01CA22FA55AC16B9 CRC64;
MSGRRRAYPQ PQYATGPAEM ATPPAPNQFQ QQQPVQQPVQ QYGVDQMQGQ FQQMNVGGVG
PTGVPPAPQY SYQQPGQPQQ SPQLSYDPYQ PQPQANTGVY GQGMGGVPPS AVPAGGAGYG
GYGQQNNIGL GAQLNALYTT DLSRDLPPPI AELSFQPPPI TLPDNATLIP ASKTANATPE
YFRSTLNVVP TNSSLLKKSK LPLAIVVNPY NALKIENENV PVTCDTVISR CRRCRGYINP
FVTLAENGRR WRCNFCNLLN DIPSAFDYDE ISGQVKNKFD RVELNHSVVE FIAPKEYMAR
APQPIVYTFI IDVSVHAIQS GLTGTITRTI LESLDRIPNE NKTARVSFIG VDSNLHYIRF
NEGLEGTEIL VVADIDEPFL PSPGGLLVNL DENREAIEKL LLDFPSYFEN NANQGFALGP
ALKAGHKMIS NIGGKLVCFA ATLPNIGEGK LSVRDEASVA GKAKEAKALL APADSFYKSF
AVTCNSSQVT VDLFLTSSAY QDVATLSNLA RYTAGQTHFY PAWTSNKYED VAKLSKEVSD
HLSQDIALEA VLRVRGSTGF RMSSFYGNFF NRSSDLCSFP TFPRDQSYLI EMSIEETINK
PVVYFQAAVL HSTCFGERRI RVMNLALPTS SKLVDIYASA DQLAIANYFT HKAIEKALSS
SLPEAREYLI ARVVDILNVY RKELVAGNVS GASPLQISTN LRMLPLLLFC LTKHLAFRGE
RVPSDHRAAA LNNLGSSPIP QLIKSIYPTV YSLHNMPDTC GLPGVKEDED DEEGAGAEID
VVLPDPINDS KASWENYGLY LIDNGSELFL WVSGNVVPGL VQDLFGTENL YEIPTGKTEL
PEFSLEESEF NYRVRQIIGK IREQNDSIIW KNLYVVVGAS SNEPIEISQQ RDLMALRMWA
SSCLVEDKTG SEPSYRDFLT SLKSKVSQ
