SEC24_ASHGO
ID SEC24_ASHGO Reviewed; 891 AA.
AC Q75B16;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Protein transport protein SEC24;
GN Name=SEC24; OrderedLocusNames=ADL239C;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(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; AE016817; AAS51681.1; -; Genomic_DNA.
DR RefSeq; NP_983857.1; NM_209210.1.
DR AlphaFoldDB; Q75B16; -.
DR SMR; Q75B16; -.
DR STRING; 33169.AAS51681; -.
DR EnsemblFungi; AAS51681; AAS51681; AGOS_ADL239C.
DR GeneID; 4619992; -.
DR KEGG; ago:AGOS_ADL239C; -.
DR eggNOG; KOG1985; Eukaryota.
DR HOGENOM; CLU_004589_2_1_1; -.
DR InParanoid; Q75B16; -.
DR OMA; TFPRDQS; -.
DR Proteomes; UP000000591; Chromosome IV.
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:0005048; F:signal sequence binding; IEA:EnsemblFungi.
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 GO; GO:0016236; P:macroautophagy; IEA:EnsemblFungi.
DR GO; GO:1902953; P:positive regulation of ER to Golgi vesicle-mediated transport; IEA:EnsemblFungi.
DR GO; GO:0070863; P:positive regulation of protein exit from endoplasmic reticulum; IEA:EnsemblFungi.
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..891
FT /note="Protein transport protein SEC24"
FT /id="PRO_0000295475"
FT REGION 207..232
FT /note="Zinc finger-like"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 210
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 891 AA; 99622 MW; 6633CB9E2E0B707B CRC64;
MSGHKKRVYP EAQYQYGAQP AAPSQGFPPG PAMSPPMQAQ QFLTPAQQQL HQQIDQATSS
MGNMNLHNVP VVDPSTFYQA GVASPPVAPH AVAGTQYNEQ PYGHMSIGKP MNQLYPIDLF
QELPPPITDL SLPPPPLLVP AERIVVPSEE ANASPDYLRC TLNAIPKTNG LLKKSKLPLA
MVIRPYLHLE DSIDPPPLNM DGCIVRCRRC RSYINPFVTF LEGGRRWRCN FCNLANDVPQ
AFDMDMQGVP INRYDRNEIQ RAVVEYLAPK EYAVRQPPPS CYAFVFDVSQ NAIKNGLLAT
AARTLLESLD SLPNYDERTR ITILAVDHTI HYFSVPLDEE GDHIRMMDVV DLDEPFLPMP
DTMFVSLKDC RNNLEKLLSQ IPDIFQSNIL PKFALGPALK AAHNLIKGIG GKIIVVSATL
PNIGIGKLNK RNEASVANTS KEASQLLSCG DSFYKNFTID CNKTQVTIDM FLASDDYVDF
ASVSNLGRYT GGQTHFYPGF TALNMIDVTK FSKEFSKHIT MDLSMEAVMR ARGSTGLRMS
RFYGHFFNRS SDLCAFPTFP RDQSYVFEIS IDEQIVRDYV YLQIAVLLSQ NTGQRRIRVI
TVCIPTTDSL AEVYASADQL AMTVYHSQKA IEKVMSSGFE DAREYLDRSV QEVLATYKKE
IAMSNTAGGA PLRLCANLRM WPLLMHSLTK HMAFRSGIIP ADHRAAALNA LESLPLPYFI
KNIYPSVYSL HDMPDEAGLP NENGEIVLPQ PINATSSLFE RYGLYLLDTG MDMFLWLGGD
AVPELVMDVF GTQDIMQIQV GKGELPILEN SEFNERVRNV IVKLREHDDI ITYPTLHIVR
GASPSEPMNH ASAREVASLR LWATSQLVED KVQSSFTYRE FLQSMKTKTS K
