SEC24_ASPOR
ID SEC24_ASPOR Reviewed; 913 AA.
AC Q2ULI0;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Protein transport protein sec24;
GN Name=sec24; ORFNames=AO090003000403;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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; AP007155; BAE57585.1; -; Genomic_DNA.
DR RefSeq; XP_001819587.1; XM_001819535.2.
DR AlphaFoldDB; Q2ULI0; -.
DR SMR; Q2ULI0; -.
DR STRING; 510516.Q2ULI0; -.
DR EnsemblFungi; BAE57585; BAE57585; AO090003000403.
DR GeneID; 5991570; -.
DR KEGG; aor:AO090003000403; -.
DR VEuPathDB; FungiDB:AO090003000403; -.
DR HOGENOM; CLU_004589_2_1_1; -.
DR OMA; TFPRDQS; -.
DR Proteomes; UP000006564; Chromosome 2.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:EnsemblFungi.
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..913
FT /note="Protein transport protein sec24"
FT /id="PRO_0000295479"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..263
FT /note="Zinc finger-like"
FT BINDING 238
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 260
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 263
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 913 AA; 99544 MW; 5582D120FE9F1432 CRC64;
MAAPQGGYPP QEGYGQPAGY ESPSQQAAGL APAPAQHGGR KKRAYAGEAF ELGSGANAGL
GGQLPAGGTY GGYPAQPQAA GYQQPVYGAD PTQMQAAAQG YAAPAAPAVA QMTQQFGAMG
VTDPHLMPPQ PVPQAAQAPR PVLNHLYPTD LLTQPFNVAE LDYPPPPIVL PQGTSVYPSP
TANCPPKYVR STLNAVPTTH SLLKKSKLPF ALVIQPYGAL HDSEDQVPVI PDQVISRCRR
CRSYINPFVT FLDHGHRWRC NMCNLTNDVP QAFDWDTTLQ RPADRALRPD LNHAVVEFVA
PQEYMVRPPQ PLVYLFLIDV SYASVTNGLL ATSARCIKES LERIPNADRR TRLGFIAVDS
SLHYFSIPRD GSENSDPRML VVSDLDEPFL PIPGDLLVTL SECRENIETF LDKLQEMFQN
TQNNGCAMGS ALRAGYKLIA PVGGKMTVLS SSLPNIGHGA LTMREDKKVL GTSKESGLLQ
TANSFYKSFA VECSKAQVSV DMFLFSSQYQ DVASLSNLPR YTGGQTYFYP GWNAARGEDA
IKFAREFSEY LSSEIGLEAV LRVRATTGLR MSTFYGNFFN RSSDLCAFPA FPRDQAYVVE
VAIDETVTKP VVCMQTAVLH TTCNGERRIR VLTLALPTTQ SLADVYASAD QQAIATYFSH
KAVERALGSG LEPAREALQA KAVELLATYR KELAGGSVSG GGLQFPANLR GLPVLFLALI
KNLGLRKSAQ IPTDMRSAAL CLLSTLPLPL LIQYIYPKMY SLHDMPDNAG LPDEQTGEIV
LPPPVNLSSE RVVPYGLYLI DDGQTQFLWV GRDAVPQLIV DVFGLPDKSQ LRVGKQNLPD
LDNDMNQRVR AVIEKSRDHR SKGCGSIVVP HLYVVKEDGE PGLRLWAQTM LVEDRADQGV
SLVQWMGNLQ EKV
