SEC23_ASPOR
ID SEC23_ASPOR Reviewed; 769 AA.
AC Q2URM9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Protein transport protein sec23;
GN Name=sec23; ORFNames=AO090005000760;
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.
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. SEC23 subfamily.
CC {ECO:0000305}.
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DR EMBL; AP007151; BAE55786.1; -; Genomic_DNA.
DR RefSeq; XP_001817788.1; XM_001817736.2.
DR AlphaFoldDB; Q2URM9; -.
DR SMR; Q2URM9; -.
DR STRING; 510516.Q2URM9; -.
DR EnsemblFungi; BAE55786; BAE55786; AO090005000760.
DR GeneID; 5989733; -.
DR KEGG; aor:AO090005000760; -.
DR VEuPathDB; FungiDB:AO090005000760; -.
DR HOGENOM; CLU_008658_3_0_1; -.
DR OMA; FPPHYAE; -.
DR Proteomes; UP000006564; Chromosome 1.
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:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd11287; Sec23_C; 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; IPR037364; Sec23.
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; IPR037550; Sec23_C.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR11141; PTHR11141; 1.
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..769
FT /note="Protein transport protein sec23"
FT /id="PRO_0000295453"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 769 AA; 85572 MW; 2AA76F87A4697EBD CRC64;
MDYEALKDQW SDVEDRDGIR LSWNTFPSSR MEASRLVVPI GAVYTPLKDK PDSPLLQYEP
VTCKAPCRAV LNPYANVDVR ARIWICPFCL MRNPLPPHYK DITESTIPPE LHPLSTTIEY
QLARPAPTPP IFVYVVDTCQ EEDSLKALKD TLVMSLSLLP ANALVGLITY GTMAQVHELG
YTECAKSYVF RGSKEYAAKQ VQEMLGLLSA GVRPNMPQQP ARPPLGPAAR FLLPVQQAEF
QITNVLEQLQ RDPWPVANDK RPLRCTGVAL SVAVGLLETS FQNAGGRIMV FTSGPATEGP
GHVVGPELKE PMRSHHDIDR DNIKYYKKAV KFYDAMAKRA ANNGHIVDVF AGCLDQVGLL
EMKNLVNYTG GHMLLTDSFT SSQFKQSFVR IFDKDANDNL LMGFNASLEV LTTKELKVTG
LIGHAVSLNK KSSSVGETEC GIGNTCAWKM CGIDPSSSYG VYFEIANQGG PAAVQPGPQR
GMMQFLTYYQ HSSGHYHLRV TTVARNLSGP AGDPTLAQSF DQEAAAVLMA RIAVFKAEVD
DGPDVLRWVD RMLIRLCSRF ADYRKDDPTS FRLEKNFTLY PQFMFHLRRS QFLQFFNNSP
DETAFYRHVL NHEDVGDSLV MIQPTLDSYS LEHEGSQPVL LDSASIQPSH ILLLDTFFHI
LIFHGETIAE WRKAGYQDQE GYENLKALLE QPKEDARELI SDRFPLPRFI VCDAGGSQAR
FLLSKLNPST THTTGGYGGG VTSQTIFTDD VSLQTFMDHL MKLAVSGTS
