SC23A_DANRE
ID SC23A_DANRE Reviewed; 765 AA.
AC Q7SZE5; Q4V948;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Protein transport protein Sec23A {ECO:0000305};
DE AltName: Full=SEC23-related protein A;
GN Name=sec23a {ECO:0000250|UniProtKB:Q15436};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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 for their transport to the Golgi complex.
CC {ECO:0000250|UniProtKB:Q15436}.
CC -!- SUBUNIT: COPII is composed of at least five proteins: the Sec23/24
CC complex, the Sec13/31 complex and Sar1. {ECO:0000250|UniProtKB:Q15436}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15436}. Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q15436}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q15436}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q15436}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q15436}. Note=Enriched at endoplasmic reticulum
CC exit sites (ERES), also known as transitional endoplasmic reticulum
CC (tER). {ECO:0000250|UniProtKB:Q15436}.
CC -!- DOMAIN: The Gelsolin-like repeat mediates interaction with proteins
CC containing PPP motifs. {ECO:0000250|UniProtKB:Q15436}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000305}.
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DR EMBL; BC052768; AAH52768.1; -; mRNA.
DR EMBL; BC097063; AAH97063.1; -; mRNA.
DR RefSeq; NP_998630.1; NM_213465.1.
DR AlphaFoldDB; Q7SZE5; -.
DR SMR; Q7SZE5; -.
DR STRING; 7955.ENSDARP00000116386; -.
DR PaxDb; Q7SZE5; -.
DR Ensembl; ENSDART00000160156; ENSDARP00000137308; ENSDARG00000104230.
DR Ensembl; ENSDART00000168055; ENSDARP00000139718; ENSDARG00000104230.
DR Ensembl; ENSDART00000169522; ENSDARP00000134628; ENSDARG00000104230.
DR GeneID; 406774; -.
DR KEGG; dre:406774; -.
DR CTD; 10484; -.
DR ZFIN; ZDB-GENE-040426-2823; sec23a.
DR eggNOG; KOG1986; Eukaryota.
DR GeneTree; ENSGT00390000006916; -.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; Q7SZE5; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 270617at2759; -.
DR PhylomeDB; Q7SZE5; -.
DR TreeFam; TF300693; -.
DR Reactome; R-DRE-204005; COPII-mediated vesicle transport.
DR Reactome; R-DRE-2132295; MHC class II antigen presentation.
DR Reactome; R-DRE-5694530; Cargo concentration in the ER.
DR Reactome; R-DRE-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR PRO; PR:Q7SZE5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000104230; Expressed in presomitic mesoderm and 38 other tissues.
DR ExpressionAtlas; Q7SZE5; baseline and differential.
DR GO; GO:0030127; C:COPII vesicle coat; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; IMP:ZFIN.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; ISS:UniProtKB.
DR GO; GO:0048702; P:embryonic neurocranium morphogenesis; IMP:ZFIN.
DR GO; GO:0035138; P:pectoral fin morphogenesis; IMP:ZFIN.
DR GO; GO:0006605; P:protein targeting; IMP:ZFIN.
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 2: Evidence at transcript level;
KW Cytoplasm; Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Membrane; Metal-binding; Protein transport; Reference proteome; Transport;
KW Zinc.
FT CHAIN 1..765
FT /note="Protein transport protein Sec23A"
FT /id="PRO_0000318934"
FT REPEAT 632..718
FT /note="Gelsolin-like"
FT /evidence="ECO:0000255"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q15436"
FT CONFLICT 580
FT /note="F -> L (in Ref. 1; AAH97063)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 765 AA; 86080 MW; 8059BDF16CD43059 CRC64;
MATFQEFIQQ NEDRDGVRFS WNVWPSSRLE ATRMVVPVAS LFTPLKERPD LPPIQYEPVL
CSRATCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPTYAG ISEVNQPAEL LPQFSTIEYV
VQRGPQMPLN FLYVVDTCME DDDLQALKES LQMSLSLLPP TALVGLITFG RMVQVHELGC
EGISKSYVFR GTKDLNAKQL QEMLGLTKPA AAQAGRGPQQ PQVPPSNRFL QPVQKIDMNL
TDLLGELQRD PWPVTQGKRP LRSLGVALSI AVGLLECTFP NTGARIMAFI GGPATQGPGM
VVGDELKTPI RSWHDIEKDN AKFMKKATKH YEALANRAAA NGHIIDIYAC ALDQTGLLEM
KCCTNYTGGY MVMADSFNTS LFKQTFQRVF TKDVQGCFKM ALAGTLEIKT SREIKISGAI
GPCVSLNAKG PCVSENEMGT GGTSQWKICG LDPNTTLGFY FEVVNQHNAP IPQGGRGAIQ
YVTQYQHSSG QRRIRVTTIA RNWADAQSQI QSIAASFDQE AAAILMARLA VYKAETEEGP
DVLRWLDRQL IRLCQKFGDY HKEDPNSFRF SETFSLYPQF MFHLRRSPFL QVFNNSPDES
TYYRHQFMRQ DLTQSLIMVQ PILYAYSFNG PPEPVLLDSS SILPDRILLM DTFFQILIYH
GETVSQWRKA GYQDMPEYEN FRHLLQAPVD DAQELLHTRF PMPRYIDTEH GGSQARFLLS
KVNPSQTHNN MYAWGQESGA PILTDDVSLQ VFMDHLKKLA VSSAA
