ID   SC23A_XENTR             Reviewed;         765 AA.
AC   Q05AS9;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Protein transport protein Sec23A {ECO:0000305};
DE   AltName: Full=SEC23-related protein A;
GN   Name=sec23a {ECO:0000250|UniProtKB:Q15436};
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (SEP-2006) 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; BC123946; AAI23947.1; -; mRNA.
DR   RefSeq; NP_001072659.1; NM_001079191.1.
DR   RefSeq; XP_012824104.1; XM_012968650.2.
DR   AlphaFoldDB; Q05AS9; -.
DR   SMR; Q05AS9; -.
DR   PaxDb; Q05AS9; -.
DR   DNASU; 780116; -.
DR   Ensembl; ENSXETT00000067553; ENSXETP00000071395; ENSXETG00000032554.
DR   GeneID; 780116; -.
DR   KEGG; xtr:780116; -.
DR   CTD; 10484; -.
DR   Xenbase; XB-GENE-999781; sec23a.
DR   eggNOG; KOG1986; Eukaryota.
DR   HOGENOM; CLU_008658_3_0_1; -.
DR   InParanoid; Q05AS9; -.
DR   OrthoDB; 270617at2759; -.
DR   Reactome; R-XTR-204005; COPII-mediated vesicle transport.
DR   Reactome; R-XTR-2132295; MHC class II antigen presentation.
DR   Reactome; R-XTR-5694530; Cargo concentration in the ER.
DR   Reactome; R-XTR-983170; Antigen Presentation: Folding, assembly and peptide loading of class I MHC.
DR   Proteomes; UP000008143; Chromosome 8.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000032554; Expressed in skeletal muscle tissue and 12 other tissues.
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:0090110; P:COPII-coated vesicle cargo loading; ISS:UniProtKB.
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   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_0000318935"
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"
SQ   SEQUENCE   765 AA;  86039 MW;  17C21F2D6EA66CA6 CRC64;
     MTTFLEFIQQ NEDRDGVRFS WNVWPSSRLE ATRMVVPVAA LLTPLKERPD LPPIQYEPVL
     CSRTTCRAVL NPLCQVDYRA KLWACNFCYQ RNQFPPTYAG ISEMNQPAEL LPQFSSIEYV
     VQRGPQMPLI FLYVVDTCME DEDLQALKES MQMSLSLLPP TALVGLITFG RMVHVHELGC
     EGISKSYVFR GNKDLTGKQI QEMLSLTKSP AAQQGRGPQV QQPPPSNRFL QPVQNIDMNL
     TDLLGELQRD PWPVPQGKRP LRSSGAALSI AVGLLECTFP NTGARIMMFI GGPATQGPGM
     VVGDELKTPI RSWHDIEKDN AKYVKKATKH YEALAHRAAA SGHVIDIYAC ALDQTGLLEM
     KCCPNNTGGY MVMGDSFNTS LFKQTFQRVF TKDAQSNFKM AFGGTLEIKT SRELKISGAI
     GPCVSLNAKG PCVSENEIGT GGTCQWKICG INPFTTLAVY FEVVNQHNAP IPQGGRGAIQ
     FVTQYQHSSG QRRIRVTTIA RNWADAQTQI QNIAASFDQE AAAILMARLA VYRAETEEGP
     DVLRWLDRQL IRLCQKFGEY HKDDPVSFKF SETFSLYPQF MFHLRRSPFL QVFNNSPDES
     SYYRHHFMRQ DLTQSLIMVQ PILYAYSFNG PPEPVLLDSS SILPDRILLM DTFFQILIYL
     GETIAQWKKA GYQDMPEYEN FRHLLQAPVD DGQEILQSRF PMPRYIDTEH GGSQARFLLS
     KVNPSQTHNN MYGWGQESGA PILTDDVSLQ VFMDHLKKLA VSSAA