SC23A_CHICK
ID SC23A_CHICK Reviewed; 767 AA.
AC Q5ZK03;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Protein transport protein Sec23A {ECO:0000305};
DE AltName: Full=SEC23-related protein A;
GN Name=SEC23A {ECO:0000250|UniProtKB:Q15436};
GN ORFNames=RCJMB04_14a13 {ECO:0000312|EMBL:CAG31940.1};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(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 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; AJ720281; CAG31940.1; -; mRNA.
DR RefSeq; NP_001006179.1; NM_001006179.1.
DR RefSeq; XP_015138961.1; XM_015283475.1.
DR RefSeq; XP_015138962.1; XM_015283476.1.
DR RefSeq; XP_015138963.1; XM_015283477.1.
DR RefSeq; XP_015138964.1; XM_015283478.1.
DR AlphaFoldDB; Q5ZK03; -.
DR SMR; Q5ZK03; -.
DR BioGRID; 678193; 1.
DR STRING; 9031.ENSGALP00000014280; -.
DR PaxDb; Q5ZK03; -.
DR Ensembl; ENSGALT00000014296; ENSGALP00000014280; ENSGALG00000008793.
DR GeneID; 416724; -.
DR KEGG; gga:416724; -.
DR CTD; 10483; -.
DR VEuPathDB; HostDB:geneid_416724; -.
DR eggNOG; KOG1986; Eukaryota.
DR GeneTree; ENSGT00390000006916; -.
DR HOGENOM; CLU_008658_3_0_1; -.
DR InParanoid; Q5ZK03; -.
DR OMA; PWNIIPV; -.
DR OrthoDB; 270617at2759; -.
DR PhylomeDB; Q5ZK03; -.
DR TreeFam; TF300693; -.
DR PRO; PR:Q5ZK03; -.
DR Proteomes; UP000000539; Chromosome 3.
DR Bgee; ENSGALG00000008793; Expressed in spleen and 13 other tissues.
DR ExpressionAtlas; Q5ZK03; 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:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
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..767
FT /note="Protein transport protein Sec23A"
FT /id="PRO_0000318933"
FT REPEAT 634..720
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 767 AA; 86304 MW; 2D04B494F0EE52E5 CRC64;
MATYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPLAC LLTPLRERPD LPPVQYEPVL
CSRPTCKAVL NPLCQVDYRA KLWACNFCFQ RNQFPPAYAG ISEVNQPAEL MPQFSTIEYI
VQRGPQTPLI FLYVVDTCLE EEDLQALKES LQMSLSLLPA DALVGLITFG RMIQVHELSC
EGISKSYVFR GTKDLTAKQI QDMLGLSRPA VPIQQGRPLQ APEQPVISSR FLQPVHKIDM
NLTDLLGELQ RDPWPVTQGK RPLRSTGVAL SIAVGLLEGT FPNTGARIML FTGGPPTQGP
GMVVGDELKT PIRSWHDIEK DNARFMKKAT KHYETLANRT ATNGHCIDIY ACALDQTGLL
EMKCCANLTG GHMVMGDSFN TSLFKQTFQR VFNKGLNGEF RMAFGANLEV KTSRELKIAG
AIGPCVSLNV KGPCVSENEL GIGGTSQWKI CGLDPCTTLA IYFEVVNQHN APIPQGGRGA
VQFVTQYQHS STQKRIRVTT IARNWADAQS QLQHIEAAFD QEAAAVLMAR LGVYRAESEE
GPDVLRWLDR QLIRLCQKFG QYNKDDPNSF RLSESFSLYP QFMFHLRRSP FLQVFNNSPD
ESSYYRHHFA RQDLTQSLIM IQPILYAYSF HGPPEPVLLD SSSILPDRIL LMDTFFQIVI
YLGETIAQWQ KAGYQDMPEY ENFKHLLQAP LDDAQEILQT RFPMPRYVHT EHGGSQARFL
LSKVNPSQTH NNLYAWGQES GAPILTDDVS LQVFMDHLKK LAVSSAA
