ID A0A1W4WG52_AGRPL Unreviewed; 771 AA.
AC A0A1W4WG52;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN Name=LOC108735444 {ECO:0000313|RefSeq:XP_018322904.1};
OS Agrilus planipennis (Emerald ash borer) (Agrilus marcopoli).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Elateriformia;
OC Buprestoidea; Buprestidae; Agrilinae; Agrilus.
OX NCBI_TaxID=224129 {ECO:0000313|Proteomes:UP000192223, ECO:0000313|RefSeq:XP_018322904.1};
RN [1] {ECO:0000313|RefSeq:XP_018322904.1}
RP IDENTIFICATION.
RC TISSUE=Entire body {ECO:0000313|RefSeq:XP_018322904.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|RuleBase:RU365030}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU365030}. Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side
CC {ECO:0000256|RuleBase:RU365030}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000256|ARBA:ARBA00009210, ECO:0000256|RuleBase:RU365030}.
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DR RefSeq; XP_018322904.1; XM_018467402.2.
DR AlphaFoldDB; A0A1W4WG52; -.
DR STRING; 224129.A0A1W4WG52; -.
DR EnsemblMetazoa; XM_018467402.2; XP_018322904.1; LOC108735444.
DR GeneID; 108735444; -.
DR KEGG; apln:108735444; -.
DR InParanoid; A0A1W4WG52; -.
DR OrthoDB; 5474700at2759; -.
DR Proteomes; UP000192223; Unplaced.
DR GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR GO; GO:0005789; C:endoplasmic reticulum 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; cd01478; Sec23-like; 1.
DR CDD; cd11287; Sec23_C; 1.
DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR Gene3D; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR Gene3D; 3.40.20.10; Severin; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 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; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR PANTHER; PTHR11141:SF0; PROTEIN TRANSPORT PROTEIN SEC23; 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; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF82754; C-terminal, gelsolin-like domain of Sec23/24; 1.
DR SUPFAM; SSF81811; Helical domain of Sec23/24; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR SUPFAM; SSF82919; Zn-finger domain of Sec23/24; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU365030};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329,
KW ECO:0000256|RuleBase:RU365030};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824,
KW ECO:0000256|RuleBase:RU365030};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892,
KW ECO:0000256|RuleBase:RU365030};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365030};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU365030};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU365030};
KW Reference proteome {ECO:0000313|Proteomes:UP000192223};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT DOMAIN 58..98
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 128..396
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 407..510
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 524..622
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 638..724
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
SQ SEQUENCE 771 AA; 86913 MW; 723D944ED8A15A05 CRC64;
MATFEEYIQQ NEDRDGIRFT WNVWPSSRIE AARLVVPLGC LYQPVKERPD LPPIQYDPVL
CTRNNCRAIL NPLCQVDYRA KLWVCNFCFQ RNPFPPQYAA ISEQHQPAEL MPTFSTIEYT
ITRAQCLPPI FLYVVDTCMD EEELGALKDS LQMSLSLLPS NALIGLITFG KMVQVHELGT
EGCSKSYVFR GTKDLTAKQI QEMLGLTKVA AVPHQQQPQM RGGPHPPAAP PSSRFLQPIA
NCDICLTDLI GELQRDPWPV PQGKRPLRST GAALSIAVGL LECTYPNTGA RIMMFLGGPC
SQGPGQVVND DLKQPIRSHH DIHKDNARYM KKAIKHYEGL AVRAATNSHC VDIYSCALDQ
TGLMEMKQCC NSTGGHMVMA DSFNSSLFKQ TFQRVFARDQ KGDLKMAFNA VLEVKCSREL
KVQGAIGACV SLNVKSPLVA DSEIGMGNTV QWKMCTLMPN NTTALFFEVV NQHSAPIPQG
GRGCVQFITQ YQHCSGQKRI RVTTIARNWA DAATNLHHIS AGFDQEAAAV LMARMVVYRA
ESDDGPDVLR WVDRMLIRLC QKFGEYNKDD PGSFRLSENF SLYPQFMYHL RRSQFLQVFN
NSPDETSFYR HMLMREDLTQ SLIMIQPILY SYSFNGPPEP VLLDTSSIQP DRILLMDTFF
QILIFHGETI AQWRSLKYQD MPEYENFRQL LQAPVDDAQE ILQTRFPMPR YIDTEQGGSQ
ARFLLSKVNP SQTHNNMYSY GGDSGAPVLT DDVSLQIFMD HLKKLAVSST A
//
