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Database: UniProt
Entry: A0A3B0KRP7_DROGU
LinkDB: A0A3B0KRP7_DROGU
Original site: A0A3B0KRP7_DROGU 
ID   A0A3B0KRP7_DROGU        Unreviewed;       807 AA.
AC   A0A3B0KRP7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN   ORFNames=DGUA_6G015719 {ECO:0000313|EMBL:SPP87921.1};
OS   Drosophila guanche (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7266 {ECO:0000313|EMBL:SPP87921.1, ECO:0000313|Proteomes:UP000268350};
RN   [1] {ECO:0000313|Proteomes:UP000268350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (JAN-2018) 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. {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   EMBL; OUUW01000013; SPP87921.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0KRP7; -.
DR   STRING; 7266.A0A3B0KRP7; -.
DR   Proteomes; UP000268350; Unassembled WGS sequence.
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT   TRANSMEM        772..793
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          58..98
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          127..403
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          414..517
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          531..629
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          645..731
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
FT   REGION          206..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   807 AA;  90595 MW;  5DF031495A8E6FF8 CRC64;
     MTTYEEFIQQ NEDRDGVRLT WNVWPSSRID ASRLVVPLAC LYQPLKERPD LPPIQYEPVL
     CTRSNCRAIL NPLCQVDYRA KLWVCNFCFQ RNPFPPQYAA ISEQHQPAEL IPGFSTIEYT
     ITRAPTMPPV FIFLVDTCMD EEELDALKDS LQMSLSLLPP NALVGLITFG KMIQVHELGA
     EGCSKSYVFR GTKDLTAKQV QDMLGIGRGA APGPQQPGQA MPGQQRPNAP AAGAPVPPAH
     RFLQPISQCD AALGDLLSEL QRDPWPVSQG KRYLRSTGAA LSIAVGLLEC TYPNTGGRIM
     SFVGGPCSQG PGQVVDDELK HPIRSHHDIH KDNVKFMKKA IKHFDALALR AATNGHSVDI
     YSCALDQTGL LEMKQLCNST GGHMVMGDSF NSSLFKQTFQ RVFARDSRND LKMAFNATLE
     VKCSRELKIS GGIGSCVSLN VKSPSVSDVE IGMGNTVQWK LCTLNPSSTV AYFFEVVNQH
     AAPIPQGGRG CIQFITQYQH PSGQRRIRVT TLARNWADAT TNVHHISAGF DQEAAAVLMA
     RMVVYRAETD EGPDILRWVD RQLIRLCQKF GEYTKDDPNS FRLSQNFSLF PQFMYHLRRS
     QFLQVFNNSP DETTFYRHML MREDLTQSLI MIQPILYSYS FNGPPEPVLL DTASIQADRI
     LLMDTFFQIL IYHGETIAQW RALKYQDMPE YENFKQLLQA PVDDAQEILQ TRFPMPRYID
     TEHGGSQARF LLSKVNPSQT HNNMYAYGQP AIGQTTVVHL FFVHCFHTGN PLSFVVSKLL
     LVFGVGFVGV GFARHFPTRP FPAHHFD
//
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