ID A0A103XBN4_CYNCS Unreviewed; 728 AA.
AC A0A103XBN4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN ORFNames=Ccrd_024963 {ECO:0000313|EMBL:KVH87749.1};
OS Cynara cardunculus var. scolymus (Globe artichoke) (Cynara scolymus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=59895 {ECO:0000313|EMBL:KVH87749.1, ECO:0000313|Proteomes:UP000243975};
RN [1] {ECO:0000313|EMBL:KVH87749.1, ECO:0000313|Proteomes:UP000243975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2C {ECO:0000313|EMBL:KVH87749.1};
RX PubMed=26786968; DOI=10.1038/srep19427;
RA Scaglione D., Reyes-Chin-Wo S., Acquadro A., Froenicke L., Portis E.,
RA Beitel C., Tirone M., Mauro R., Lo Monaco A., Mauromicale G., Faccioli P.,
RA Cattivelli L., Rieseberg L., Michelmore R., Lanteri S.;
RT "The genome sequence of the outbreeding globe artichoke constructed de novo
RT incorporating a phase-aware low-pass sequencing strategy of F1 progeny.";
RL Sci. Rep. 6:19427-19427(2016).
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}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC23 subfamily.
CC {ECO:0000256|RuleBase:RU365030}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KVH87749.1}.
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DR EMBL; LEKV01005870; KVH87749.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A103XBN4; -.
DR STRING; 59895.A0A103XBN4; -.
DR EnsemblPlants; KVH87749; KVH87749; Ccrd_024963.
DR Gramene; KVH87749; KVH87749; Ccrd_024963.
DR OMA; TSRIWFC; -.
DR Proteomes; UP000243975; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0090114; P:COPII-coated vesicle budding; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd11287; Sec23_C; 1.
DR Gene3D; 2.60.40.1670; beta-sandwich domain of Sec23/24; 1.
DR Gene3D; 1.20.58.340; Magnesium transport protein CorA, transmembrane region; 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 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 PANTHER; PTHR11141; PROTEIN TRANSPORT PROTEIN SEC23; 1.
DR PANTHER; PTHR11141:SF22; 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 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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU365030};
KW Cytoplasmic vesicle {ECO:0000256|RuleBase:RU365030};
KW Endoplasmic reticulum {ECO:0000256|RuleBase:RU365030};
KW ER-Golgi transport {ECO:0000256|RuleBase:RU365030};
KW Membrane {ECO:0000256|RuleBase:RU365030, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU365030};
KW Protein transport {ECO:0000256|RuleBase:RU365030};
KW Reference proteome {ECO:0000313|Proteomes:UP000243975};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|RuleBase:RU365030}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 6..211
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 226..326
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 338..435
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 452..538
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
SQ SEQUENCE 728 AA; 81536 MW; 44A363E5EE30753E CRC64;
MKFPYDVHIS SGFVVFRTLV IVYFLQFQII DLLGIHTSVR QHLGKPQGVQ KHGFVLPVSE
CEFNITTAIE DIHESSPLTP GHRSPRCTGA AILVAVGLLE GCSTTTGSHI MVFTSGPATM
GPGLVVSQDL NQSIRTHRDI NTGHAPFYWK SCEFYKQISE KLTDLSMVLH LFACSLDQVG
ATEMRAAVER SGGFMMLAES FESDQFRKCL RHIFCRDKEG FLNMCFDATI KIITTKDVKI
CGAIGPCVSL RKKNGSVSDK EIGEGGTNIW KLGTMTDKMC IAFFFQVSEE QKAQPGTAFF
IQFITKYRHG NMGIRKRVTS AARRWVSSGA PEIAAGFDQE TAAAVMARLA VHETEKNFPR
EVVRWLDKEL ISFASKFGDY ICEDPSSFRL SSNFSLYPQF MYHLRRSQFI DVFNSSPDET
TFFQLTLTRE GVVGSLIMIQ PTLSQYSFDG PPIPVLLDVC SLSPDVILLF DSYFYVVIHY
GSKIARWKKL GYDRDPNHEN FRKLLEAPEV EAEQLVAQRI PVPKLVRCEQ HGSQARFLLA
KLNPSATHKS SYVDGSEVIM TDDVSLQAFI KHLQELAVQE LETDAYPALD EFTSKMGRVW
LNVGIFQPQL SLVRAASCGA ASWFLGSPTI GSKISRASRA SVMMVHGDEN DVEELEMLLE
AYFMQIDGTL NKLTSLREYI DDTEDYINIQ LELFLSSGTV CMSIYSLVTG QVDDEPSVKP
APRVMWRS
//
