ID A0A0K9NVK2_ZOSMR Unreviewed; 863 AA.
AC A0A0K9NVK2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN ORFNames=ZOSMA_58G01060 {ECO:0000313|EMBL:KMZ60648.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ60648.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(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}. 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|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:KMZ60648.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LFYR01001606; KMZ60648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9NVK2; -.
DR STRING; 29655.A0A0K9NVK2; -.
DR OMA; WMERLGH; -.
DR OrthoDB; 463590at2759; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0030127; C:COPII vesicle coat; IBA:GO_Central.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd11280; gelsolin_like; 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; 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; 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:SF6; PROTEIN TRANSPORT PROTEIN SEC23; 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:UP000036987};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT DOMAIN 184..222
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 264..492
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 509..601
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 613..711
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 863 AA; 94611 MW; 4196BFCB3FED9649 CRC64;
MADLPPLGYN TFATPPTTPA PTMEKRPIQS PSSIASQLTS KLPIQMSPQS QSPLHSSVTP
TPVPSSDGGS TTASQFSTPP GPPVFSTPLR PAAIPFRTTP TTPQNAPFSP VPSPPLYSNG
STEKPSKIPA NVDEACLDTP YVLFSAHKVM KQRKLANTQC LGFGALVSPG GDVASATQII
QRDPHRCQNC GAYVNLYCEI LLASGQWQCV ICKKLNGSDG EYVASRREDL FHLTELCSPT
VDYIQTGNRR PGYLPVIDSR ISSPVFLVID ECLDEAHLQH LQGSLHAFVD SLSPKTRIGI
ITYGRTVSIY DFSEGLMAAA DVLPGEKSPT LDSLHALIYG TGIYLSQVHA SLPVVHSIFS
SLRPYKYGFP EASRDRCLGV AVEVALAIIQ GPSPEASHGV VKRPGGNCRI LVCAGGPNTY
GPGSVPHSFS HPNYPYVEKT AIKWMDNLGQ KARNLDTVVD VLCAGTCPVR VPVLQPLAKC
SGGVLILQDD FGEAFGVNLQ RASTRAAGSH GVFEIRCSND ILVTNVIGPG EEAPLESRDV
FKNDDFTCIQ MLSVEESQCF SLSMESNGDI ENDHVYFQFA IRYLNSFQAE YSRVITVRLP
TVDSLSAYLQ SVQQDVLAVL IAKRTLLRAQ TFSDAVGMRS IIDERVRDIA AKFGTQSSNS
KLYRFPKELF SLPEHLFHLR RGPLLGSIVG HEDERSVLRN LFLHASFDLS LRMLSPRCLM
YREEGTFEEL PAYDLAMQSD TAVVLDHGTD VFIWLGAELV AQEGKRASAL AACRTLAEEL
TDQRFPSPRI LSFKEGSSQA RYFVSRLIPA HKDPPYEQEV RFPQLQSLNS EQRAKLKSSF
IQFDDYSLIE WMRSMKLSSP EPS
//
