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Database: UniProt
Entry: A0A0E0R7P2_ORYRU
LinkDB: A0A0E0R7P2_ORYRU
Original site: A0A0E0R7P2_ORYRU 
ID   A0A0E0R7P2_ORYRU        Unreviewed;       769 AA.
AC   A0A0E0R7P2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
OS   Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI11G12240.4, ECO:0000313|Proteomes:UP000008022};
RN   [1] {ECO:0000313|Proteomes:UP000008022}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA   Zhao Q.;
RL   Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblPlants:ORUFI11G12240.4}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) 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: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic vesicle, COPII-coated
CC       vesicle membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane
CC       protein {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   AlphaFoldDB; A0A0E0R7P2; -.
DR   EnsemblPlants; ORUFI11G12240.4; ORUFI11G12240.4; ORUFI11G12240.
DR   Gramene; ORUFI11G12240.4; ORUFI11G12240.4; ORUFI11G12240.
DR   Proteomes; UP000008022; Unassembled WGS sequence.
DR   GO; GO:0030127; C:COPII vesicle coat; IEA:InterPro.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
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; 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; 2.
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   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000008022};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365030};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU365030}.
FT   DOMAIN          51..83
FT                   /note="Zinc finger Sec23/Sec24-type"
FT                   /evidence="ECO:0000259|Pfam:PF04810"
FT   DOMAIN          125..404
FT                   /note="Sec23/Sec24 trunk"
FT                   /evidence="ECO:0000259|Pfam:PF04811"
FT   DOMAIN          415..519
FT                   /note="Sec23/Sec24 beta-sandwich"
FT                   /evidence="ECO:0000259|Pfam:PF08033"
FT   DOMAIN          533..622
FT                   /note="Sec23/Sec24 helical"
FT                   /evidence="ECO:0000259|Pfam:PF04815"
FT   DOMAIN          638..725
FT                   /note="Gelsolin-like"
FT                   /evidence="ECO:0000259|Pfam:PF00626"
SQ   SEQUENCE   769 AA;  83950 MW;  E02C7ABBFDDE1A40 CRC64;
     MAADPSAAAA AAPDPDGPDA VRLTWNAWPR SKVEASRCVV PLAAAISPPP CSALLNPFAR
     VDFAAKIWIC PLCFSRNHFP PHYAAISESN VPAELFPQCS TVEYLLAGAA PAAGVPLHQG
     GPPAPPPPVF LFVIDTCVIE EELEYVKMSM RKAVALLPEH ALVGLVTFGT QVHLHELGFS
     DLSKIYVFRG TKEISKEQIL DQLGLAGAGR PGFPKMPQQP GGPQINGMHP PATAGLLDEL
     QPDQWPVETG NRAIRCTGVA LSPDQWPVET GNRAIRCTGV ALSVAAGLLG ACMPGTGARI
     IALLGGPCTE GPGMIVSKDL SEPVRSHKDL DKDAAPHFQK AVKFYDGLAK QLVSQGHVLD
     VFASALDQVG LAEMKVAIER TGGLVVLSES FGHSVFKDSF KRIFEGGEQS LDLSFNGTLE
     INCSKDIKVQ GIIGPCTSLE KKGALCADTV VGQGNTTAWK MCGLDRNTSL TVFFDVSPSE
     RSSQPGHQNP DLYIQFVTSY QHPEGQMRIR VTTICRKWVD GSTNTEELVE GFDQETAAVV
     LARYISLKME MEEEFDATRW LDRSLIRLCS RFGDYRKDDP SSFSLHSNFS LFPQFMFNLR
     RSQFVQTAYF RMLLNRESIT NSVAMIQPSL ISFSFDSPPS PVFLDVASIA ADRILLLDAY
     FSVVIFHGMT IAQWRNMGYQ NQPEHQQFAQ LLQAPHEEAQ IIIKGRFPAP RLVVCDQHGS
     QARFLLAKLN PSATYNSAHD VPPGSDIIFT DDVSFQVFCE HLQRLAVQS
//
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