ID A0A165K532_EXIGL Unreviewed; 381 AA.
AC A0A165K532;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Protein transport protein SEC23 {ECO:0000256|RuleBase:RU365030};
GN ORFNames=EXIGLDRAFT_459703 {ECO:0000313|EMBL:KZV95805.1};
OS Exidia glandulosa HHB12029.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Auriculariales; Exidiaceae; Exidia.
OX NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZV95805.1, ECO:0000313|Proteomes:UP000077266};
RN [1] {ECO:0000313|EMBL:KZV95805.1, ECO:0000313|Proteomes:UP000077266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12029 {ECO:0000313|EMBL:KZV95805.1,
RC ECO:0000313|Proteomes:UP000077266};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(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: Cytoplasm {ECO:0000256|RuleBase:RU365030}.
CC Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {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}. Golgi apparatus 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|ARBA:ARBA00009210, ECO:0000256|RuleBase:RU365030}.
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; KV425951; KZV95805.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165K532; -.
DR STRING; 1314781.A0A165K532; -.
DR InParanoid; A0A165K532; -.
DR OrthoDB; 5474700at2759; -.
DR Proteomes; UP000077266; 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:0000139; C:Golgi 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; 1.20.120.730; Sec23/Sec24 helical domain; 1.
DR Gene3D; 3.40.20.10; Severin; 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; IPR012990; Sec23_24_beta_S.
DR InterPro; IPR037550; Sec23_C.
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 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.
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 Golgi apparatus {ECO:0000256|RuleBase:RU365030};
KW Membrane {ECO:0000256|RuleBase:RU365030};
KW Metal-binding {ECO:0000256|RuleBase:RU365030};
KW Protein transport {ECO:0000256|RuleBase:RU365030};
KW Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW Transport {ECO:0000256|RuleBase:RU365030};
KW Zinc {ECO:0000256|RuleBase:RU365030}.
FT DOMAIN 13..115
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 128..226
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 240..329
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
SQ SEQUENCE 381 AA; 42328 MW; D260074326D86BC9 CRC64;
MFAKGDDGHL QMGLNATFDV QCTKELKVSG LIGHAVSINK KSACVGETEI GIGGTSAWKV
CALMPRTALA VYFEVVTPAG QSLQPGTRGL IQFVTHYQHA SGQMRLRVTT LARNFVDGTS
PSLSVSFDQE AAAALMARVA VFKAEIDDSP DVLRWLDRML IRLCQKFADY RKEDPSSFRL
SDNFSIYPQF MFHLRRSQFL QVFNNSPDET AFYRHVMNEE DVNNSLIMIQ PTLMSYALDQ
PQPQPVLLDS MSVKPDVILL LDTFFHILIF HGETIAQWRK AGYHEQEGYE NLKELLSLPV
ADAQDLLVDR FPIPRYIVCD QHGSQARFLT SKLNPSTTHM SQGMYGTSSG GGSGAAIFTD
DVSLQVFMEA LKRLAVGAAT Q
//
