ID R9AFG8_WALI9 Unreviewed; 1151 AA.
AC R9AFG8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Protein transport protein SEC23 {ECO:0000313|EMBL:EOR00953.1};
GN ORFNames=J056_004765 {ECO:0000313|EMBL:EOR00953.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR00953.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle
CC membrane {ECO:0000256|ARBA:ARBA00004299}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004299}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004299}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004397}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004255}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004255}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004255}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}. 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}.
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DR EMBL; KE007232; EOR00953.1; -; Genomic_DNA.
DR RefSeq; XP_009268230.1; XM_009269955.1.
DR AlphaFoldDB; R9AFG8; -.
DR STRING; 1299270.R9AFG8; -.
DR GeneID; 20377717; -.
DR KEGG; wic:J056_004765; -.
DR eggNOG; KOG1986; Eukaryota.
DR HOGENOM; CLU_008658_0_0_1; -.
DR OMA; FPPHYAE; -.
DR OrthoDB; 5474700at2759; -.
DR Proteomes; UP000014064; 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:0005254; F:chloride channel activity; IEA:InterPro.
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; 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; IPR021134; Bestrophin-like.
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; PF01062; Bestrophin; 2.
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 Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 444..482
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 511..775
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 786..888
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 901..999
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 1015..1101
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 109..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 150..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1151 AA; 128505 MW; 01DC065C74AE6B3E CRC64;
MVSIVIGLLV SMRASSSIQR WQEGRNLWSN IQSTVRSFMR LSSSVLEVNS HFENEKAIEE
FVGLILAFPV ALKYHLRENQ NKGLDELDLQ VLLPKGYLAS LKKTFPSRVR FESTSPDPSQ
PPSRTSSLQS SQENDKNKEL NEEKPSTTVK NVDSDVPDSS INRQQPASNA TNEVEKQHQQ
LNDKENDELL SVPQSVLSNS RPRNIPLSVL RLLQVYLNGF YNNRPEKAKD QTKTHIDTAL
YVNLTGYVKE MTSWLTEAEK IRDTPIPLIL SIHLNQVLGL YLLAIPPQLV SSLGWMAIPI
TGIVAFFFCG IDAISSQLSE PFGRHLNNLP IDQYCLDMVK EAQDIGGVPS SISRDALGNG
LANKPSYSFK PTPNTVNNLF QRDIEQPTAN MQVVEDVEER DGIRLSWNVW PSSRIEATRT
VVPISALYVP FKEREDLPPV LYEPVTCKSC RSILNPYCQI DVRGKLWICP FCLSRNAFPP
HYKDISNTNL PAELLPKYTT IEYTLSRPVQ VPPIFLFVVD TCLDAEDFQA LKETITLGLS
LLPPNALVGL ITFGTMTQVH EIGFNTCPKS YVFRGTKDYS PGQISSMLGI TPRSTTLPSQ
QQQRPGQLHG AARFLQPVQD AEFQLTSILD NLSRDPWPVP SDKRSFRCTG AALSVAVGIL
ENSFPNSGAR IMTFVGGPAT EGPGMVVSNE LKEPIRSHHD IERDSVKHFK RATRFYESLS
KRASSNGHVV DIYAGCLDQI GLLEMKSLPN LTNGALVLSD SFATLIFKQS FQRLFEKDEF
GNLKMGFNAT MDVQTSKELK VSGAIGHLTS AQKKSACVGE TEIGVGQTSA WKIGSINPRT
TLGVYFEVVS PPGQPVQQNQ RGLIQFITHY QSSSGQYKLR VTTIARNFAD AGSPAIAGSF
DQEAAAVLMA RIAVFKAEID DSPDVLRWLD RMLIRLCQKF ADYHKEDPTS FRLSENFGIY
PQFMFHLRRS QFLQVFNNSP DETAFYRHIL NEEDVNNSLV MIQPTLMSFS LDGPPQPVLL
DSVSIKNDVI LLLDTFFHIL IWHGETIAQW RKANYQDQEG YENFKELLTL PTNDAQDLLA
DRFPIPRYVV CDQGGSQARF LLSKLNPSTT HMSGGIYGSQ NAAGQAIFTD DVSLQVFMEH
LKRLAVGAST S
//
