ID A0A3N4J334_9PEZI Unreviewed; 972 AA.
AC A0A3N4J334;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Protein transport protein SEC24 {ECO:0000256|ARBA:ARBA00021213};
DE AltName: Full=Protein transport protein sec24 {ECO:0000256|ARBA:ARBA00013453};
GN ORFNames=L873DRAFT_1847583 {ECO:0000313|EMBL:RPA92742.1};
OS Choiromyces venosus 120613-1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Tuberaceae; Choiromyces.
OX NCBI_TaxID=1336337 {ECO:0000313|EMBL:RPA92742.1, ECO:0000313|Proteomes:UP000276215};
RN [1] {ECO:0000313|EMBL:RPA92742.1, ECO:0000313|Proteomes:UP000276215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=120613-1 {ECO:0000313|EMBL:RPA92742.1,
RC ECO:0000313|Proteomes:UP000276215};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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|ARBA:ARBA00025471}.
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}.
CC -!- SIMILARITY: Belongs to the SEC23/SEC24 family. SEC24 subfamily.
CC {ECO:0000256|ARBA:ARBA00008334}.
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; ML120466; RPA92742.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4J334; -.
DR STRING; 1336337.A0A3N4J334; -.
DR Proteomes; UP000276215; 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:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR CDD; cd01479; Sec24-like; 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; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR036180; Gelsolin-like_dom_sf.
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; IPR041742; Sec24-like_trunk_dom.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR006895; Znf_Sec23_Sec24.
DR InterPro; IPR036174; Znf_Sec23_Sec24_sf.
DR PANTHER; PTHR13803; SEC24-RELATED PROTEIN; 1.
DR PANTHER; PTHR13803:SF39; SECRETORY 24AB, ISOFORM A; 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|ARBA:ARBA00022490};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000276215};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 290..327
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 364..602
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 609..691
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 702..805
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 832..885
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 972 AA; 105225 MW; 9F8A34C9AA2B5E5E CRC64;
MASPPPPPPG TAPYGDPNQY AYQQGYAQPD PYGQQQQVPP AAGGYGQAPP YGQQAYGQPA
PTPQASGPPL AAGPAPGAHG GRGKRRGYAE EQYEFGAGAN AGLTPAQNPA YASQSMGGYP
NPQEQQQSQF VSPMGGTPPV MGTQGGYGVP QGMSGAGAGN IAAGGYEPAG APGMGGVTQS
FGQMGLTPAG GIQKVQSLNP LFTTDLMQQP LNVAELEFPP PEILLPPNAS LTPSPNSNCP
PQYMRSTINA VPTTHSLLKK SKLPFALIIQ PYTSLHDAED PVPLVSDTVI SRCRRCRSYI
NPYVTFLDHG HRWRCNMCNL TNDVPQAFDW DQAAQKNLDR WQRPELNSSV VEFIAPQEYM
VRPPQPLVYL FLLDVSYSAV QCGLLATAAR TILESLDRIP NADKRTRLGF ICVDSSLHYF
AIPRDSSEPS MLVVSDLDEP FLPIPGDLLV PLAECREGIE NLLGKLQDMF QNSQNGSSCM
GSALQAGHKL ISAIGGKIIV LTATLPCLGA GKLDNREDKK LLGTSKESAL LQTANSFYKS
FAVECSKNQV SVDMFLFSNS YQDVASLSNL PRYTGGQTYF YPGWNATRSE DAIKFAREFS
DHLSAEIALE AVMRVRATTG LRMQTFYGNF FNRSSDLCAF PAFPRDQGYV VEVAIDEALG
KQFVCMQTAV LHTTCNGERR IRVMTLALPT TQNLSDVYAS ADQVAITTFF SHKAVEKTLS
SGLEQAREAL QAKLTELLIT FKKELTASHV GAATPLSFAA NLRGLVVLFL GLMKHVGLRK
SAQIPTDLRS AALCLLSTLP APMLIQYIHP KFYSLHDMPD SCGLPDPTTG EIILPPAMNL
SSERLAPFGC YLIDDTQVQF LWIGPQAVPQ LVQDVFGLPG VEHVKVGKTT LPHLEGPGSE
FNERVRAVVE KSRDHKSKKV GSITVPHLYV VRGDGEPSLR LWAQTMLIED RTDQGVSLGQ
FLAQLKEKVN NS
//
