ID A7F0N1_SCLS1 Unreviewed; 964 AA.
AC A7F0N1;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE RecName: Full=Sec23/Sec24 family protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SS1G_11149 {ECO:0000313|EMBL:EDN95273.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN95273.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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}.
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DR EMBL; CH476637; EDN95273.1; -; Genomic_DNA.
DR RefSeq; XP_001587908.1; XM_001587858.1.
DR AlphaFoldDB; A7F0N1; -.
DR STRING; 665079.A7F0N1; -.
DR EnsemblFungi; EDN95273; EDN95273; SS1G_11149.
DR GeneID; 5484077; -.
DR KEGG; ssl:SS1G_11149; -.
DR VEuPathDB; FungiDB:sscle_12g087970; -.
DR eggNOG; KOG1984; Eukaryota.
DR HOGENOM; CLU_004589_1_0_1; -.
DR InParanoid; A7F0N1; -.
DR OMA; INPFMTF; -.
DR OrthoDB; 977017at2759; -.
DR Proteomes; UP000001312; 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:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR GO; GO:0090110; P:COPII-coated vesicle cargo loading; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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; 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:SF4; SECRETORY 24CD, ISOFORM C; 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 Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000001312};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 251..289
FT /note="Zinc finger Sec23/Sec24-type"
FT /evidence="ECO:0000259|Pfam:PF04810"
FT DOMAIN 329..576
FT /note="Sec23/Sec24 trunk"
FT /evidence="ECO:0000259|Pfam:PF04811"
FT DOMAIN 581..665
FT /note="Sec23/Sec24 beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF08033"
FT DOMAIN 677..776
FT /note="Sec23/Sec24 helical"
FT /evidence="ECO:0000259|Pfam:PF04815"
FT DOMAIN 804..850
FT /note="Gelsolin-like"
FT /evidence="ECO:0000259|Pfam:PF00626"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 964 AA; 106185 MW; 1C801C4B9067A82F CRC64;
MAQPPFQQQP YYGGQPVYQD QGNPMMHPTD PNDLGMENLQ ISNQQPAPRK KKKDRHAYHV
VEAQGSSQAF NGIPQGGVPP SAFLNADPSL IPSPGGQFLN SPITPQMSQF PAPVNAPFNP
TNPATPAEFA ARTGPGDAFS ANVQTSAQGR VDPDQIPSVP RSRDAIAQYY LKNVYPTFEH
HLPPPATVPF VAYDQGNASP KFARLTMNNI PSTADALHST GLPLGLLLQP LAPLQPGELE
IPVLDFGETG PPRCHRCRAY INPFMVFRSG GNKFVCNMCN YANDVPAEYF CATTPQGARV
DREQRPELMR GTVEFLVPKE YWSQEPVGLR WIFLIDVGQE ALNKGFLEAF CEGILAALYG
GDDSTEEDGS SKRKIPEGSK VGFVTFDKDI HFYNMNPALE QAQMLIMPDI EDPFVPLSDG
LFVDPYEAKS NITSLLSQLP QLFSQIKNPE PALLPTINAA MAALEKTGGK IVCSLSALPT
WGPGRLFLRD DGKQHGGEQD KKLFTTEHPG WRKAADKMVA TGVGIDLFLA APGGGYLDIA
TIGHVAAATG GETFYYPNFV SPRDNEKLSH EIVRSVTRET GYQALMKVRC SNGLQISSYH
GNFIQHTFGA DIEFGVIDSD KAMGVLFSYD GKLDSKLDAH FQSALLYTTA SGERRVRCSN
VIASVSDQPK ECMNFVDQDA IYSLIAKEAA SKMLAHSLKE IRGALSEKNV DILAGYRKNF
SGSHPPGQLV LPEHLKEFSM YILGLIKSRA FKGGQEPSDR RVHDARMIKS MGALELSLYL
YPRMIPIHNL APEDGFANED GHLRMPPSVR ASFARVEEGG VYLVDNGQNC YLWMHGQTSP
NLIVDLFGED KDNLKALDPY LSSLPVLQTH LSAQVRNILE YLKTMRGAKA LTIQLARQGL
DGAEYEFARL LVEDRNNEAQ SYVDWLVHLH RHVQLELTGQ RKKDDSGDNS SITSNFAGLR
PPYW
//
