ID A0A0D7ATH9_9AGAR Unreviewed; 345 AA.
AC A0A0D7ATH9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Sec20-domain-containing protein {ECO:0000313|EMBL:KIY61527.1};
GN ORFNames=CYLTODRAFT_427491 {ECO:0000313|EMBL:KIY61527.1};
OS Cylindrobasidium torrendii FP15055 ss-10.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Physalacriaceae;
OC Cylindrobasidium.
OX NCBI_TaxID=1314674 {ECO:0000313|EMBL:KIY61527.1, ECO:0000313|Proteomes:UP000054007};
RN [1] {ECO:0000313|EMBL:KIY61527.1, ECO:0000313|Proteomes:UP000054007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FP15055 ss-10 {ECO:0000313|EMBL:KIY61527.1,
RC ECO:0000313|Proteomes:UP000054007};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004163}. Membrane
CC {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC {ECO:0000256|ARBA:ARBA00004211}.
CC -!- SIMILARITY: Belongs to the SEC20 family.
CC {ECO:0000256|ARBA:ARBA00037934}.
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DR EMBL; KN880923; KIY61527.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7ATH9; -.
DR STRING; 1314674.A0A0D7ATH9; -.
DR OrthoDB; 1709334at2759; -.
DR Proteomes; UP000054007; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:InterPro.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IEA:InterPro.
DR InterPro; IPR005606; Sec20.
DR PANTHER; PTHR12825; BNIP1-RELATED; 1.
DR PANTHER; PTHR12825:SF0; VESICLE TRANSPORT PROTEIN SEC20; 1.
DR Pfam; PF03908; Sec20; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW ER-Golgi transport {ECO:0000256|ARBA:ARBA00022892};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054007};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 212..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 289..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 38029 MW; 9D13CDEACD3CCFAC CRC64;
MPPVPPTFSP EAVQLIDSIE RRFKDVREYQ IPRLRAFKGT LGAQQDLATE VREDIDTVGR
LIESLELSVG DLKSARDRNQ LQHLVDGFTG SLAAVRREYR TALLESKRAI DSMSKSNREE
LLKSNVASKK YDEKSTGDLL MKANNDVTDA LQRTIGLMQG ELEKSVLSTQ MLESSTATLR
STSATHDTLT NVMGTSKQLI TALEKADWMD RMLIMAALLF FILVVLFIIK QRLVDRGVRI
AFWWTRFLPG LGSDPDDALL EKLEKGVRTT LEVAPSVLTS LAAGLTASGT TGTTAQATEN
PATVEEEEPS PIDTALSTQP SDSVVESEDA RTLTTQDAVY VHEEL
//
