ID M7X2D3_RHOT1 Unreviewed; 514 AA.
AC M7X2D3;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Epsin domain protein {ECO:0000313|EMBL:EMS24491.1};
GN ORFNames=RHTO_04670 {ECO:0000313|EMBL:EMS24491.1};
OS Rhodotorula toruloides (strain NP11) (Yeast) (Rhodosporidium toruloides).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=1130832 {ECO:0000313|EMBL:EMS24491.1, ECO:0000313|Proteomes:UP000016926};
RN [1] {ECO:0000313|EMBL:EMS24491.1, ECO:0000313|Proteomes:UP000016926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NP11 {ECO:0000313|EMBL:EMS24491.1,
RC ECO:0000313|Proteomes:UP000016926};
RX PubMed=23047670; DOI=10.1038/ncomms2112;
RA Zhu Z., Zhang S., Liu H., Shen H., Lin X., Yang F., Zhou Y.J., Jin G.,
RA Ye M., Zou H., Zou H., Zhao Z.K.;
RT "A multi-omic map of the lipid-producing yeast Rhodosporidium toruloides.";
RL Nat. Commun. 3:1112-1112(2012).
CC -!- SIMILARITY: Belongs to the epsin family.
CC {ECO:0000256|ARBA:ARBA00010130}.
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DR EMBL; KB722644; EMS24491.1; -; Genomic_DNA.
DR RefSeq; XP_016275610.1; XM_016418334.1.
DR AlphaFoldDB; M7X2D3; -.
DR GeneID; 27368683; -.
DR eggNOG; KOG2056; Eukaryota.
DR HOGENOM; CLU_012678_0_0_1; -.
DR OrthoDB; 1532at2759; -.
DR Proteomes; UP000016926; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0051179; P:localization; IEA:UniProt.
DR CDD; cd16991; ENTH_Ent1_Ent2; 1.
DR Gene3D; 1.25.40.90; -; 1.
DR InterPro; IPR013809; ENTH.
DR InterPro; IPR008942; ENTH_VHS.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR12276; EPSIN/ENT-RELATED; 1.
DR PANTHER; PTHR12276:SF110; FI19443P1; 1.
DR Pfam; PF01417; ENTH; 1.
DR SMART; SM00273; ENTH; 1.
DR SUPFAM; SSF48464; ENTH/VHS domain; 1.
DR PROSITE; PS50942; ENTH; 1.
DR PROSITE; PS50330; UIM; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121}.
FT DOMAIN 18..150
FT /note="ENTH"
FT /evidence="ECO:0000259|PROSITE:PS50942"
FT REGION 140..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 276..312
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 140..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..355
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 57676 MW; CDCF27E085B0DE83 CRC64;
MSAGLQTMGK SVMRVAKNSI KGYSDTQTKV RDATSNDPWG PSGTQMAELA QLTYNQQDFV
EIIEMLDKRL NDKGKNWRHV FKSLTVLDYI LHAGSENVVQ YFRENLYVVK TLKEFQYIDE
YGKDQGANVR QKAKDITNLL LDENRMRSQR ASRKDMRNRM AGRRTSPSRN ERPSRATPPP
GGAGGDADLQ AAIEASKRSA EEEARRKRGG KGEDELEEAL RLSREEEERR QRELAANGGG
NLFDEQQRNA NALIDMDAPT VQQPMQTGWM SFNPYQAQQQ AQMEEYMRQQ QLLELQRQQE
QQQMMYQQQQ AAMQQQYQQQ QAYEDYMRQQ QMLYMQQQAQ QPQQQAIQPQ PTGFGANNPF
AAFASPPPAS SPAPPQSQAS TSSAFGDSFQ PEPAAPSPAP QPQQPQRTGG GRFKATGDDK
HADLARMLGA GREDGLDTFG NIGSARVPVW QQKTGQQVAN GQGPLAPQTT GLAKPLNPFG
NVTGNYQAPT QFNQPTGFQQ QQQKQDNEQP FFTI
//
