EIS1_YEASV
ID EIS1_YEASV Reviewed; 843 AA.
AC E7LYB2;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Eisosome protein 1;
GN Name=EIS1; ORFNames=VIN13_3618;
OS Saccharomyces cerevisiae (strain VIN 13) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=764099;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VIN 13;
RX PubMed=21304888; DOI=10.1371/journal.pgen.1001287;
RA Borneman A.R., Desany B.A., Riches D., Affourtit J.P., Forgan A.H.,
RA Pretorius I.S., Egholm M., Chambers P.J.;
RT "Whole-genome comparison reveals novel genetic elements that characterize
RT the genome of industrial strains of Saccharomyces cerevisiae.";
RL PLoS Genet. 7:E1001287-E1001287(2011).
CC -!- FUNCTION: Required for normal formation of eisosomes, large cytoplasmic
CC protein assemblies that localize to specialized domains on plasma
CC membrane and mark the site of endocytosis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic granule {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Note=Localizes at the eisosomes. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EIS1 family. {ECO:0000305}.
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DR EMBL; ADXC01000060; EGA77517.1; -; Genomic_DNA.
DR PRIDE; E7LYB2; -.
DR EnsemblFungi; EGA77517; EGA77517; VIN13_3618.
DR HOGENOM; CLU_013228_0_0_1; -.
DR OMA; EHTFSGF; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR024527; Eisosome1.
DR PANTHER; PTHR28298; PTHR28298; 1.
DR Pfam; PF12757; Eisosome1; 1.
PE 3: Inferred from homology;
KW Acetylation; Cell membrane; Membrane; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT CHAIN 2..843
FT /note="Eisosome protein 1"
FT /id="PRO_0000410807"
FT REGION 13..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..797
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 798..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 401
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 584
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 720
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 763
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 816
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 828
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05050"
SQ SEQUENCE 843 AA; 93315 MW; F80F9C51AB939C9E CRC64;
MSLISAVEDR DIHNIGKTSG GGSRTSSITS SKKSLKHGSK SLRKPKVYQT TGELLSREAL
YKAKLKYGVY QSPAQSYSIG VSDAHAASDK AANLAHDNQT TVEAYKRMFI DPNATKAASK
MGPKVVRNNS ITSATSKTSX ESQTKRKSKE SPGAAASKAY SMTMETTSLS SQTNSRSYSI
TSASSVLSGA SGSFNSTVNP KPKTLNLEKV LVGAEKKAES RIKERWEPEK TNFQYGVKTD
EHGNLNQFSF SNEMMNNIMA KVDAPKAQDL QKVKKVSAEK EAKSMKFALG AANAVKDMHP
GEDIDKSIAL KAQKRETYLS QLTSQQVLTL ARANVDRQLD IIEKSDMHRK LFTNMEYNKA
AVAVAQSNHQ KKTEFHNKIN MGGGLFLSPE DITKIASGLI SPVLGEVSER AEAQRAMDEE
IAERTEAYNK SLNEWETMER SIISNDAKVL TTTANRHQTE KKTSQEKIKA SFDALVARMD
TKVAERETLL EDTKSKEIEF KKQMQQELKD EKARLDQDLE EWGKKCEQDI TEARKEQEEL
LKPYHDDLAN AEAEHKTLVE ERDXINAEIS RLQDAIVDHK RKISGYGNDL DAQKNRNIRE
DDKLLELGQT KESLESHLND DVIILANKAK EQAELSTKEA RLKQLEVDSL INERKSELNA
TXIELKKEKL XLLEAMKDVA SARGDDKIDE EKVKKLIGMT SEEYLTQNKS VEKNVEDLPT
QLEXIEEGDE LKKEEIVGAE TKNSGGDGVP VSTAAKEATE TSSAVQTKEP EEKISIGNKS
SGKEDANDCK SAEHSKEISV SQKAGNNKSL GVSPDSLEHT FSGFSQGSSI EDDQDAISNQ
EKK
