EIS1_YEAS1
ID EIS1_YEAS1 Reviewed; 843 AA.
AC B3LLS9;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Eisosome protein 1;
GN Name=EIS1; ORFNames=SCRG_01927;
OS Saccharomyces cerevisiae (strain RM11-1a) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=285006;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM11-1a;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Cuomo C.,
RA Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E.W., Brockman W., MacCallum I.A., Rounsley S., Young S.K.,
RA LaButti K., Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA O'Leary S., Kodira C.D., Zeng Q., Yandava C., Alvarado L., Pratt S.,
RA Kruglyak L.;
RT "Annotation of the Saccharomyces cerevisiae RM11-1a genome.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
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; CH408047; EDV11532.1; -; Genomic_DNA.
DR AlphaFoldDB; B3LLS9; -.
DR SMR; B3LLS9; -.
DR EnsemblFungi; EDV11532; EDV11532; SCRG_01927.
DR HOGENOM; CLU_013228_0_0_1; -.
DR Proteomes; UP000008335; Unassembled WGS sequence.
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_0000410802"
FT REGION 13..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..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..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..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; 93387 MW; 1B09E2B7D34CB6D6 CRC64;
MSLISAVEDR DIHNIGKTSG GGSRTSSITS SKKSLKHGSK SLRKPKVYQT TGELLSREAL
YKAKLKYGVY QSPAQSYSIG VSDAHAASDK AANLAHDNQT TVEAYKRMFI DPNATKAASK
MGPKVVRNNS ITSATSKTSK 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 ERDEINAEIS RLQDAIVDHK RKISGYGNDL DAQKNRNIRE
DDKLLELGQT KESLESHLND DVIILANKAK EQAELSTKEA RLKQLEVDSL INERKSELNA
TEIELKKEKL NLLEAMKDVA SARGDDKIDE EKVKKLIGMT SEEYLTQNKS VEKNVEDLPT
QLEKIEEGDE LKKEEIVGAE TKNSGGDGVP VSTAAKEATE TSSAVQTKEP EEKISIGNKS
SGKEDANDCK SAEHSKEISV SQKAGNNKSL GVSPDSLEHT FSGFSQGSSI EDDQDAISNQ
EKK
