ID   SEG1_ASHGO              Reviewed;         656 AA.
AC   Q75DQ4;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 2.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Eisosome protein SEG1;
DE   AltName: Full=Stabilizer of eisosome in gossypii protein 1;
GN   Name=SEG1; OrderedLocusNames=ABL037C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
RN   [3]
RP   FUNCTION.
RX   PubMed=21525038; DOI=10.1242/jcs.082487;
RA   Seger S., Rischatsch R., Philippsen P.;
RT   "Formation and stability of eisosomes in the filamentous fungus Ashbya
RT   gossypii.";
RL   J. Cell Sci. 124:1629-1634(2011).
CC   -!- FUNCTION: Important for the stabilization of eisosomes, large
CC       cytoplasmic protein assemblies that localize to specialized domains on
CC       the plasma membrane to cluster specific proteins at sites of membrane
CC       invaginations. {ECO:0000269|PubMed:21525038}.
CC   -!- SUBUNIT: Component of eisosomes, large cytoplasmic protein assemblies
CC       that localize to specialized domains termed MCCs on the plasma
CC       membrane. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Localizes
CC       to eisosomes. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SEG1 family. {ECO:0000305}.
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DR   EMBL; AE016815; AAS50734.2; -; Genomic_DNA.
DR   RefSeq; NP_982910.2; NM_208263.2.
DR   AlphaFoldDB; Q75DQ4; -.
DR   STRING; 33169.AAS50734; -.
DR   EnsemblFungi; AAS50734; AAS50734; AGOS_ABL037C.
DR   GeneID; 4618993; -.
DR   KEGG; ago:AGOS_ABL037C; -.
DR   eggNOG; ENOG502S0GH; Eukaryota.
DR   HOGENOM; CLU_417941_0_0_1; -.
DR   InParanoid; Q75DQ4; -.
DR   OMA; VKKWVPS; -.
DR   Proteomes; UP000000591; Chromosome II.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Reference proteome.
FT   CHAIN           1..656
FT                   /note="Eisosome protein SEG1"
FT                   /id="PRO_0000430247"
FT   REGION          28..95
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          135..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..656
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        35..49
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..91
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..217
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..367
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        415..467
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..577
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        620..638
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   656 AA;  70308 MW;  BB9146F22A00F262 CRC64;
     MLRKQTPGRA RPADVEAVAA VSALGKVMNQ DGTALDHSKV RKRESMLPTR GRSGRGGVRR
     ASAESAGRRT RSEDGKAARS ARERHMEDEF NAFGGRATAG VAKEVPARGG ADDGPVMTTK
     YVPSPRGLVK VTVPVSAGSS AHSSLRKSAS IHTGMNMRHG SGSRRASMTS AGSDAARRQA
     KSTAESSSAR TRSNKPKPRP SGDSHSPSPT TRAPVTPRRT TVKDLVAPPL PEEPEDSVST
     SGKGESIVPL NEKEEEQDEQ PFDSEANARS SPKTPKQGGH VPALEVSQHG FQTPVPDGPT
     MAEYLQSADP ILSAGATQRQ RELEEAEAAS TTPDGDRLKI GKSPSPMKSA MKNSPSAGTS
     KYNRPPLDTS SAADGAYLSL TTAENTRLNA QLSDDKMRKS PTLRQPKRRV SVHSPKTPSA
     ASADRSSKVL RQFSLSKPQG RTLAMNKNNS GEKQAQSPTS PKSNQKKVDP SVLYPREPPK
     KKSSFERERP QHKNLGFKNL SLRSEASNEF MYQGTLEGEI HQSPGQHVGH ETPKKALLSV
     TAEGWKSRFS DSDSENDSPP FSSNASGSTQ PSSHRDSSLA HHGGFGLFKH KDHHGHKPKH
     SLGASLASAK PHEPQKARLA PTSNRGSNTL SAERPLKNHN SFSGKLKKLF GKKHAT