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SEL1_SCHPO
ID   SEL1_SCHPO              Reviewed;         636 AA.
AC   O13858; Q9UU73;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Eisosome protein sle1;
DE   AltName: Full=SEG1-like eisosome protein 1;
GN   Name=sle1; Synonyms=seg1; ORFNames=SPAC1A6.07;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 109-298, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=22869600; DOI=10.1083/jcb.201202097;
RA   Moreira K.E., Schuck S., Schrul B., Frohlich F., Moseley J.B.,
RA   Walther T.C., Walter P.;
RT   "Seg1 controls eisosome assembly and shape.";
RL   J. Cell Biol. 198:405-420(2012).
CC   -!- FUNCTION: Important for the biogenesis of filamentous 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:22869600}.
CC   -!- SUBUNIT: Component of eisosomes, large cytoplasmic protein assemblies
CC       that localize to specialized domains termed MCCs on the plasma
CC       membrane. {ECO:0000269|PubMed:22869600}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22869600};
CC       Peripheral membrane protein {ECO:0000269|PubMed:10759889}; Cytoplasmic
CC       side {ECO:0000269|PubMed:22869600}. Cell tip
CC       {ECO:0000269|PubMed:22869600}. Note=Localizes to eisosomes.
CC       {ECO:0000269|PubMed:22869600}.
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DR   EMBL; CU329670; CAB16357.1; -; Genomic_DNA.
DR   EMBL; AB027774; BAA87078.1; -; Genomic_DNA.
DR   PIR; T38010; T38010.
DR   RefSeq; NP_593199.1; NM_001018595.2.
DR   AlphaFoldDB; O13858; -.
DR   BioGRID; 278944; 15.
DR   STRING; 4896.SPAC1A6.07.1; -.
DR   iPTMnet; O13858; -.
DR   MaxQB; O13858; -.
DR   PaxDb; O13858; -.
DR   PRIDE; O13858; -.
DR   EnsemblFungi; SPAC1A6.07.1; SPAC1A6.07.1:pep; SPAC1A6.07.
DR   GeneID; 2542484; -.
DR   KEGG; spo:SPAC1A6.07; -.
DR   PomBase; SPAC1A6.07; sle1.
DR   VEuPathDB; FungiDB:SPAC1A6.07; -.
DR   eggNOG; KOG1181; Eukaryota.
DR   HOGENOM; CLU_513042_0_0_1; -.
DR   InParanoid; O13858; -.
DR   OMA; KLFKIRF; -.
DR   PRO; PR:O13858; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR   GO; GO:0036286; C:eisosome filament; IDA:PomBase.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0007009; P:plasma membrane organization; IC:PomBase.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome.
FT   CHAIN           1..636
FT                   /note="Eisosome protein sle1"
FT                   /id="PRO_0000304029"
FT   REGION          1..297
FT                   /note="Required for targeting the protein to eisosomes"
FT   REGION          111..205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          222..284
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          313..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          400..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          572..604
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..283
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..387
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..446
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..483
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..514
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   636 AA;  69794 MW;  D704DB95EBD1EDC3 CRC64;
     MSHASKNYNA QLTAAAASTA LHGTKKIYNS NENDRAVNSF LGNRTSYGEA VNGSPQYDYM
     RSRMSTLGSA NQPMAPPSLR NRSSVYLPTP AGPPQIPVNT GKRYTLTSSS ANYMTKSERQ
     MRPPKSYDFP PSQQVRPSTS RSPSYASYNS EEVNFQSYQD PRLLPRTSQM YMPDNNYSPA
     VKSPAAQRRS SSYMVPANSR GSPANYNTPY YPTAIPPPIE EYSPSVSLPT SPVAEESYNN
     VQRSSTVRNN TTQKSVLKKP SRKMSPAYTS SYRQNSPSSQ VPPVSKKHVI IYENKEGSSS
     SESVYEDVFE DFDPSGSNQA SLRSTSTIHY TPSSKRISVI PPNTSNIGSR VVSRSGQNNN
     QPAQPGQYNQ QSQPVQSYQS GQSTQHFQPV QPIQPVQSTQ YYQPSSPVQP VQNGVPAPPM
     QPVQSTQYYQ PSSPVQPVQN VKPAQPAQPS LEDAAKRRVE EMLRQMDITP TASSTTANNA
     YASAEPHPSA FPDDMNSVFS DSSFERERDS GRGRSTNLFS KFKSGRSRSK ASGEAPYSYP
     APPVPSVNNA GARLTLRDSG AAPEATYSLR QPSNHAYSEG RSYTFTGGQP PSVPTMPYGS
     RFANDSDSMM GSTADFSSKK KGGKFKAFKK FFKMRF
 
 
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