位置:首页 > 蛋白库 > DSE2_KLULA
DSE2_KLULA
ID   DSE2_KLULA              Reviewed;         264 AA.
AC   Q6CRM2;
DT   01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Protein DSE2;
DE   AltName: Full=Daughter-specific expression protein 2;
DE   Flags: Precursor;
GN   Name=DSE2; OrderedLocusNames=KLLA0D07942g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Involved in pseudohyphal growth, cell wall metabolism and
CC       required for the separation of the mother and daughter cells.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall. Membrane {ECO:0000250};
CC       Lipid-anchor, GPI-anchor {ECO:0000250}. Note=GPI-anchored cell wall
CC       protein (GPI-CWP). {ECO:0000250}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382124; CAH00513.1; -; Genomic_DNA.
DR   RefSeq; XP_453417.1; XM_453417.1.
DR   AlphaFoldDB; Q6CRM2; -.
DR   STRING; 28985.XP_453417.1; -.
DR   EnsemblFungi; CAH00513; CAH00513; KLLA0_D07942g.
DR   GeneID; 2893450; -.
DR   KEGG; kla:KLLA0_D07942g; -.
DR   eggNOG; ENOG502S41K; Eukaryota.
DR   HOGENOM; CLU_1031328_0_0_1; -.
DR   InParanoid; Q6CRM2; -.
DR   OMA; TRVYPIT; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0009277; C:fungal-type cell wall; IEA:EnsemblFungi.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0007124; P:pseudohyphal growth; IEA:EnsemblFungi.
DR   GO; GO:0000920; P:septum digestion after cytokinesis; IEA:EnsemblFungi.
DR   InterPro; IPR026225; DSE2.
DR   PRINTS; PR02066; DSEPROTEIN2.
PE   3: Inferred from homology;
KW   Cell wall; Cell wall biogenesis/degradation; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Membrane; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..247
FT                   /note="Protein DSE2"
FT                   /id="PRO_0000285353"
FT   PROPEP          248..264
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000285354"
FT   REGION          75..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        75..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..213
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           247
FT                   /note="GPI-anchor amidated aspartate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   264 AA;  28409 MW;  0C99CB80D65F307B CRC64;
     MQFKKSSIVS FLSLLGSLTK AAAEVRLVTM DGVVYSYQVV TSTIKPATTY VETIYYTTTY
     VEAVTLTNHA VTSTTRESVV TSTLSSTSLL PETTEESTQE DEQTTDFTST TDVESTTDVT
     STTAETATLE PTTSDETYTT ELTPTTSVKT TLENDDSTSV ITTKSTSKAN TQSISRKTST
     LTPTVTSETT ESTSAETLSS TDKSTSTSSS SVLEPMVTNT DCQVVYEYTD DDEYYSTVEI
     SGTESVDAAT TYTKTRTVYA TISS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024