位置:首页 > 蛋白库 > RBR2_CANAL
RBR2_CANAL
ID   RBR2_CANAL              Reviewed;         168 AA.
AC   Q5A6M2; A0A1D8PST4; Q5A6W7;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Repressed By RIM101 protein 2;
DE            EC=3.1.1.-;
DE   AltName: Full=Predicted GPI-anchored protein 21;
DE   Flags: Precursor;
GN   Name=RBR2; Synonyms=PGA21; OrderedLocusNames=CAALFM_CR04420CA;
GN   ORFNames=CaO19.532, CaO19.8165;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN   [4]
RP   INDUCTION.
RX   PubMed=12397174; DOI=10.1073/pnas.232566499;
RA   Lan C.Y., Newport G., Murillo L.A., Jones T., Scherer S., Davis R.W.,
RA   Agabian N.;
RT   "Metabolic specialization associated with phenotypic switching in
RT   Candidaalbicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14907-14912(2002).
RN   [5]
RP   PREDICTION OF GPI-ANCHOR.
RX   PubMed=12845604; DOI=10.1002/yea.1007;
RA   De Groot P.W., Hellingwerf K.J., Klis F.M.;
RT   "Genome-wide identification of fungal GPI proteins.";
RL   Yeast 20:781-796(2003).
RN   [6]
RP   INDUCTION.
RX   PubMed=15189998; DOI=10.1128/ec.3.3.776-784.2004;
RA   Lotz H., Sohn K., Brunner H., Muhlschlegel F.A., Rupp S.;
RT   "RBR1, a novel pH-regulated cell wall gene of Candida albicans, is
RT   repressed by RIM101 and activated by NRG1.";
RL   Eukaryot. Cell 3:776-784(2004).
RN   [7]
RP   INDUCTION.
RX   PubMed=16987174; DOI=10.1111/j.1365-2958.2006.05367.x;
RA   Bennett R.J., Johnson A.D.;
RT   "The role of nutrient regulation and the Gpa2 protein in the mating
RT   pheromone response of C. albicans.";
RL   Mol. Microbiol. 62:100-119(2006).
RN   [8]
RP   INDUCTION.
RX   PubMed=17164403; DOI=10.1074/mcp.m600210-mcp200;
RA   Fernandez-Arenas E., Cabezon V., Bermejo C., Arroyo J., Nombela C.,
RA   Diez-Orejas R., Gil C.;
RT   "Integrated proteomics and genomics strategies bring new insight into
RT   Candida albicans response upon macrophage interaction.";
RL   Mol. Cell. Proteomics 6:460-478(2007).
CC   -!- FUNCTION: Probable cell wall protein which may have esterase activity,
CC       with a preference for esters of fatty acids from 4 to 16 carbon atoms.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000250}. Membrane
CC       {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
CC   -!- INDUCTION: Expression is regulated upon white-opaque switching.
CC       Repressed by RIM101 and alpha pheromone, and up-regulated upon
CC       interaction with macrophages. {ECO:0000269|PubMed:12397174,
CC       ECO:0000269|PubMed:15189998, ECO:0000269|PubMed:16987174,
CC       ECO:0000269|PubMed:17164403}.
CC   -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC       reticulum and serves to target the protein to the cell surface. There,
CC       the glucosamine-inositol phospholipid moiety is cleaved off and the
CC       GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC       glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SRP1/TIP1 family. {ECO:0000305}.
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; CP017630; AOW31179.1; -; Genomic_DNA.
DR   RefSeq; XP_717395.2; XM_712302.2.
DR   AlphaFoldDB; Q5A6M2; -.
DR   STRING; 237561.Q5A6M2; -.
DR   GeneID; 3640983; -.
DR   KEGG; cal:CAALFM_CR04420CA; -.
DR   CGD; CAL0000175612; RBR2.
DR   VEuPathDB; FungiDB:CR_04420C_A; -.
DR   eggNOG; ENOG502RZ9R; Eukaryota.
DR   HOGENOM; CLU_129392_0_0_1; -.
DR   InParanoid; Q5A6M2; -.
DR   OMA; ATELPWY; -.
DR   OrthoDB; 1643601at2759; -.
DR   PRO; PR:Q5A6M2; -.
DR   Proteomes; UP000000559; Chromosome R.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000992; SRP1_TIP1.
DR   Pfam; PF00660; SRP1_TIP1; 1.
PE   1: Evidence at protein level;
KW   Cell wall; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein; Membrane;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..143
FT                   /note="Repressed By RIM101 protein 2"
FT                   /id="PRO_0000424781"
FT   PROPEP          144..168
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000424782"
FT   REGION          111..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        111..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   LIPID           143
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   168 AA;  16830 MW;  8C8A673C49957E75 CRC64;
     MRFAFTTVSL SLLLSSLVAS DAASSDVQFL TALVGDYQDH KTDYIKFFAT AKDVPGDLST
     LATKVLTYTD DSYTTLLNDD SLNVSNLEAY ATSLPWYSRI QADAGGKGSA SGSASGSGSA
     KSTASAEKSS GSSASASSTA GGSSSKGGVS ELVAPVGAVV GALAVALM
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024