RCR1_YEAST
ID RCR1_YEAST Reviewed; 213 AA.
AC P38212; D6VQ06;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Protein RCR1;
DE AltName: Full=Resistance to Congo red protein 1;
GN Name=RCR1; OrderedLocusNames=YBR005W; ORFNames=YBR0111;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=15590673; DOI=10.1074/jbc.m409428200;
RA Imai K., Noda Y., Adachi H., Yoda K.;
RT "A novel endoplasmic reticulum membrane protein Rcr1 regulates chitin
RT deposition in the cell wall of Saccharomyces cerevisiae.";
RL J. Biol. Chem. 280:8275-8284(2005).
RN [5]
RP INTERACTION WITH PMT4 AND RSP5, AND MUTAGENESIS OF 82-PRO-PRO-83; PRO-105;
RP LYS-130 AND LYS-208.
RX PubMed=17213653; DOI=10.1271/bbb.60446;
RA Imai K., Noda Y., Adachi H., Yoda K.;
RT "Peculiar protein-protein interactions of the novel endoplasmic reticulum
RT membrane protein Rcr1 and ubiquitin ligase Rsp5.";
RL Biosci. Biotechnol. Biochem. 71:249-252(2007).
CC -!- FUNCTION: Regulates chitin deposition in the cell wall.
CC {ECO:0000269|PubMed:15590673}.
CC -!- SUBUNIT: Interacts with PMT4 and WW domain of RSP5.
CC {ECO:0000269|PubMed:17213653}.
CC -!- INTERACTION:
CC P38212; P39940: RSP5; NbExp=3; IntAct=EBI-21381, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15590673}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:15590673}.
CC -!- DOMAIN: Transmembrane domain is required, and the cytoplasmic region
CC conserved between RCR1 and RCR2 is also essential, to endow resistance
CC to Congo red.
CC -!- DOMAIN: The PY motif is recognized directly by the WW domains of RSP5.
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DR EMBL; Z35874; CAA84941.1; -; Genomic_DNA.
DR EMBL; AY692680; AAT92699.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07126.1; -; Genomic_DNA.
DR PIR; S45857; S45857.
DR RefSeq; NP_009559.1; NM_001178353.1.
DR AlphaFoldDB; P38212; -.
DR SMR; P38212; -.
DR BioGRID; 32706; 78.
DR IntAct; P38212; 2.
DR STRING; 4932.YBR005W; -.
DR iPTMnet; P38212; -.
DR PaxDb; P38212; -.
DR PRIDE; P38212; -.
DR EnsemblFungi; YBR005W_mRNA; YBR005W; YBR005W.
DR GeneID; 852290; -.
DR KEGG; sce:YBR005W; -.
DR SGD; S000000209; RCR1.
DR VEuPathDB; FungiDB:YBR005W; -.
DR eggNOG; ENOG502S7RD; Eukaryota.
DR GeneTree; ENSGT00940000176721; -.
DR HOGENOM; CLU_078289_2_1_1; -.
DR InParanoid; P38212; -.
DR OMA; SLDTDYG; -.
DR BioCyc; YEAST:G3O-28993-MON; -.
DR PRO; PR:P38212; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38212; protein.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006033; P:chitin localization; IMP:SGD.
DR GO; GO:0016192; P:vesicle-mediated transport; IGI:SGD.
DR InterPro; IPR020999; Chitin_synth_reg_RCR.
DR PANTHER; PTHR28187; PTHR28187; 1.
DR Pfam; PF12273; RCR; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Endoplasmic reticulum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..213
FT /note="Protein RCR1"
FT /id="PRO_0000202466"
FT TOPO_DOM 1..39
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..213
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 190..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 104..107
FT /note="PY motif"
FT COMPBIAS 190..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 82..83
FT /note="PP->QA: Reduced interaction with WW domain of RSP5.
FT No interaction with WW domain of RSP5; when in association
FT with A-105."
FT /evidence="ECO:0000269|PubMed:17213653"
FT MUTAGEN 105
FT /note="P->A: Reduced interaction with WW domain of RSP5. No
FT interaction with WW domain of RSP5; when in association
FT with 82-QA-83."
FT /evidence="ECO:0000269|PubMed:17213653"
FT MUTAGEN 130
FT /note="K->A: No effect in conferring Congo red resistance;
FT when associated with A-208."
FT /evidence="ECO:0000269|PubMed:17213653"
FT MUTAGEN 208
FT /note="K->A: No effect in conferring Congo red resistance;
FT when associated with A-130."
FT /evidence="ECO:0000269|PubMed:17213653"
SQ SEQUENCE 213 AA; 23887 MW; 0784FB182C16F1B0 CRC64;
MGLISYENEA INEVKKADNH HVSKFVTSYY GPSSSSWQSG IWILFVLFVA AVILIILFTF
VANRRRRRMG RAPIRGTAWL TPPSYRQSQQ QYTGTVQQRT DDYVPEYTET ANEHDLGYYD
QRGEFHPNDK AAYVAPPPLV QECSSESVNS LERPPAAVVH QANSLDTDYG LTRPSNGRVP
AVSDTVEQLE RLPGGTTTQE INPPERAKVN ARS
