RCY1_YEAST
ID RCY1_YEAST Reviewed; 840 AA.
AC P39531; D6VVZ0; P39530; P87193;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 4.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Recyclin-1;
GN Name=RCY1; OrderedLocusNames=YJL204C; ORFNames=J0318, J0320;
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 [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7754713; DOI=10.1002/yea.320100912;
RA Purnelle B., Coster F., Goffeau A.;
RT "The sequence of a 36 kb segment on the left arm of yeast chromosome X
RT identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6,
RT CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two
RT homologues to chromosome III genes.";
RL Yeast 10:1235-1249(1994).
RN [2]
RP SEQUENCE REVISION.
RA Purnelle B.;
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [4]
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 [5]
RP FUNCTION.
RX PubMed=10769031; DOI=10.1083/jcb.149.2.397;
RA Wiederkehr A., Avaro S., Prescianotto-Baschong C., Haguenauer-Tsapis R.,
RA Riezman H.;
RT "The F-box protein Rcy1p is involved in endocytic membrane traffic and
RT recycling out of an early endosome in Saccharomyces cerevisiae.";
RL J. Cell Biol. 149:397-410(2000).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SKP1.
RX PubMed=11287615; DOI=10.1128/mcb.21.9.3105-3117.2001;
RA Galan J.M., Wiederkehr A., Seol J.H., Haguenauer-Tsapis R., Deshaies R.J.,
RA Riezman H., Peter M.;
RT "Skp1p and the F-box protein Rcy1p form a non-SCF complex involved in
RT recycling of the SNARE Snc1p in yeast.";
RL Mol. Cell. Biol. 21:3105-3117(2001).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-409, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Involved in recycling plasma membrane proteins internalized
CC by endocytosis. Required for recycling of the v-SNARE SNC1.
CC {ECO:0000269|PubMed:10769031, ECO:0000269|PubMed:11287615}.
CC -!- SUBUNIT: Interacts with SKP1. {ECO:0000269|PubMed:11287615}.
CC -!- INTERACTION:
CC P39531; P52286: SKP1; NbExp=4; IntAct=EBI-26224, EBI-4090;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11287615}. Bud neck
CC {ECO:0000269|PubMed:11287615}. Cell tip {ECO:0000269|PubMed:11287615}.
CC Note=In unpolarized G1 cells this protein is found in patches in the
CC cytoplasm, while after bud emergence it is concentrated in nascent buds
CC and at the mother-bud neck. Accumulates at the shmoo tips of cells
CC treated with pheromone. Localization depends on an intact actin
CC cytoskeleton and a functional secretory pathway.
CC -!- MISCELLANEOUS: Present with 2700 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; X77688; CAA54753.1; -; Genomic_DNA.
DR EMBL; Z49479; CAA89499.1; -; Genomic_DNA.
DR EMBL; Z49480; CAA89501.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08606.1; -; Genomic_DNA.
DR PIR; S77615; S77615.
DR RefSeq; NP_012331.1; NM_001181637.1.
DR AlphaFoldDB; P39531; -.
DR SMR; P39531; -.
DR BioGRID; 33554; 224.
DR DIP; DIP-7247N; -.
DR IntAct; P39531; 1.
DR STRING; 4932.YJL204C; -.
DR iPTMnet; P39531; -.
DR MaxQB; P39531; -.
DR PaxDb; P39531; -.
DR PRIDE; P39531; -.
DR TopDownProteomics; P39531; -.
DR EnsemblFungi; YJL204C_mRNA; YJL204C; YJL204C.
DR GeneID; 853226; -.
DR KEGG; sce:YJL204C; -.
DR SGD; S000003740; RCY1.
DR VEuPathDB; FungiDB:YJL204C; -.
DR eggNOG; KOG3745; Eukaryota.
DR GeneTree; ENSGT00390000012837; -.
DR HOGENOM; CLU_003875_1_1_1; -.
DR InParanoid; P39531; -.
DR OMA; SNHCFLL; -.
DR BioCyc; YEAST:G3O-31632-MON; -.
DR PRO; PR:P39531; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P39531; protein.
DR GO; GO:0051286; C:cell tip; IEA:UniProtKB-SubCell.
DR GO; GO:0005933; C:cellular bud; HDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005768; C:endosome; IDA:SGD.
DR GO; GO:0000145; C:exocyst; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0000149; F:SNARE binding; IMP:SGD.
DR GO; GO:0034498; P:early endosome to Golgi transport; IMP:SGD.
DR GO; GO:0032456; P:endocytic recycling; IMP:SGD.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0006893; P:Golgi to plasma membrane transport; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR009976; Sec10-like.
DR PANTHER; PTHR12100; PTHR12100; 1.
DR Pfam; PF07393; Sec10; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..840
FT /note="Recyclin-1"
FT /id="PRO_0000119953"
FT DOMAIN 1..48
FT /note="F-box"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 840 AA; 97471 MW; E8CDB82E00490886 CRC64;
MDDLLKVPEI VTNIASYLST VDYLSFQQVN KRVYAIINGK NDSKYWSLKL TRMGLQQVHS
NEEEEITLLD ENDNQNSLRI FEIYKSFTAQ NSKKIFVKFY RCYNSYARKL YNNNLANFFP
TSYSNDPLKQ TRILNFIKKY NFSNKNDIET FTRIETNFNI LREIFINSVL KESELNYQSN
NLAAVARFMK ILLISNEESN AIEFFKSKAD LPPSLTVLPS NDELFWAEQP REEDSGGSTV
IFNSKNLDTF LNQLRDFLNE KIKLADILFK DEFPVILQFI ESFIQDILLD ILNNILLSYS
EFLKENGKDS KANYECVPEL YFTFIKKFDT ELNDSVNAGA NFRKVVRDLL NLYLEPFVVN
YMNQTTRVFE SLINSQLANY DTQVQDKQRE QNAKIYNTLK DQTDASSASN NELPNDLSII
TETSKTVPEA DSKPSTIHQS VHSTDISNDK LDFLSSFTKI FKFSNNENQR LKQQLQLAYN
LNLISNNLQN IKSLISLDLC YKILQETSEK TDQIYKFHTI ESLLPLIKLR CQEIFKILIT
QLNKNHVKPA FEKAILLLQK YNPNEIEQIE IKFNSLSPAN TQVEPLVQFT ELINIGDIIL
QMISIFYKNE LIPKKIIDKN KDFLNDVIQL KKNFETSIDD FVAEGLNIGI NKLMDEISFV
FKTLQLPDDY NPPPPSRNSP IRDIKPTKCA IRVVELLSNH CFLLTGATDK GTIDVYQQEI
GERFFNEIVK HLKKCFISTE GAIWLICDLN YFYDFIANKL KQKNVVPYFV GLKSIGQLYI
ISGKDSKELG KLISDLGKFN GIFTQEEIYE FVQRRSDWVR VRKDVEKVMY GLGIRDCCIM
