RAX1_YEAST
ID RAX1_YEAST Reviewed; 435 AA.
AC Q08760; D6W300;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Bud site selection protein RAX1;
DE AltName: Full=Revert to axial protein 1;
GN Name=RAX1; OrderedLocusNames=YOR301W;
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].
RX PubMed=9153758;
RX DOI=10.1002/(sici)1097-0061(199704)13:5<479::aid-yea104>3.0.co;2-g;
RA Poirey R., Cziepluch C., Tobiasch E., Pujol A., Kordes E., Jauniaux J.-C.;
RT "Sequence and analysis of a 36.2 kb fragment from the right arm of yeast
RT chromosome XV reveals 19 open reading frames including SNF2 (5' end), CPA1,
RT SLY41, a putative transport ATPase, a putative ribosomal protein and an
RT SNF2 homologue.";
RL Yeast 13:479-482(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14980713; DOI=10.1016/j.gene.2003.11.021;
RA Fujita A., Lord M., Hiroko T., Hiroko F., Chen T., Oka C., Misumi Y.,
RA Chant J.;
RT "Rax1, a protein required for the establishment of the bipolar budding
RT pattern in yeast.";
RL Gene 327:161-169(2004).
RN [5]
RP INTERACTION WITH BUD8; BUD9 AND RAX2, AND SUBCELLULAR LOCATION.
RX PubMed=15356260; DOI=10.1091/mbc.e04-07-0600;
RA Kang P.J., Angerman E., Nakashima K., Pringle J.R., Park H.-O.;
RT "Interactions among Rax1p, Rax2p, Bud8p, and Bud9p in marking cortical
RT sites for bipolar bud-site selection in yeast.";
RL Mol. Biol. Cell 15:5145-5157(2004).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=16847258; DOI=10.1073/pnas.0604075103;
RA Kim H., Melen K., Oesterberg M., von Heijne G.;
RT "A global topology map of the Saccharomyces cerevisiae membrane proteome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
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 IDENTIFICATION BY 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: Required for the establishment of the bipolar budding
CC pattern. Involved in selecting bud sites at both the distal and
CC proximal poles of daughter cells as well as near previously used
CC division sites on mother cells. Has a role in the localization of BUD8,
CC the distal bipolar budding landmark, and of BUD9, the proximal pole
CC landmark. {ECO:0000269|PubMed:14980713}.
CC -!- SUBUNIT: Interacts with BUD8, BUD9 and RAX2.
CC {ECO:0000269|PubMed:15356260}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Bud
CC neck. Bud tip. Note=Before cytokinesis, RAX1 concentrates as a ring at
CC the mother-bud neck and to the tip of the bud. The RAX1 ring splits at
CC cytokinesis, endowing each progeny cell with a RAX1 ring and additional
CC RAX1 localization at the distal bud pole of the newborn daughter cell.
CC The rings persist at the cell cortex for several generations, giving
CC rise to cells decorated by multiple rings.
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DR EMBL; Z75209; CAA99619.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA11066.1; -; Genomic_DNA.
DR PIR; S67205; S67205.
DR RefSeq; NP_014945.3; NM_001183720.3.
DR AlphaFoldDB; Q08760; -.
DR BioGRID; 34689; 82.
DR IntAct; Q08760; 4.
DR MINT; Q08760; -.
DR STRING; 4932.YOR301W; -.
DR iPTMnet; Q08760; -.
DR MaxQB; Q08760; -.
DR PaxDb; Q08760; -.
DR PRIDE; Q08760; -.
DR EnsemblFungi; YOR301W_mRNA; YOR301W; YOR301W.
DR GeneID; 854477; -.
DR KEGG; sce:YOR301W; -.
DR SGD; S000005827; RAX1.
DR VEuPathDB; FungiDB:YOR301W; -.
DR eggNOG; ENOG502QRI8; Eukaryota.
DR GeneTree; ENSGT00390000015077; -.
DR HOGENOM; CLU_029881_1_1_1; -.
DR InParanoid; Q08760; -.
DR OMA; VYSWFGV; -.
DR BioCyc; YEAST:G3O-33785-MON; -.
DR Reactome; R-SCE-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q08760; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q08760; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005621; C:cellular bud scar; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR Gene3D; 1.10.167.10; -; 1.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..435
FT /note="Bud site selection protein RAX1"
FT /id="PRO_0000262736"
FT TOPO_DOM 1..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..325
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..435
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 126..257
FT /note="RGS"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
SQ SEQUENCE 435 AA; 50161 MW; BBF40C6635ACAEC0 CRC64;
MKEELSKVSS MQNFEMIQRE RLPTLYEVLI QRTSQPVDLW TFYTFLSQFP YAINYLDFWV
DLMTHTRLCK NYIELVRKSL INFPQEQQQN GSTSTATFDL LNALIEEGHL DPEAPDKLLE
NSGPDVPFSP KLNELLGDWK HQSGIGQEAL RNEDVALIVD EIMKRRSQQD GKPQITTKQL
LHSAVGLCNT YLVSPEQSER YLSNIPMETR NRIIESVQIE RKYDIEIFDD LKNLTYQFLE
MDCFPKFLSR VALHNIHDEI SDWRFHSVGV TNEKSNRSRG QTHISRSPFS NHTSISRIGF
GLLWLGIGFW IGYVLIFLAY SRAIRVVTVV PFTLGCYCIV CGMYQVDIVY SWFGVTQRLL
HRHKNAGNDE GDASSDTDHV PMILAVFGGR RRLTRIEHPF TRQLLRKRGL WCLLLVVGAT
AAFTVIFSCV PGRRV
