RAX2_YEAST
ID RAX2_YEAST Reviewed; 1220 AA.
AC Q12465; D6VY84;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Bud site selection protein RAX2;
DE AltName: Full=Revert to axial protein 2;
DE Flags: Precursor;
GN Name=RAX2; OrderedLocusNames=YLR084C; ORFNames=L2389, L9449.12;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11110666; DOI=10.1126/science.290.5498.1975;
RA Chen T., Hiroko T., Chaudhuri A., Inose F., Lord M., Tanaka S., Chant J.,
RA Fujita A.;
RT "Multigenerational cortical inheritance of the Rax2 protein in orienting
RT polarity and division in yeast.";
RL Science 290:1975-1978(2000).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [5]
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 [6]
RP INTERACTION WITH RAX1, SUBCELLULAR LOCATION, AND GLYCOSYLATION.
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).
CC -!- FUNCTION: Required for the maintenance of the bipolar budding pattern.
CC Involved in selecting bud sites at both the distal and proximal poles
CC of daughter cells as well as near previously used division sites on
CC mother cells. {ECO:0000269|PubMed:11110666}.
CC -!- SUBUNIT: Interacts with RAX1. {ECO:0000269|PubMed:15356260}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Bud neck. Bud tip. Note=Before cytokinesis, RAX2 concentrates
CC as a ring at the mother-bud neck and to the tip of the bud. The RAX2
CC ring splits at cytokinesis, endowing each progeny cell with a RAX2 ring
CC and additional RAX2 localization at the distal bud pole of the newborn
CC daughter cell. The rings persist at the cell cortex for several
CC generations, giving rise to cells decorated by multiple rings.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:15356260}.
CC -!- MISCELLANEOUS: Present with 3670 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U53880; AAB67588.1; -; Genomic_DNA.
DR EMBL; Z73256; CAA97644.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09400.1; -; Genomic_DNA.
DR PIR; S64916; S64916.
DR RefSeq; NP_013185.1; NM_001181971.1.
DR AlphaFoldDB; Q12465; -.
DR SMR; Q12465; -.
DR BioGRID; 31357; 86.
DR IntAct; Q12465; 3.
DR MINT; Q12465; -.
DR STRING; 4932.YLR084C; -.
DR iPTMnet; Q12465; -.
DR MaxQB; Q12465; -.
DR PaxDb; Q12465; -.
DR PRIDE; Q12465; -.
DR EnsemblFungi; YLR084C_mRNA; YLR084C; YLR084C.
DR GeneID; 850773; -.
DR KEGG; sce:YLR084C; -.
DR SGD; S000004074; RAX2.
DR VEuPathDB; FungiDB:YLR084C; -.
DR eggNOG; ENOG502QQZD; Eukaryota.
DR HOGENOM; CLU_005863_0_0_1; -.
DR InParanoid; Q12465; -.
DR OMA; NMYTPGC; -.
DR BioCyc; YEAST:G3O-32235-MON; -.
DR PRO; PR:Q12465; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12465; 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:0005783; C:endoplasmic reticulum; HDA:SGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:1902929; C:plasma membrane of growing cell tip; 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:0000282; P:cellular bud site selection; IBA:GO_Central.
DR GO; GO:0061161; P:positive regulation of establishment of bipolar cell polarity regulating cell shape; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IMP:SGD.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR SUPFAM; SSF50998; SSF50998; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..1220
FT /note="Bud site selection protein RAX2"
FT /id="PRO_0000262737"
FT TOPO_DOM 21..1162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1163..1183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1184..1220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1129..1151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 45
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 69
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 171
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 187
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 333
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 365
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 516
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 613
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 620
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 677
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 705
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 713
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 721
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 731
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 758
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 792
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 848
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 861
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 884
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 890
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 908
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 923
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 942
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 980
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 983
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1011
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1024
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1031
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1060
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1071
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1098
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1220 AA; 133959 MW; C8D83EA5C903ADE8 CRC64;
MFVHRLWTLA FPFLVEISKA SQLENIKSLL DIEDNVLPNL NISQNNSNAV QILGGVDALS
FYEYTGQQNF TKEIGPETSS HGLVYYSNNT YIQLEDASDD TRIDKITPFG VDSFILSGSG
TINNISVGNQ ILYNLSTLSM TPIFNQSLGA VQAVLADNSS IYFGGNFSYN NGSMTGYSAL
IWDSISNTTQ LLPFGGFGEN SSVNSIVKLN NDNILFAGQF YTLDDPSALI SSSNNGTNST
SSLNATTLEL GQRIPLRYAS WDSQGSTTFA SDSLVCPNTN EDAWLYPDTS GSLVCNLPYE
VSPTKIRLYN SQRSDSEISV FQILTDPSSS IMNLTYLDPL SGELKNCGEF CPLYSRATLL
SASQNVSSSM DMITFIDNNK TDVKWTSDFQ DFAFVNELPV SSLKFVALNS YGGSVGLSGL
ELYQDTFSTY ANDSLNEYGC SALTNDSSSS TLSSNDWYNG LTGESYIAAK YVPDQNEPIP
RVKFYPNIIH PGHYTINMYT PGCLQDNTCS ARGIVNVTMW NQQNNTIMKT YLIYQNNDNL
KYDQIYSGYL DFSPEIVLEY VSGIYTTNTA TVVVADQVNV ITVSLDAFNT LSDSSNAKKE
TLLNGILQYQ KSNFTSTRLN ETKVGNTTLN LFPVKNYPKN SSLYADIYDN KLVIGGVSNR
ISIVDLNDDF EVTSSKNQTI QGDVHGITKT NQGLLIFGDI LSSNNQSAVF LFNGSFENVF
NQSRTVNSAL NISLANNDFI VLDNDYVVNA SSNALIRNSS SFSLSLWAAG NNGDGDVLFS
GAVSHMQYGN LNGSVRFLNE NEIEPLNLEG GIVPYLGAYL NESATAYAYE VDSLNKIYFS
NEVYPSWNWS SGITQMLYAD NQTLLAVSAG SSTTAELSIF DLRNLTMIAN ETLGSNARIN
ALVNFEKNCS MLVGGDFQMT EPNCTGLCLY NYESKTWSTF LNNTIFGEIT QLSFTNSSEL
IISGLFETKE YQSIRLGSFN LTNSTMIPLL SGSEGKLNSF TVTEDSIVAW NDTSLFIYRN
QEWNITSLPG NASSISSVSA IYTDIESNTL NKRGINNVNN GSILLLNGNF NISQYGYLQS
LLFDFQKWTP YFISETTNTS NYNPIIFINR DVSTEFNSQS PLANVNITVT SPQSTSSQPP
SSSASSESKS KSKKKKIGRG FVVLIGLALA LGTVSVLGIA GVILAYVFKD PEGDYKPIKP
RIDENEMLDT VPPEKLMKFV
