AXL2_YEAST
ID AXL2_YEAST Reviewed; 823 AA.
AC P38928; D6VVE6; Q96VY8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Axial budding pattern protein 2;
DE AltName: Full=Bud site selection protein 10;
DE AltName: Full=Suppressor of RHO3 protein 4;
DE Flags: Precursor;
GN Name=AXL2; Synonyms=BUD10, SRO4; OrderedLocusNames=YIL140W;
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], FUNCTION, GLYCOSYLATION, SUBCELLULAR
RP LOCATION, AND TOPOLOGY.
RX PubMed=8846915; DOI=10.1101/gad.10.7.777;
RA Roemer T., Madden K., Chang J., Snyder M.;
RT "Selection of axial growth sites in yeast requires Axl2p, a novel plasma
RT membrane glycoprotein.";
RL Genes Dev. 10:777-793(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8805277; DOI=10.1016/s0960-9822(02)00543-2;
RA Halme A., Michelitch M., Mitchell E.L., Chant J.;
RT "Bud10p directs axial cell polarization in budding yeast and resembles a
RT transmembrane receptor.";
RL Curr. Biol. 6:570-579(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-775.
RA Mathew P.W.;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 80-823.
RX PubMed=7871890; DOI=10.1002/yea.320101115;
RA Torpey L.E., Gibbs P.E.M., Nelson J., Lawrence C.W.;
RT "Cloning and sequence of REV7, a gene whose function is required for DNA
RT damage-induced mutagenesis in Saccharomyces cerevisiae.";
RL Yeast 10:1503-1509(1994).
RN [7]
RP FUNCTION.
RX PubMed=1448099; DOI=10.1128/mcb.12.12.5690-5699.1992;
RA Matsui Y., Toh-E A.;
RT "Yeast RHO3 and RHO4 ras superfamily genes are necessary for bud growth,
RT and their defect is suppressed by a high dose of bud formation genes CDC42
RT and BEM1.";
RL Mol. Cell. Biol. 12:5690-5699(1992).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=9732282; DOI=10.1083/jcb.142.5.1209;
RA Powers J., Barlowe C.;
RT "Transport of axl2p depends on erv14p, an ER-vesicle protein related to the
RT Drosophila cornichon gene product.";
RL J. Cell Biol. 142:1209-1222(1998).
RN [9]
RP GLYCOSYLATION BY PMT4, AND SUBCELLULAR LOCATION.
RX PubMed=10366591; DOI=10.1083/jcb.145.6.1177;
RA Sanders S.L., Gentzsch M., Tanner W., Herskowitz I.;
RT "O-glycosylation of Axl2/Bud10p by Pmt4p is required for its stability,
RT localization, and function in daughter cells.";
RL J. Cell Biol. 145:1177-1188(1999).
RN [10]
RP INDUCTION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11134078; DOI=10.1083/jcb.151.7.1501;
RA Lord M., Yang M.C., Mischke M., Chant J.;
RT "Cell cycle programs of gene expression control morphogenetic protein
RT localization.";
RL J. Cell Biol. 151:1501-1512(2000).
RN [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11065362; DOI=10.1099/00221287-146-11-2833;
RA Freedman T., Porter A., Haarer B.;
RT "Mutational and hyperexpression-induced disruption of bipolar budding in
RT yeast.";
RL Microbiology 146:2833-2843(2000).
RN [12]
RP FUNCTION, AND INTERACTION WITH BUD5.
RX PubMed=11313501; DOI=10.1126/science.1060360;
RA Kang P.J., Sanson A., Lee B., Park H.-O.;
RT "A GDP/GTP exchange factor involved in linking a spatial landmark to cell
RT polarity.";
RL Science 292:1376-1378(2001).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12221111; DOI=10.1091/mbc.e02-03-0151;
RA Cullen P.J., Sprague G.F. Jr.;
RT "The roles of bud-site-selection proteins during haploid invasive growth in
RT yeast.";
RL Mol. Biol. Cell 13:2990-3004(2002).
RN [14]
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 [15]
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 [16]
RP SUBCELLULAR LOCATION.
RX PubMed=15282802; DOI=10.1002/yea.1133;
RA Sundin B.A., Chiu C.-H., Riffle M., Davis T.N., Muller E.G.D.;
RT "Localization of proteins that are coordinately expressed with Cln2 during
RT the cell cycle.";
RL Yeast 21:793-800(2004).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-673 AND SER-676, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [18]
RP INTERACTION WITH BEM1; BUD3; BUD4; CDC24 AND CDC42, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=17460121; DOI=10.1091/mbc.e06-09-0822;
RA Gao X.D., Sperber L.M., Kane S.A., Tong Z., Tong A.H., Boone C., Bi E.;
RT "Sequential and distinct roles of the cadherin domain-containing protein
RT Axl2p in cell polarization in yeast cell cycle.";
RL Mol. Biol. Cell 18:2542-2560(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; SER-673 AND SER-676, AND
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 haploid cells axial budding pattern. Acts as an
CC anchor to help direct new growth components and/or polarity
CC establishment components like the BUD5 GTP/GDP exchange factor to
CC localize at the cortical axial budding site. Regulates septin
CC organization in late G1 independently of its role in polarity-axis
CC determination. {ECO:0000269|PubMed:11065362,
CC ECO:0000269|PubMed:11134078, ECO:0000269|PubMed:11313501,
CC ECO:0000269|PubMed:12221111, ECO:0000269|PubMed:1448099,
CC ECO:0000269|PubMed:17460121, ECO:0000269|PubMed:8805277,
CC ECO:0000269|PubMed:8846915}.
CC -!- SUBUNIT: Interacts with BEM1, BUD3, BUD4, BUD5, CDC24 and CDC42.
CC {ECO:0000269|PubMed:11313501, ECO:0000269|PubMed:17460121}.
CC -!- INTERACTION:
CC P38928; P25558: BUD3; NbExp=2; IntAct=EBI-3397, EBI-3840;
CC P38928; P47136: BUD4; NbExp=2; IntAct=EBI-3397, EBI-3848;
CC P38928; P25300: BUD5; NbExp=2; IntAct=EBI-3397, EBI-3853;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10366591,
CC ECO:0000269|PubMed:11065362, ECO:0000269|PubMed:11134078,
CC ECO:0000269|PubMed:12221111, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:17460121,
CC ECO:0000269|PubMed:8805277, ECO:0000269|PubMed:8846915,
CC ECO:0000269|PubMed:9732282}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:10366591, ECO:0000269|PubMed:11065362,
CC ECO:0000269|PubMed:11134078, ECO:0000269|PubMed:12221111,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15282802,
CC ECO:0000269|PubMed:17460121, ECO:0000269|PubMed:8805277,
CC ECO:0000269|PubMed:8846915, ECO:0000269|PubMed:9732282}. Note=In small
CC buds, localizes to incipient bud sites, emerging buds and to the bud
CC periphery. In large buds, localizes as a ring at the bud neck. Requires
CC ERV14 to be efficiently delivered to the cell surface. Recruitment to
CC the bud neck after S/G2 phase of the cell cycle depends on BUD3 and
CC BUD4.
CC -!- INDUCTION: Expression shows a peak at the start of the cell cycle just
CC before bud emergence in late G1 phase. {ECO:0000269|PubMed:11134078}.
CC -!- PTM: O-glycosylated by PMT4 and N-glycosylated. O-glycosylation
CC increases activity in daughter cells by enhancing stability and
CC promoting localization to the plasma membrane. May also be O-
CC glycosylated by PMT1 and PMT2. {ECO:0000269|PubMed:10366591,
CC ECO:0000269|PubMed:8846915}.
CC -!- MISCELLANEOUS: Present with 396 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- CAUTION: Ref.5 refers to this gene as REV7. REV7 is however the
CC adjacent gene. {ECO:0000305}.
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DR EMBL; U49845; AAA98666.1; -; Genomic_DNA.
DR EMBL; Z38059; CAA86138.1; -; Genomic_DNA.
DR EMBL; AF395906; AAK83884.1; -; Genomic_DNA.
DR EMBL; U07228; AAA67919.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08412.1; -; Genomic_DNA.
DR PIR; S48394; S48394.
DR RefSeq; NP_012126.1; NM_001179488.1.
DR AlphaFoldDB; P38928; -.
DR SMR; P38928; -.
DR BioGRID; 34851; 140.
DR DIP; DIP-8163N; -.
DR IntAct; P38928; 9.
DR MINT; P38928; -.
DR STRING; 4932.YIL140W; -.
DR iPTMnet; P38928; -.
DR MaxQB; P38928; -.
DR PaxDb; P38928; -.
DR PRIDE; P38928; -.
DR EnsemblFungi; YIL140W_mRNA; YIL140W; YIL140W.
DR GeneID; 854666; -.
DR KEGG; sce:YIL140W; -.
DR SGD; S000001402; AXL2.
DR VEuPathDB; FungiDB:YIL140W; -.
DR eggNOG; ENOG502QURR; Eukaryota.
DR HOGENOM; CLU_017550_1_0_1; -.
DR InParanoid; P38928; -.
DR OMA; ATRGEWF; -.
DR BioCyc; YEAST:G3O-31391-MON; -.
DR PRO; PR:P38928; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P38928; protein.
DR GO; GO:0032153; C:cell division site; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0000144; C:cellular bud neck septin ring; IDA:SGD.
DR GO; GO:0000324; C:fungal-type vacuole; HDA:SGD.
DR GO; GO:0000131; C:incipient cellular bud site; IDA:SGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR006644; Cadg.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014805; SKG6/AXL2_alpha-helix_TM.
DR Pfam; PF08693; SKG6; 1.
DR SMART; SM00736; CADG; 4.
DR SUPFAM; SSF49313; SSF49313; 3.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..823
FT /note="Axial budding pattern protein 2"
FT /id="PRO_0000020773"
FT TOPO_DOM 23..508
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..823
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 447..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..771
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..627
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 50
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 260
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 324
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 389
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 495
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 823 AA; 90783 MW; 350D79758BF30771 CRC64;
MTQLQISLLL TATISLLHLV VATPYEAYPI GKQYPPVARV NESFTFQISN DTYKSSVDKT
AQITYNCFDL PSWLSFDSSS RTFSGEPSSD LLSDANTTLY FNVILEGTDS ADSTSLNNTY
QFVVTNRPSI SLSSDFNLLA LLKNYGYTNG KNALKLDPNE VFNVTFDRSM FTNEESIVSY
YGRSQLYNAP LPNWLFFDSG ELKFTGTAPV INSAIAPETS YSFVIIATDI EGFSAVEVEF
ELVIGAHQLT TSIQNSLIIN VTDTGNVSYD LPLNYVYLDD DPISSDKLGS INLLDAPDWV
ALDNATISGS VPDELLGKNS NPANFSVSIY DTYGDVIYFN FEVVSTTDLF AISSLPNINA
TRGEWFSYYF LPSQFTDYVN TNVSLEFTNS SQDHDWVKFQ SSNLTLAGEV PKNFDKLSLG
LKANQGSQSQ ELYFNIIGMD SKITHSNHSA NATSTRSSHH STSTSSYTSS TYTAKISSTS
AAATSSAPAA LPAANKTSSH NKKAVAIACG VAIPLGVILV ALICFLIFWR RRRENPDDEN
LPHAISGPDL NNPANKPNQE NATPLNNPFD DDASSYDDTS IARRLAALNT LKLDNHSATE
SDISSVDEKR DSLSGMNTYN DQFQSQSKEE LLAKPPVQPP ESPFFDPQNR SSSVYMDSEP
AVNKSWRYTG NLSPVSDIVR DSYGSQKTVD TEKLFDLEAP EKEKRTSRDV TMSSLDPWNS
NISPSPVRKS VTPSPYNVTK HRNRHLQNIQ DSQSGKNGIT PTTMSTSSSD DFVPVKDGEN
FCWVHSMEPD RRPSKKRLVD FSNKSNVNVG QVKDIHGRIP EML
