AXL1_YEAST
ID AXL1_YEAST Reviewed; 1208 AA.
AC P40851; D6W4C1;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Putative protease AXL1;
DE EC=3.4.24.-;
GN Name=AXL1; OrderedLocusNames=YPR122W; ORFNames=P9642.4;
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 44774 / DBY747;
RX PubMed=7990931; DOI=10.1038/372567a0;
RA Fujita A., Oka C., Arikawa Y., Katagai T., Tonouchi A., Kuhara S.,
RA Misumi Y.;
RT "A yeast gene necessary for bud-site selection encodes a protein similar to
RT insulin-degrading enzymes.";
RL Nature 372:567-570(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 INTERACTION WITH BUD5, AND SUBCELLULAR LOCATION.
RX PubMed=12176366; DOI=10.1016/s0960-9822(02)01042-4;
RA Lord M., Inose F., Hiroko T., Hata T., Fujita A., Chant J.;
RT "Subcellular localization of Axl1, the cell type-specific regulator of
RT polarity.";
RL Curr. Biol. 12:1347-1352(2002).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262, 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).
CC -!- FUNCTION: Probable protease. Involved in axial budding.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Interacts with BUD5. {ECO:0000269|PubMed:12176366}.
CC -!- SUBCELLULAR LOCATION: Bud neck {ECO:0000269|PubMed:12176366}.
CC Note=Mother-bud neck and division site remnants of haploid cells.
CC -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family. {ECO:0000305}.
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DR EMBL; D17787; BAA04613.1; -; Genomic_DNA.
DR EMBL; U40828; AAB68063.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11537.1; -; Genomic_DNA.
DR PIR; S69015; S69015.
DR RefSeq; NP_015447.1; NM_001184219.1.
DR AlphaFoldDB; P40851; -.
DR SMR; P40851; -.
DR BioGRID; 36291; 194.
DR DIP; DIP-4872N; -.
DR IntAct; P40851; 3.
DR STRING; 4932.YPR122W; -.
DR MEROPS; M16.007; -.
DR iPTMnet; P40851; -.
DR MaxQB; P40851; -.
DR PaxDb; P40851; -.
DR PRIDE; P40851; -.
DR EnsemblFungi; YPR122W_mRNA; YPR122W; YPR122W.
DR GeneID; 856240; -.
DR KEGG; sce:YPR122W; -.
DR SGD; S000006326; AXL1.
DR VEuPathDB; FungiDB:YPR122W; -.
DR eggNOG; KOG0959; Eukaryota.
DR GeneTree; ENSGT00940000175681; -.
DR HOGENOM; CLU_008088_0_0_1; -.
DR InParanoid; P40851; -.
DR OMA; TGSHNDP; -.
DR BioCyc; YEAST:G3O-34261-MON; -.
DR PRO; PR:P40851; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; P40851; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0043332; C:mating projection tip; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IMP:SGD.
DR GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR GO; GO:0000755; P:cytogamy; IMP:SGD.
DR GO; GO:0071432; P:peptide mating pheromone maturation involved in positive regulation of conjugation with cellular fusion; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR SUPFAM; SSF63411; SSF63411; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome; Zinc.
FT CHAIN 1..1208
FT /note="Putative protease AXL1"
FT /id="PRO_0000074417"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10096"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CONFLICT 113
FT /note="E -> G (in Ref. 1; BAA04613)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1208 AA; 138332 MW; 4FC2F237CC3FD978 CRC64;
MSLREVTNYE VSFYIPLSYS NRTHKVCKLP NGILALIISD PTDTSSSCSL TVCTGSHNDP
KDIAGLAHLC EHMILSAGSK KYPDPGLFHT LIAKNNGSQN AFTTGEQTTF YFELPNTQNN
GEFTFESILD VFASFFKEPL FNPLLISKEI YAIQSEHEGN ISSTTKIFYH AARILANPDH
PFSRFSTGNI HSLSSIPQLK KIKLKSSLNT YFENNFFGEN ITLCIRGPQS VNILTKLALS
KFGDIKPKSA VKERSISIRT RSFRRSKSLK KRQDSSKNDY SDLKTFKILN TTWEKKYKNT
MCFQQFPECN SIFINSNKVP IMRLLFPVSD KNTRFTKDDI KIYSHLWCEL FGDESPGSLS
YYLASKGWLT GCFAFTSEFA IGDIGLILEL ELTNSGWENI KRITTIVLNR LLPSFYVMNI
DYLITFLKEQ NLIDLVSFLY QSSEDLPMEE CSKLSGILQD DLECLTPPNI FKGFKSLIEI
DDPNIEKYEN TKANIQWWTG QAIKFQNFLK SFMNHDNMRL LLLGNIKSGN IFDKMKNKSD
ICTDFFYEFE YYTANVHLAS DNKFHSNSSY EFNFPTGNLF LPDCVSDPLK LQQLFLECSL
KSKFATLRPQ IYSEPTRTKP QLVSENQNYE MWILKEDPNF ASDNKSVVSF EVLGLGIKPS
PEATIHLEVL AQALFIITSS FLYPALRIGY TYEIASSSKG NVTLRFTISG FPEGVFTIVK
TFVDTLKLIA TDPTFLSKDT LRKARILVRN KYKNASSDNC VKLASVGLLI VLEKYIWTLE
DRINALELTE LESFEKFCFL FWRNPKHLVL FMQGSLEYAD AINRYLNNNF TQHLKISNEG
SKPTIRLYPP PSTKDLDQGT NAFISYNGHQ DDPNNSIVYF IQTAQRDDIK NLTLTFLTEY
LFSLTLVPDL RNKKQIGYIV LGGLRVLTDT VGIHITVMSG SSGHNLETRI NEYLSYLQLQ
VLNRFTEFDF RRILLEPFLN LLKQNSTKQF EGSAGPVDLL NEIVANVQNG DNYTLNNKQM
RQHRKVRNKI AEGRLNFQED HEMIDISFLQ KLTLKKYLAF FESKISIYSA QRSKLSIMIT
SPMAEKEIAS RKMFLQLEAF LKINGFAIKN EDLKKIVEHS KGNPILLVKN LFTYFRRRNE
VFKLGTVVLQ EILKIIGMNL KQRYGSILGF SSQDGEGQEI EKFWNNDTSP IVPLQELPEP
NFFRKAAF
