YIK8_YEAST
ID YIK8_YEAST Reviewed; 696 AA.
AC P40483; D6VVH9; Q6B2N8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Putative zinc metalloproteinase YIL108W;
DE EC=3.4.24.-;
GN OrderedLocusNames=YIL108W;
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=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 [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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY
RP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [8]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-245; LYS-478; LYS-518;
RP LYS-579; LYS-590 AND LYS-596, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion. {ECO:0000250};
CC -!- INTERACTION:
CC P40483; Q06449: PIN3; NbExp=3; IntAct=EBI-25176, EBI-35523;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M10B family. {ECO:0000305}.
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DR EMBL; Z38125; CAA86272.1; -; Genomic_DNA.
DR EMBL; AY692692; AAT92711.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08445.1; -; Genomic_DNA.
DR PIR; S48464; S48464.
DR RefSeq; NP_012158.1; NM_001179456.1.
DR AlphaFoldDB; P40483; -.
DR SMR; P40483; -.
DR BioGRID; 34883; 39.
DR DIP; DIP-5657N; -.
DR IntAct; P40483; 5.
DR MINT; P40483; -.
DR STRING; 4932.YIL108W; -.
DR iPTMnet; P40483; -.
DR MaxQB; P40483; -.
DR PaxDb; P40483; -.
DR PRIDE; P40483; -.
DR EnsemblFungi; YIL108W_mRNA; YIL108W; YIL108W.
DR GeneID; 854698; -.
DR KEGG; sce:YIL108W; -.
DR SGD; S000001370; YIL108W.
DR VEuPathDB; FungiDB:YIL108W; -.
DR eggNOG; KOG4525; Eukaryota.
DR GeneTree; ENSGT00730000114706; -.
DR HOGENOM; CLU_009601_2_1_1; -.
DR InParanoid; P40483; -.
DR OMA; ALRFRFH; -.
DR BioCyc; YEAST:G3O-31363-MON; -.
DR PRO; PR:P40483; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40483; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09613; Jacalin_metallopeptidase_like; 1.
DR Gene3D; 2.100.10.30; -; 1.
DR InterPro; IPR001229; Jacalin-like_lectin_dom.
DR InterPro; IPR036404; Jacalin-like_lectin_dom_sf.
DR InterPro; IPR033862; Jacalin-like_metallopeptidase.
DR InterPro; IPR021917; Unchr_Zn-peptidase-like.
DR Pfam; PF12044; Metallopep; 1.
DR SUPFAM; SSF51101; SSF51101; 1.
DR PROSITE; PS51752; JACALIN_LECTIN; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Isopeptide bond; Metal-binding; Metalloprotease;
KW Phosphoprotein; Protease; Reference proteome; Ubl conjugation; Zinc.
FT CHAIN 1..696
FT /note="Putative zinc metalloproteinase YIL108W"
FT /id="PRO_0000078181"
FT DOMAIN 522..695
FT /note="Jacalin-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01088"
FT ACT_SITE 319
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 478
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 518
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 579
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 590
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CROSSLNK 596
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 696
FT /note="L -> F (in Ref. 3; AAT92711)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 696 AA; 77414 MW; 89ED15503933653B CRC64;
MVGSKDIDLF NLRENEQIVS PCLIVHGKCN KQNGAKTVQV QHPQLPPITY PIHNQFFKAT
VILTPGENKL TFVTDTNTAR TIVCYYTPLT QNPPVHLCLI LAKDSPLQFD SPREQKDREG
GNGLELAIKK LRLGARLMQA YTNEQMLRNS MGNRTFPFVE EFTWDTLFER PAMRNTIKIH
VVRSEKTVKE IQDPDIAQQN SKGKNTGALF GIAMDALKSY GGPFTNNEKP VQAACMFLDT
HWDGKLIRGH AALGGGDDSI KLAIFGSHGL YSWPTCLEQL VPYFTDETRS STSEVANDCN
ECGTYWECLT ITLGAFMHEI GHLLGCPHQE SGVMLRGYTT LNRSFLTKEA YSVRTNSTGA
SPPIFPKEEC TWNRLDTVRF LYHPSFTLPQ DYYDPSFMRP TKLGGYPNIK HSVYPLGNGS
CRILSPTGIY LIEIICDDLA RGHIEYLPVS LGGQGPQREV IVTLDDLRAR LPKNELAKFG
NTFKLKILSV NAPETEFDKF PSLLDVQPLD MSKYGFSKNV QGIKSPLYGR SDGGNAVGVV
AFDVRLVTAV RIYHGYALDG VRFYYKEKPT GTKDAPASKP SVPPRNYFSK ITHSIKNHAS
INEENLKSVL FGHETQNFTD ATLEPGEIII GFNLRCGAWV DAIQIITSHG RMTDMFGNKD
GGGFAELQPP NGQYILGVTG RVGQWVDAFG IIYGAL
