ECM5_YEAST
ID ECM5_YEAST Reviewed; 1411 AA.
AC Q03214; D6VZZ9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Protein ECM5;
DE AltName: Full=Extracellular matrix protein 5;
GN Name=ECM5; OrderedLocusNames=YMR176W; ORFNames=YM8010.06;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 IDENTIFICATION.
RX PubMed=9335584; DOI=10.1093/genetics/147.2.435;
RA Lussier M., White A.-M., Sheraton J., di Paolo T., Treadwell J.,
RA Southard S.B., Horenstein C.I., Chen-Weiner J., Ram A.F.J., Kapteyn J.C.,
RA Roemer T.W., Vo D.H., Bondoc D.C., Hall J., Zhong W.-W., Sdicu A.-M.,
RA Davies J., Klis F.M., Robbins P.W., Bussey H.;
RT "Large scale identification of genes involved in cell surface biosynthesis
RT and architecture in Saccharomyces cerevisiae.";
RL Genetics 147:435-450(1997).
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).
CC -!- FUNCTION: May be involved in cell wall organization and biogenesis.
CC -!- INTERACTION:
CC Q03214; P32561: RPD3; NbExp=5; IntAct=EBI-27382, EBI-15864;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z49808; CAA89909.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10073.1; -; Genomic_DNA.
DR PIR; S55123; S55123.
DR RefSeq; NP_013901.1; NM_001182682.1.
DR AlphaFoldDB; Q03214; -.
DR BioGRID; 35354; 68.
DR ComplexPortal; CPX-1372; SNT2C histone deacetylase complex.
DR DIP; DIP-6678N; -.
DR IntAct; Q03214; 6.
DR STRING; 4932.YMR176W; -.
DR iPTMnet; Q03214; -.
DR MaxQB; Q03214; -.
DR PaxDb; Q03214; -.
DR PRIDE; Q03214; -.
DR EnsemblFungi; YMR176W_mRNA; YMR176W; YMR176W.
DR GeneID; 855214; -.
DR KEGG; sce:YMR176W; -.
DR SGD; S000004788; ECM5.
DR VEuPathDB; FungiDB:YMR176W; -.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000159220; -.
DR HOGENOM; CLU_250352_0_0_1; -.
DR InParanoid; Q03214; -.
DR OMA; KWAPVAP; -.
DR BioCyc; YEAST:G3O-32864-MON; -.
DR Reactome; R-SCE-3214842; HDMs demethylate histones.
DR PRO; PR:Q03214; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03214; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0070211; C:Snt2C complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0034599; P:cellular response to oxidative stress; IMP:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0006979; P:response to oxidative stress; IC:ComplexPortal.
DR Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Metal-binding; Nucleus;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..1411
FT /note="Protein ECM5"
FT /id="PRO_0000200597"
FT DOMAIN 118..159
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 185..279
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 476..695
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 1238..1290
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 285..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1411 AA; 162701 MW; 18768BD29934D9F9 CRC64;
MSGHDSVTKI SHILNEPVNE KVMVQNGFHE SSKIADIELE IQERPSIKQW ESPRSAVIPT
SNHNFSPFLY TQFKSRGAAP FAPETIKSVD LVELPEGVPA RVFHEKTGLF YQISPHSIPT
FILAKKELPD PIKFYELVED LGSVYGCVKL KIIPDADKFT QLNVDVDRLW FKARKQFFNS
NEFQRTKIVD FYAKLYNFHN KIKKSTLTRI PSIDKRTLDL YRLRSCVKLR GGFNAVCEKK
LWAQIGRELG YSGRIMSSLS TSLRSAYAKI LLDFDIYEEE EQAARNNEKN EDMVESEIFR
HSNSRSRDEE EPLHKKAKIH RDVFRAGSIN HEFKRMRDIK HIKGFPTYFN SLTEFKLGYT
QSTETTLPGY DFTFWENGME IYDKSKYETK TSPVYNLRQY YEKSLAVFTA IVAKFGSSYP
DLFAKHTTLP QKEFERLYFH LLSEHFIDFE IDTGLGLPCS MRSPGNNSSN EKFAIKNILD
QWNLDNIPLN ELSLLQHLDL DMANFTRTTY DIGMLFSCQG WSVSDHFLPS IDFNHLGSTK
LVYSIAPKDM EKFEALIARG KSEWDTIQSR PRYSTSDDEL KSFIETDFYK SFLDAEQSAD
YSNTGDNSKN SFPEDKIAGN TLHDGSQSDF IFEPNFILAN GIKLYKTTQE QGSYIFKFPK
AFTCSIGSGF YLSQNAKFAP SSWLRFSSEA AKWTSKMGFL PGLDVNQLLI NALLNSNNPV
LRKKCRDLIS NYVVEEAENS KKLGELIGTV DVVYNKLNYI SDISLESTGL SKIVVTHGAL
QRNLSLKEFV VLLEKPENGA HSICGIPIRD QSGNLNVCLH SYFDSASLGI ALDGLDKPPT
SYLLVHNEDF EKKWDVLMTS TFRNRTVPLN IIQYLISHTD SNTEFNRMLR SNFDDSLLLI
EKCKKFIKTF VDVSCSVKDV DFGNGFNLRH LPLKFSDNMA DNLESLYESV RKCSIEFSEK
PTIIRLYHVS RQFPIDNRDI IDGNNLDLLK ELYQKSLTIP LKVSYWTKLT RKICRLEWLS
VYEHIFIERC DIKNEDPAKY SLPLLYSYFE FGLKYCDSED IDKLGEVRKL ILKYQDMMQK
VRVFLKKDPP SKISLSDLED VLLDIEEYRL PIQSSFFSEL DYVIREIENA KKMNDVNILY
NTDNIDKIDE LIRKNDPKFV KFANQFNGSR LDKRPLASDN SGSVKAKQEL KVFKLWNQHL
DQIMQKNKFI EILPSIFRCL DLKSDKYIPL ESCSKRQTKY CFCRRVEEGT AMVECEICKE
WYHVDCISNG ELVPPDDPNV LFVCSICTPP CMAVDNIEGV TFELDDLKRI LVESLKLSLI
PDPPILKNLF DVFAFALNFK NEMEKELFTN GYVNQLSSTH KIKYYLRKLK GSQCGFTNLT
DPLRKHCQVK DAEAIKWLTD NGRIIITGIP N
