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NAA25_YEAST
ID   NAA25_YEAST             Reviewed;         796 AA.
AC   Q12387; D6W1Z2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=N-terminal acetyltransferase B complex subunit MDM20;
DE            Short=NatB complex subunit MDM20;
DE   AltName: Full=Dislikes extra CIN8 protein 1;
DE   AltName: Full=Mitochondrial distribution and morphology protein 20;
GN   Name=MDM20; Synonyms=DEC1; OrderedLocusNames=YOL076W;
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].
RA   Kingsbury T.J., Hoyt M.A.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=9105043; DOI=10.1083/jcb.137.1.141;
RA   Hermann G.J., King E.J., Shaw J.M.;
RT   "The yeast gene, MDM20, is necessary for mitochondrial inheritance and
RT   organization of the actin cytoskeleton.";
RL   J. Cell Biol. 137:141-153(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9178509;
RX   DOI=10.1002/(sici)1097-0061(199705)13:6<583::aid-yea111>3.0.co;2-y;
RA   Tzermia M., Katsoulou C., Alexandraki D.;
RT   "Sequence analysis of a 33.2 kb segment from the left arm of yeast
RT   chromosome XV reveals eight known genes and ten new open reading frames
RT   including homologues of ABC transporters, inositol phosphatases and human
RT   expressed sequence tags.";
RL   Yeast 13:583-589(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [5]
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   [6]
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   [7]
RP   FUNCTION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=12783868; DOI=10.1074/jbc.m304690200;
RA   Polevoda B., Cardillo T.S., Doyle T.C., Bedi G.S., Sherman F.;
RT   "Nat3p and Mdm20p are required for function of yeast NatB Nalpha-terminal
RT   acetyltransferase and of actin and tropomyosin.";
RL   J. Biol. Chem. 278:30686-30697(2003).
RN   [8]
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   [9]
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   [10]
RP   FUNCTION.
RX   PubMed=12808144; DOI=10.1073/pnas.1232343100;
RA   Singer J.M., Shaw J.M.;
RT   "Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and
RT   regulate tropomyosin-actin interactions in budding yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7644-7649(2003).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
CC   -!- FUNCTION: Non-catalytic subunit of the NatB N-terminal
CC       acetyltransferase, which catalyzes acetylation of the amino-terminal
CC       methionine residues of all proteins beginning with Met-Asp or Met-Glu
CC       and of some proteins beginning with Met-Asn or Met-Met. NatB acetylates
CC       TPM1 protein and regulates tropomyocin-actin interactions. MDM20 is
CC       required for mitochondrial inheritance during budding and together with
CC       TPM1, is essential for the integrity and assembly of actin cables.
CC       Genetically interacts with CIN8. {ECO:0000269|PubMed:12783868,
CC       ECO:0000269|PubMed:12808144, ECO:0000269|PubMed:9105043}.
CC   -!- SUBUNIT: Component of the N-terminal acetyltransferase B (NatB)
CC       complex, which is composed of NAT3 and MDM20.
CC       {ECO:0000269|PubMed:12783868}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 5800 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the MDM20/NAA25 family. {ECO:0000305}.
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DR   EMBL; U36382; AAA79781.1; -; Genomic_DNA.
DR   EMBL; U54799; AAB00196.1; -; Genomic_DNA.
DR   EMBL; Z74818; CAA99086.1; -; Genomic_DNA.
DR   EMBL; AY693080; AAT93099.1; -; Genomic_DNA.
DR   EMBL; BK006948; DAA10708.1; -; Genomic_DNA.
DR   PIR; S66769; S66769.
DR   RefSeq; NP_014566.1; NM_001183330.1.
DR   AlphaFoldDB; Q12387; -.
DR   SMR; Q12387; -.
DR   BioGRID; 34326; 178.
DR   ComplexPortal; CPX-782; NatB N-alpha-acetyltransferase complex.
DR   IntAct; Q12387; 1.
DR   MINT; Q12387; -.
DR   STRING; 4932.YOL076W; -.
DR   iPTMnet; Q12387; -.
DR   MaxQB; Q12387; -.
DR   PaxDb; Q12387; -.
DR   PRIDE; Q12387; -.
DR   EnsemblFungi; YOL076W_mRNA; YOL076W; YOL076W.
DR   GeneID; 854079; -.
DR   KEGG; sce:YOL076W; -.
DR   SGD; S000005436; MDM20.
DR   VEuPathDB; FungiDB:YOL076W; -.
DR   eggNOG; KOG2053; Eukaryota.
DR   GeneTree; ENSGT00950000183174; -.
DR   HOGENOM; CLU_019572_0_0_1; -.
DR   InParanoid; Q12387; -.
DR   OMA; LPQLAYK; -.
DR   BioCyc; YEAST:G3O-33480-MON; -.
DR   BRENDA; 2.3.1.254; 984.
DR   PRO; PR:Q12387; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q12387; protein.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0031416; C:NatB complex; IDA:UniProtKB.
DR   GO; GO:0007010; P:cytoskeleton organization; IMP:SGD.
DR   GO; GO:0000001; P:mitochondrion inheritance; IMP:SGD.
DR   GO; GO:0017196; P:N-terminal peptidyl-methionine acetylation; IMP:SGD.
DR   GO; GO:0006474; P:N-terminal protein amino acid acetylation; IMP:ComplexPortal.
DR   GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:SGD.
DR   InterPro; IPR019183; N-acetylTrfase_B_cplx_non-cat.
DR   PANTHER; PTHR22767:SF3; PTHR22767:SF3; 1.
DR   Pfam; PF09797; NatB_MDM20; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..796
FT                   /note="N-terminal acetyltransferase B complex subunit
FT                   MDM20"
FT                   /id="PRO_0000079850"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   796 AA;  92809 MW;  30E57DB1B12DCD2C CRC64;
     MSDKIQEEIL GLVSRSNFKQ CYAKLGQLQK QFPNALYFKI LETYVKFKQS PGKFDYNKLL
     EEPYGLKGTT ITGDTRSLEF LHNFFVELGK YDEALHVYER GNFKFPSYEL SYHWFMKALE
     DSNYNQMSKA SLQLAKYSDS GNLPKRAYYF WNAISILAVS RFQENTLSDP KKILLSRLAR
     QSLLDLKPFQ NVQEIIVYCL VLDELFPQSR EISEEIVAIT FANFDTSVNL YLKNFILKHT
     KLLNSPQKLF EVCSKLIEKG LDDYELITNL IDAAYKLSKS KDEVKQWIDE NLGDSRNTRL
     ARLKLDIMYT DSVSESSLSY YLSKYHNKPC CSIDLNHYSG HINIDMLKSI MSKYDPEDKD
     LIHHCNILEL GLIGSDSINN YNKFKGTLEK KSVTDYSSCS TFLLEIVKDK CKKTNPELKD
     VLLCITILEN YQAKDPHNFD TMCWLIVLYM YLGLVPDAYF HFINLKIKNV QTDSLDYMIF
     SRFSTLFPNK QSDFYSKTFH EHNNLYDTSL ANLPRYIQVA FERNSYSKIL GMLEMRDKLM
     KSYTRWTKTL ENLQFSRLCN DKRGHLLQKL HEDWRSLEMT QSVSFSDNRD FSILDENFAQ
     FLNRGKILEY ANLNEESIFL TLIRELIIEA LPNGEKTEQI SALLKKLPSI NLEELLNNNL
     TEVESASFLI FFEIYENNGK NLHDLISRLM KVPINAKQNW MVSHTYLTKM ATLKTLDSLK
     RIKDKEIQKL IKNSLKELRS CCDDVFKGYS KALVQAYEEL KKDECGNLLK ELDVKAENVK
     NIKNSLLGIQ KSVRNL
 
 
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