FRA1_YEAST
ID FRA1_YEAST Reviewed; 749 AA.
AC Q07825; D6VXX5;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Putative Xaa-Pro aminopeptidase FRA1;
DE EC=3.4.11.9;
DE AltName: Full=Fe repressor of activation 1;
GN Name=FRA1; OrderedLocusNames=YLL029W;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 PROTEIN SEQUENCE OF 189-199 AND 593-609, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RA Bienvenut W.V., Peters C.;
RL Submitted (JUN-2005) to UniProtKB.
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 FUNCTION, AND INTERACTION WITH FRA2.
RX PubMed=18281282; DOI=10.1074/jbc.m801160200;
RA Kumanovics A., Chen O.S., Li L., Bagley D., Adkins E.M., Lin H.,
RA Dingra N.N., Outten C.E., Keller G., Winge D., Ward D.M., Kaplan J.;
RT "Identification of FRA1 and FRA2 as genes involved in regulating the yeast
RT iron regulon in response to decreased mitochondrial iron-sulfur cluster
RT synthesis.";
RL J. Biol. Chem. 283:10276-10286(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-69; SER-92 AND SER-95, 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: Involved in the regulation of the iron regulon in responss to
CC decreased mitochondrial iron-sulfur cluster synthesis.
CC {ECO:0000269|PubMed:18281282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of any N-terminal amino acid, including proline, that
CC is linked to proline, even from a dipeptide or tripeptide.;
CC EC=3.4.11.9;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000305};
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with FRA2. {ECO:0000250,
CC ECO:0000269|PubMed:18281282}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 3237 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}.
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DR EMBL; Z73134; CAA97478.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09291.1; -; Genomic_DNA.
DR PIR; S64780; S64780.
DR RefSeq; NP_013071.1; NM_001181849.1.
DR AlphaFoldDB; Q07825; -.
DR SMR; Q07825; -.
DR BioGRID; 31223; 197.
DR DIP; DIP-6443N; -.
DR IntAct; Q07825; 4.
DR MINT; Q07825; -.
DR STRING; 4932.YLL029W; -.
DR MEROPS; M24.A10; -.
DR iPTMnet; Q07825; -.
DR MaxQB; Q07825; -.
DR PaxDb; Q07825; -.
DR PRIDE; Q07825; -.
DR EnsemblFungi; YLL029W_mRNA; YLL029W; YLL029W.
DR GeneID; 850630; -.
DR KEGG; sce:YLL029W; -.
DR SGD; S000003952; FRA1.
DR VEuPathDB; FungiDB:YLL029W; -.
DR eggNOG; KOG2413; Eukaryota.
DR GeneTree; ENSGT00940000157716; -.
DR HOGENOM; CLU_011781_2_6_1; -.
DR InParanoid; Q07825; -.
DR OMA; YRPGKWG; -.
DR BioCyc; YEAST:G3O-32133-MON; -.
DR Reactome; R-SCE-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q07825; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q07825; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR GO; GO:0034396; P:negative regulation of transcription from RNA polymerase II promoter in response to iron; IMP:SGD.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd01085; APP; 1.
DR Gene3D; 3.40.350.10; -; 2.
DR Gene3D; 3.90.230.10; -; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR033740; Pept_M24B.
DR InterPro; IPR032416; Peptidase_M24_C.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF53092; SSF53092; 1.
DR SUPFAM; SSF55920; SSF55920; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 1: Evidence at protein level;
KW Aminopeptidase; Cytoplasm; Direct protein sequencing; Hydrolase; Manganese;
KW Metal-binding; Metalloprotease; Phosphoprotein; Protease;
KW Reference proteome.
FT CHAIN 1..749
FT /note="Putative Xaa-Pro aminopeptidase FRA1"
FT /id="PRO_0000185086"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 551
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 562
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 562
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT BINDING 660
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 674
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255"
FT BINDING 674
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
SQ SEQUENCE 749 AA; 84924 MW; 372FFF818A5FBDB9 CRC64;
MTSKPSTSDG RAHSISHVPG THMRGTSASH SPRPFRPCAD CTCSPGLLSR QGRRASLFLR
QLENSRRSSS MLLNELKGAG GGSSAGNGSV YSCDSLCAVN REVNTTDRLL KLRQEMKKHD
LCCYIVPSCD EHQSEYVSLR DQRRAFISGF SGSAGVACIT RDLLNFNDDH PDGKSILSTD
GRYFNQARQE LDYNWTLLRQ NEDPITWQEW CVREALEMAK GLGNKEGMVL KIGIDPKLIT
FNDYVSFRKM IDTKYDAKGK VELVPVEENL VDSIWPDFET LPERPCNDLL LLKYEFHGEE
FKDKKEKLLK KLNDKASSAT TGRNTFIVVA LDEICWLLNL RGSDIDYNPV FFSYVAINED
ETILFTNNPF NDDISEYFKI NGIEVRPYEQ IWEHLTKITS QASSAEHEFL IPDSASWQMV
RCLNTSTNAN GAIAKKMTAQ NFAIIHSPID VLKSIKNDIE IKNAHKAQVK DAVCLVQYFA
WLEQQLVGRE ALIDEYRAAE KLTEIRKTQR NFMGNSFETI SSTGSNAAII HYSPPVENSS
MIDPTKIYLC DSGSQFLEGT TDITRTIHLT KPTKEEMDNY TLVLKGGLAL ERLIFPENTP
GFNIDAIARQ FLWSRGLDYK HGTGHGIGSF LNVHEGPMGV GFRPHLMNFP LRAGNIISNE
PGYYKDGEYG IRIESDMLIK KATEKGNFLK FENMTVVPYC RKLINTKLLN EEEKTQINEY
HARVWRTIVH FLQPQSISYK WLKRETSPL
