PEF1_YEAST
ID PEF1_YEAST Reviewed; 335 AA.
AC P53238; D6VUJ3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Peflin;
DE AltName: Full=Penta-EF hand domain-containing protein 1;
GN Name=PEF1; OrderedLocusNames=YGR058W;
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=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 324.
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 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 [4]
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 [5]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF
RP GLU-218.
RX PubMed=17640275; DOI=10.1111/j.1365-2958.2007.05852.x;
RA Vernarecci S., Colotti G., Ornaghi P., Schiebel E., Chiancone E.,
RA Filetici P.;
RT "The yeast penta-EF protein Pef1p is involved in cation-dependent budding
RT and cell polarization.";
RL Mol. Microbiol. 65:1122-1138(2007).
CC -!- FUNCTION: Calcium-binding protein that is required for polar bud growth
CC and cell wall abscission. Can also bind zinc ions.
CC {ECO:0000269|PubMed:17640275}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17640275}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17640275}. Nucleus
CC {ECO:0000269|PubMed:17640275}. Bud tip {ECO:0000269|PubMed:17640275}.
CC Bud neck {ECO:0000269|PubMed:17640275}. Note=Accumulates at the site of
CC bud emergence in G1 cells. In small budded G1 cells, localizes
CC asymmetrically on the tip of the daughter cell and in the nucleus. At a
CC later stage of the G1 phase, is found at the emerging bud cortex and
CC localizes in the nucleus. In large budded G2/M cells, localizes
CC preferentially at the bud neck between the dividing mother and daughter
CC cells, with very weak signals in the nucleus.
CC {ECO:0000269|PubMed:17640275}.
CC -!- DOMAIN: Binds calcium via its EF-hands. {ECO:0000305|PubMed:17640275}.
CC -!- MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z72843; CAA97059.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08154.2; -; Genomic_DNA.
DR PIR; S64352; S64352.
DR RefSeq; NP_011572.2; NM_001181187.2.
DR AlphaFoldDB; P53238; -.
DR SMR; P53238; -.
DR BioGRID; 33303; 241.
DR DIP; DIP-1862N; -.
DR IntAct; P53238; 8.
DR MINT; P53238; -.
DR STRING; 4932.YGR058W; -.
DR iPTMnet; P53238; -.
DR MaxQB; P53238; -.
DR PaxDb; P53238; -.
DR PRIDE; P53238; -.
DR EnsemblFungi; YGR058W_mRNA; YGR058W; YGR058W.
DR GeneID; 852949; -.
DR KEGG; sce:YGR058W; -.
DR SGD; S000003290; PEF1.
DR VEuPathDB; FungiDB:YGR058W; -.
DR eggNOG; KOG0037; Eukaryota.
DR HOGENOM; CLU_863808_0_0_1; -.
DR InParanoid; P53238; -.
DR OMA; NTHFCIS; -.
DR BioCyc; YEAST:G3O-30775-MON; -.
DR PRO; PR:P53238; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53238; protein.
DR GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR GO; GO:0005934; C:cellular bud tip; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030427; C:site of polarized growth; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:SGD.
DR GO; GO:0008270; F:zinc ion binding; IDA:SGD.
DR GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0003400; P:regulation of COPII vesicle coating; IDA:SGD.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Metal-binding; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..335
FT /note="Peflin"
FT /id="PRO_0000073720"
FT DOMAIN 144..192
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 198..223
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 224..259
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 260..300
FT /note="EF-hand 4"
FT /evidence="ECO:0000305"
FT DOMAIN 301..332
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 23..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 170
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 176
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 181
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT MUTAGEN 218
FT /note="E->A: Induces EGTA and SDS sensitivity."
FT /evidence="ECO:0000269|PubMed:17640275"
FT CONFLICT 324
FT /note="D -> Y (in Ref. 1; CAA97059)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 38342 MW; A653D29FFADA6BD7 CRC64;
MCAKKLKYAA GDDFVRYATP KEAMEETRRE FEKEKQRQQQ IKVTQAQTPN TRVHSAPIPL
QTQYNKNRAE NGHHSYGSPQ SYSPRHTKTP VDPRYNVIAQ KPAGRPIPPA PTHYNNLNTS
AQRIASSPPP LIHNQAVPAQ LLKKVAPASF DSREDVRDMQ VATQLFHNHD VKGKNRLTAE
ELQNLLQNDD NSHFCISSVD ALINLFGASR FGTVNQAEFI ALYKRVKSWR KVYVDNDING
SLTISVSEFH NSLQELGYLI PFEVSEKTFD QYAEFINRNG TGKELKFDKF VEALVWLMRL
TKLFRKFDTN QEGIATIQYK DFIDATLYLG RFLPH
