PEFB_DICDI
ID PEFB_DICDI Reviewed; 205 AA.
AC Q95YL4; Q54BP3;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Penta-EF hand domain-containing protein 2;
DE AltName: Full=Apoptosis-linked gene 2 protein homolog B;
DE AltName: Full=Dd-ALG-2b;
DE AltName: Full=DdPEF-2;
GN Name=pefB; Synonyms=alg2B; ORFNames=DDB_G0293530;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RC STRAIN=AX2;
RX PubMed=11481037; DOI=10.1093/oxfordjournals.jbchem.a002974;
RA Ohkouchi S., Nishio K., Maeda M., Hitomi K., Adachi H., Maki M.;
RT "Identification and characterization of two penta-EF-hand Ca(2+)-binding
RT proteins in Dictyostelium discoideum.";
RL J. Biochem. 130:207-215(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBUNIT, CALCIUM-BINDING,
RP SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11927596; DOI=10.1074/jbc.m201718200;
RA Aubry L., Mattei S., Blot B., Sadoul R., Satre M., Klein G.;
RT "Biochemical characterization of two analogues of the apoptosis-linked gene
RT 2 protein in Dictyostelium discoideum and interaction with a physiological
RT partner in mammals, murine Alix.";
RL J. Biol. Chem. 277:21947-21954(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- SUBUNIT: In contrast to pefA, does not form homodimers in presence of
CC Ca(2+). May form heterodimers with pefA. {ECO:0000269|PubMed:11927596}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11481037,
CC ECO:0000269|PubMed:11927596}. Membrane {ECO:0000269|PubMed:11481037,
CC ECO:0000269|PubMed:11927596}; Peripheral membrane protein.
CC Note=Membrane-associated in the presence of Ca(2+).
CC {ECO:0000269|PubMed:11481037}.
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed throughout development
CC (at protein level). Expression peaks at the aggregation stage,
CC decreases at the tipped aggregate and remains low at later stages.
CC Expressed more abundantly in the extreme tip of the prestalk region,
CC slugs and early culminants. {ECO:0000269|PubMed:11481037,
CC ECO:0000269|PubMed:11927596}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking pefB and mutants lacking both pefA
CC and pefB grow normally in axenic medium or on bacterial lawns, and have
CC no major differentiation defect, apart from the fact that mutants
CC lacking pefB have a stalk base thicker than normal.
CC {ECO:0000269|PubMed:11927596}.
CC -!- SIMILARITY: Belongs to the Peflin/Sorcin family. {ECO:0000305}.
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DR EMBL; AB056714; BAB64571.1; -; mRNA.
DR EMBL; AF358912; AAM00238.1; -; mRNA.
DR EMBL; AF358914; AAM00240.1; -; Genomic_DNA.
DR EMBL; AAFI02000218; EAL60577.1; -; Genomic_DNA.
DR RefSeq; XP_628986.1; XM_628984.1.
DR AlphaFoldDB; Q95YL4; -.
DR SMR; Q95YL4; -.
DR STRING; 44689.DDB0215364; -.
DR PaxDb; Q95YL4; -.
DR EnsemblProtists; EAL60577; EAL60577; DDB_G0293530.
DR GeneID; 8629269; -.
DR KEGG; ddi:DDB_G0293530; -.
DR dictyBase; DDB_G0293530; pefB.
DR eggNOG; KOG0037; Eukaryota.
DR HOGENOM; CLU_051357_1_1_1; -.
DR InParanoid; Q95YL4; -.
DR OMA; RDTGQQG; -.
DR PhylomeDB; Q95YL4; -.
DR PRO; PR:Q95YL4; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0005737; C:cytoplasm; IDA:dictyBase.
DR GO; GO:0016020; C:membrane; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; IDA:dictyBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:dictyBase.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:dictyBase.
DR GO; GO:0030587; P:sorocarp development; IGI:dictyBase.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13202; EF-hand_5; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Membrane; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..205
FT /note="Penta-EF hand domain-containing protein 2"
FT /id="PRO_0000328613"
FT DOMAIN 45..75
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 76..111
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 119..141
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 54
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 56
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 58
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 60
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 65
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 89
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 91
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 93
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 95
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 205 AA; 23307 MW; 32E471BB86191AB0 CRC64;
MYGYGYTPAV VAPTVMSFSF VPPQAFQQCW FYSLYTQIQQ AQLYEMQSWF MRVDANRSGT
ISSGELQYLN IGGTPLGIET ATKLIKVFDH NKNGQIDFYE YAALHQFINN LYRCFVANDR
NFSGTIDANE IYNALITSGF QLPFPTVNYL FLKLSPSGYG LLFTQFLNLC ATVALTRSLF
EWNDPMRTGV VHLNLAQLYD IIALV
