CANB1_DICDI
ID CANB1_DICDI Reviewed; 180 AA.
AC Q55G87; Q55G86; Q9GP83;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Calcineurin subunit B type 1;
DE AltName: Full=Calcineurin regulatory subunit 1;
DE AltName: Full=Protein phosphatase 2B regulatory subunit 1;
GN Name=cnbA; ORFNames=DDB_G0267446;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2),
RP FUNCTION, INTERACTION WITH CANA, AND DEVELOPMENTAL STAGE.
RC STRAIN=AX2;
RX PubMed=11352578; DOI=10.1006/jmbi.2001.4645;
RA Aichem A., Mutzel R.;
RT "Unconventional mRNA processing in the expression of two calcineurin B
RT isoforms in Dictyostelium.";
RL J. Mol. Biol. 308:873-882(2001).
RN [2]
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).
RN [3]
RP FUNCTION.
RX PubMed=16512895; DOI=10.1186/1471-213x-6-12;
RA Boeckeler K., Tischendorf G., Mutzel R., Weissenmayer B.;
RT "Aberrant stalk development and breakdown of tip dominance in Dictyostelium
RT cell lines with RNAi-silenced expression of calcineurin B.";
RL BMC Dev. Biol. 6:12-12(2006).
CC -!- FUNCTION: Regulatory subunit of calcineurin, a calcium-dependent,
CC calmodulin stimulated protein phosphatase (PubMed:11352578). Confers
CC calcium sensitivity (PubMed:11352578). Important for stalk formation
CC (PubMed:16512895). {ECO:0000269|PubMed:11352578,
CC ECO:0000269|PubMed:16512895}.
CC -!- SUBUNIT: Forms a complex composed of a calmodulin-dependent catalytic
CC subunit canA (also known as calcineurin A) and a regulatory Ca(2+)-
CC binding subunit cnbA (also known as calcineurin B).
CC {ECO:0000250|UniProtKB:P63098}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=CNBL;
CC IsoId=Q55G87-1; Sequence=Displayed;
CC Name=2; Synonyms=CNBS;
CC IsoId=Q55G87-2; Sequence=VSP_033147;
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is present in constant amounts in
CC vegetative cells and throughout development. Isoform 2 is barely
CC detectable in vegetative and early preaggregative cells, but present at
CC high levels during aggregation and in later stages (at protein level).
CC {ECO:0000269|PubMed:11352578}.
CC -!- MISCELLANEOUS: Amoeba with reduced cnbA levels produce smaller stalk
CC cells and smaller stalks due to incomplete vacuolization of stalk
CC cells. {ECO:0000269|PubMed:16512895}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ301668; CAC20026.2; -; Genomic_DNA.
DR EMBL; AAFI02000003; EAL73175.1; -; Genomic_DNA.
DR EMBL; AAFI02000003; EAL73176.1; -; Genomic_DNA.
DR RefSeq; XP_001134484.1; XM_001134484.1.
DR RefSeq; XP_647297.1; XM_642205.1.
DR AlphaFoldDB; Q55G87; -.
DR SMR; Q55G87; -.
DR STRING; 44689.DDB0191204; -.
DR PaxDb; Q55G87; -.
DR EnsemblProtists; EAL73175; EAL73175; DDB_G0267446.
DR EnsemblProtists; EAL73176; EAL73176; DDB_G0267446.
DR GeneID; 8616103; -.
DR KEGG; ddi:DDB_G0267446; -.
DR dictyBase; DDB_G0267446; cnbA.
DR eggNOG; KOG0034; Eukaryota.
DR InParanoid; Q55G87; -.
DR OMA; DTNFDRD; -.
DR PhylomeDB; Q55G87; -.
DR Reactome; R-DDI-2871809; FCERI mediated Ca+2 mobilization.
DR Reactome; R-DDI-4086398; Ca2+ pathway.
DR Reactome; R-DDI-5607763; CLEC7A (Dectin-1) induces NFAT activation.
DR PRO; PR:Q55G87; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005955; C:calcineurin complex; IDA:dictyBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008597; F:calcium-dependent protein serine/threonine phosphatase regulator activity; IDA:dictyBase.
DR GO; GO:0019902; F:phosphatase binding; IBA:GO_Central.
DR GO; GO:0097720; P:calcineurin-mediated signaling; IMP:dictyBase.
DR GO; GO:0031287; P:positive regulation of sorocarp stalk cell differentiation; IMP:dictyBase.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:dictyBase.
DR GO; GO:0043157; P:response to cation stress; IMP:dictyBase.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR015757; Calcineur_B.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR45942; PTHR45942; 1.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Lipoprotein; Metal-binding; Myristate;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..180
FT /note="Calcineurin subunit B type 1"
FT /id="PRO_0000331196"
FT DOMAIN 25..60
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 62..92
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 94..129
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 135..170
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 138..143
FT /note="canA/calcineurin A binding"
FT /evidence="ECO:0000250|UniProtKB:P63098"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 42
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 44
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 49
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 107
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 118
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 150
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 152
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 154
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT SITE 125
FT /note="Interaction with PxVP motif in substrates of the
FT catalytic subunit"
FT /evidence="ECO:0000250|UniProtKB:P63098"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_033147"
FT CONFLICT 80
FT /note="F -> S (in Ref. 1; CAC20026)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="G -> V (in Ref. 1; CAC20026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 180 AA; 20757 MW; 5E9956F9CF2BBD15 CRC64;
MGNQHSLLNK EQLEQMKDNS SFSEAELKKL YRRFQMLDKD GSGTLTTDEF LSIPDLALNP
LLERVIQIFD QNKDNEIEFF EFVGTLATLS HKGTKEDKLK FLFQIYDIDC DGFISNGELF
QVLKMMVGTN LNDVQLQQIV DKTIIEGDYD KDGKISFDEF IHMIGNQEGI EEKLSVNWSE
