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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}.
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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
 
 
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