CHP3_XENTR
ID CHP3_XENTR Reviewed; 214 AA.
AC Q0V9B1; A4II70;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Calcineurin B homologous protein 3;
DE AltName: Full=Tescalcin {ECO:0000250|UniProtKB:Q96BS2};
DE Short=TSC {ECO:0000250|UniProtKB:Q96BS2};
GN Name=tesc; Synonyms=chp3;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAI21663.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=N6 {ECO:0000312|EMBL:AAI21663.1};
RC TISSUE=Ovary {ECO:0000312|EMBL:AAI21663.1}, and
RC Tadpole {ECO:0000312|EMBL:AAI35887.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Functions as an integral cofactor in cell pH regulation by
CC controlling plasma membrane-type Na(+)/H(+) exchange activity. Promotes
CC the induction of hematopoietic stem cell differentiation toward
CC megakaryocytic lineage. Essential for the coupling of ERK cascade
CC activation with the expression of ETS family genes in megakaryocytic
CC differentiation. Also involved in granulocytic differentiation in a
CC ERK-dependent manner. Inhibits the phosphatase activity of calcineurin
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer (By similarity).
CC {ECO:0000250|UniProtKB:Q9JKL5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BS2,
CC ECO:0000250|UniProtKB:Q9JKL5}. Cytoplasm {ECO:0000250|UniProtKB:Q96BS2,
CC ECO:0000250|UniProtKB:Q9JKL5}. Membrane {ECO:0000250|UniProtKB:Q96BS2};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q96BS2}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96BS2}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q96BS2}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q9JKL5}.
CC -!- DOMAIN: Binds calcium via its EF-hands. Calcium-binding mediates a
CC conformational change. Can also bind magnesium (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family. CHP
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI35887.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC121662; AAI21663.1; -; mRNA.
DR EMBL; BC135886; AAI35887.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001072423.1; NM_001078955.1.
DR AlphaFoldDB; Q0V9B1; -.
DR SMR; Q0V9B1; -.
DR STRING; 8364.ENSXETP00000059666; -.
DR PaxDb; Q0V9B1; -.
DR DNASU; 779877; -.
DR Ensembl; ENSXETT00000062972; ENSXETP00000059666; ENSXETG00000030230.
DR GeneID; 779877; -.
DR KEGG; xtr:779877; -.
DR CTD; 54997; -.
DR Xenbase; XB-GENE-991111; tesc.
DR eggNOG; KOG0034; Eukaryota.
DR HOGENOM; CLU_061288_10_0_1; -.
DR InParanoid; Q0V9B1; -.
DR OMA; EIETRMH; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q0V9B1; -.
DR TreeFam; TF354284; -.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000030230; Expressed in heart and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0019212; F:phosphatase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISS:UniProtKB.
DR GO; GO:0030854; P:positive regulation of granulocyte differentiation; ISS:UniProtKB.
DR GO; GO:0032417; P:positive regulation of sodium:proton antiporter activity; ISS:UniProtKB.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0051604; P:protein maturation; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IBA:GO_Central.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR SMART; SM00054; EFh; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Cell projection; Cytoplasm; Differentiation;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Nucleus;
KW Protein kinase inhibitor; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000255"
FT CHAIN 2..214
FT /note="Calcineurin B homologous protein 3"
FT /id="PRO_0000390720"
FT DOMAIN 110..145
FT /note="EF-hand"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000305"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 214 AA; 24666 MW; D97BEC9529B82BFB CRC64;
MGLSHSHSVE TRQLVEKTGF SAEQIEHLHK RFNSLSGDLL TIRKGHLNGI SDLEVNPIRS
KIVDAFFDKR NLRKGSSGYV EEINFEEFLT IMSYFRPLSQ NMDEENISVC RKDKLRFLFN
MYDTDNDSKI TLEEYRKVVE ELLSGNPNIE KETARSIADG AMLEAASICV GQMEPDQVYE
GITFDDFLKI WEGIDIETKM HIRFLNMESI PSCR
