CHP3_XENLA
ID CHP3_XENLA Reviewed; 214 AA.
AC Q5U554;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Calcineurin B homologous protein 3;
DE AltName: Full=Tescalcin {ECO:0000303|PubMed:19345287};
DE Short=TSC {ECO:0000250|UniProtKB:Q96BS2};
GN Name=tesc {ECO:0000303|PubMed:19345287}; Synonyms=chp3;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000312|EMBL:AAH84830.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tadpole {ECO:0000312|EMBL:AAH84830.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=19345287; DOI=10.1016/j.gep.2009.03.004;
RA Bao Y., Hudson Q.J., Perera E.M., Akan L., Tobet S.A., Smith C.A.,
RA Sinclair A.H., Berkovitz G.D.;
RT "Expression and evolutionary conservation of the tescalcin gene during
RT development.";
RL Gene Expr. Patterns 9:273-281(2009).
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}.
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DR EMBL; BC084830; AAH84830.1; -; mRNA.
DR RefSeq; NP_001088498.1; NM_001095029.2.
DR AlphaFoldDB; Q5U554; -.
DR SMR; Q5U554; -.
DR DNASU; 495366; -.
DR GeneID; 495366; -.
DR KEGG; xla:495366; -.
DR CTD; 495366; -.
DR Xenbase; XB-GENE-991117; tesc.L.
DR OMA; IFNMHDS; -.
DR OrthoDB; 1271942at2759; -.
DR Proteomes; UP000186698; Chromosome 1L.
DR Bgee; 495366; Expressed in stomach and 19 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 InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR SMART; SM00054; EFh; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
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_0000390719"
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:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 214 AA; 24826 MW; 38565CC6D3F5F571 CRC64;
MGLSHSHSVE TRELVEKTGF SAEQIEHLHK RFKSLSGDEP TIRRGHLNDI SDLVLNPIRS
KIIDAFFDKR NLRKGPSGYV EEINFEEFLI IMSYFRPLSQ HMDEENISVC RTDKLRFLFN
MYDSDNDNKI TLEEYRKVVE ELLSGNPNIE KEMARSIADG AMLEAASICV GQMEPDQVYE
GITFDDFLKI WEGIDIETKM HIRFLNMESI PSCR
