CHP3_CHICK
ID CHP3_CHICK Reviewed; 214 AA.
AC A0AVX7;
DT 19-JAN-2010, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 64.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAL64631.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Layer {ECO:0000312|EMBL:CAL64631.1};
RX PubMed=15590942; DOI=10.1101/gr.3011405;
RA Hubbard S.J., Grafham D.V., Beattie K.J., Overton I.M., McLaren S.R.,
RA Croning M.D.R., Boardman P.E., Bonfield J.K., Burnside J., Davies R.M.,
RA Farrell E.R., Francis M.D., Griffiths-Jones S., Humphray S.J., Hyland C.,
RA Scott C.E., Tang H., Taylor R.G., Tickle C., Brown W.R.A., Birney E.,
RA Rogers J., Wilson S.A.;
RT "Transcriptome analysis for the chicken based on 19,626 finished cDNA
RT sequences and 485,337 expressed sequence tags.";
RL Genome Res. 15:174-183(2005).
RN [2] {ECO:0000305}
RP IDENTIFICATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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:0000269|PubMed:19345287}. Cytoplasm
CC {ECO:0000269|PubMed:19345287}. 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}. Note=Expressed in both the nucleus and
CC cytoplasm of the embryonic testis. {ECO:0000269|PubMed:19345287}.
CC -!- TISSUE SPECIFICITY: Expressed in the bipotential gonad by E4.5 and
CC expressed in both the testis and ovary by E5.5, but with expression
CC higher in the testis. Expressed in the testis cords but also at low
CC levels in the interstitium. In the ovary, expression is principally in
CC the ovarian cortex, but also in the medulla. Also expressed in the
CC embryonic brain, with expression highest in the region between the
CC nasal placode and olfactory bulb. Also expressed in the embryonic heart
CC and tail. {ECO:0000269|PubMed:19345287}.
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; BX931037; CAL64631.1; -; mRNA.
DR RefSeq; NP_001074353.1; NM_001080884.2.
DR AlphaFoldDB; A0AVX7; -.
DR SMR; A0AVX7; -.
DR STRING; 9031.ENSGALP00000013348; -.
DR GeneID; 771113; -.
DR KEGG; gga:771113; -.
DR CTD; 54997; -.
DR VEuPathDB; HostDB:geneid_771113; -.
DR eggNOG; KOG0034; Eukaryota.
DR InParanoid; A0AVX7; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; A0AVX7; -.
DR PRO; PR:A0AVX7; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA: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 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_0000390718"
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 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:0000250"
SQ SEQUENCE 214 AA; 25051 MW; 08C6EB137EFF3124 CRC64;
MGSAQSVPPE MRALAERTGF TSEQIEQLHR RFKQLNHNRK TIRKEDFDTI PDLEFNPIRA
RIVHAFFDKR NLRKAPAGLA EEINFEDFLT IMSYFRPIEM DMDEERLESF RKEKLKFLFH
MYDADYDGII TLQEYKNVLD ELMSGNPHLE KESLRAIAEG AMLEAASACM ARTGPDEVYE
GITFEDFLKV WKGIDIETKM HVRFLTMEAI AHCY
