CHP1_CHICK
ID CHP1_CHICK Reviewed; 195 AA.
AC Q5ZM44;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Calcineurin B homologous protein 1;
DE AltName: Full=Calcineurin B-like protein;
DE AltName: Full=Calcium-binding protein CHP;
DE AltName: Full=Calcium-binding protein p22;
DE AltName: Full=EF-hand calcium-binding domain-containing protein p22;
GN Name=CHP1; Synonyms=CHP; ORFNames=RCJMB04_3d7;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
RN [2]
RP FUNCTION, AND MUTAGENESIS OF GLY-2; GLU-134 AND GLU-175.
RX PubMed=17392381; DOI=10.1152/ajpcell.00464.2006;
RA Matsushita M., Sano Y., Yokoyama S., Takai T., Inoue H., Mitsui K.,
RA Todo K., Ohmori H., Kanazawa H.;
RT "Loss of calcineurin homologous protein-1 in chicken B lymphoma DT40 cells
RT destabilizes Na+/H+ exchanger isoform-1 protein.";
RL Am. J. Physiol. 293:C246-C254(2007).
CC -!- FUNCTION: Calcium-binding protein involved in different processes such
CC as regulation of vesicular trafficking, plasma membrane Na(+)/H(+)
CC exchanger and gene transcription. Involved in the constitutive exocytic
CC membrane traffic. Mediates the association between microtubules and
CC membrane-bound organelles of the endoplasmic reticulum and Golgi
CC apparatus and is also required for the targeting and fusion of
CC transcytotic vesicles (TCV) with the plasma membrane. Functions as an
CC integral cofactor in cell pH regulation by controlling plasma membrane-
CC type Na(+)/H(+) exchange activity. Inhibits serum- and GTPase-
CC stimulated Na(+)/H(+) exchange. Plays a role as an inhibitor of
CC ribosomal RNA transcription. Acts as a negative regulator of the
CC calcineurin/NFAT signaling pathway. {ECO:0000269|PubMed:17392381}.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P61023}. Cytoplasm
CC {ECO:0000250|UniProtKB:P61023}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P61023}. Endomembrane system
CC {ECO:0000250|UniProtKB:P61023}. Endoplasmic reticulum-Golgi
CC intermediate compartment {ECO:0000250|UniProtKB:P61023}. Endoplasmic
CC reticulum {ECO:0000250|UniProtKB:P61023}. Cell membrane
CC {ECO:0000250|UniProtKB:P61023}. Membrane
CC {ECO:0000250|UniProtKB:Q99653}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q99653}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
CC -!- PTM: Calcium-binding or N-myristoylation are necessary for the
CC Na(+)/H(+) exchange activities.
CC -!- SIMILARITY: Belongs to the calcineurin regulatory subunit family. CHP
CC subfamily. {ECO:0000305}.
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DR EMBL; AJ719540; CAG31199.1; -; mRNA.
DR RefSeq; NP_001007931.1; NM_001007930.1.
DR AlphaFoldDB; Q5ZM44; -.
DR SMR; Q5ZM44; -.
DR BioGRID; 683765; 1.
DR IntAct; Q5ZM44; 1.
DR STRING; 9031.ENSGALP00000032005; -.
DR PaxDb; Q5ZM44; -.
DR Ensembl; ENSGALT00000032642; ENSGALP00000032005; ENSGALG00000008569.
DR Ensembl; ENSGALT00000066791; ENSGALP00000056837; ENSGALG00000008569.
DR GeneID; 423211; -.
DR KEGG; gga:423211; -.
DR CTD; 11261; -.
DR VEuPathDB; HostDB:geneid_423211; -.
DR eggNOG; KOG0034; Eukaryota.
DR GeneTree; ENSGT00940000154629; -.
DR HOGENOM; CLU_061288_10_5_1; -.
DR InParanoid; Q5ZM44; -.
DR OMA; HSFFADS; -.
DR OrthoDB; 1271942at2759; -.
DR PhylomeDB; Q5ZM44; -.
DR TreeFam; TF354284; -.
DR Reactome; R-GGA-2160916; Hyaluronan uptake and degradation.
DR PRO; PR:Q5ZM44; -.
DR Proteomes; UP000000539; Chromosome 5.
DR Bgee; ENSGALG00000008569; Expressed in spermatid and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:UniProtKB.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; ISS:UniProtKB.
DR GO; GO:0022406; P:membrane docking; ISS:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; ISS:UniProtKB.
DR GO; GO:0061024; P:membrane organization; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0070885; P:negative regulation of calcineurin-NFAT signaling cascade; ISS:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; ISS:UniProtKB.
DR GO; GO:0031953; P:negative regulation of protein autophosphorylation; ISS:UniProtKB.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; ISS:UniProtKB.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0060050; P:positive regulation of protein glycosylation; ISS:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0051222; P:positive regulation of protein transport; ISS:UniProtKB.
DR GO; GO:0032417; P:positive regulation of sodium:proton antiporter activity; IMP:UniProtKB.
DR GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; IDA:UniProtKB.
DR GO; GO:0051453; P:regulation of intracellular pH; ISS:UniProtKB.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Calcium; Cell membrane; Cytoplasm; Cytoskeleton; Endoplasmic reticulum;
KW Lipoprotein; Membrane; Metal-binding; Myristate; Nucleus; Phosphoprotein;
KW Protein kinase inhibitor; Protein transport; Reference proteome; Repeat;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..195
FT /note="Calcineurin B homologous protein 1"
FT /id="PRO_0000073847"
FT DOMAIN 26..61
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 66..101
FT /note="EF-hand 2"
FT /evidence="ECO:0000305"
FT DOMAIN 110..145
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 151..186
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 123
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 125
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 127
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 129
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT MUTAGEN 2
FT /note="G->A: Reduces SLC9A1/NHE1 stability. Does not reduce
FT Na(+)/H(+) SLC9A1/NHE1 exchange activities."
FT /evidence="ECO:0000269|PubMed:17392381"
FT MUTAGEN 134
FT /note="E->A: Reduces SLC9A1/NHE1 stability and Na(+)/H(+)
FT exchange activities; when associated with A-175."
FT /evidence="ECO:0000269|PubMed:17392381"
FT MUTAGEN 175
FT /note="E->A: Reduces SLC9A1/NHE1 stability and Na(+)/H(+)
FT exchange activities; when associated with A-134."
FT /evidence="ECO:0000269|PubMed:17392381"
SQ SEQUENCE 195 AA; 22447 MW; 3DB74EA4AEF2299C CRC64;
MGSRASTLLR DEEIEEIKKE TGFSHSQITR LYSRFTSLDK GENGTLSRED FQRIPELAIN
PLGDRIINAF FSEGEDQVNF RGFMRTLAHF RPIEDNEKSK DQNGPEPLNS RSNKLHFAFR
LYDLDKDDKI SRDELLQVLR MMVGVNISDE QLGSIADRTI QEADQDGDCA ISFAEFVKVL
EKVDVEQKMS IRFLH
