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Database: UniProt
Entry: P63055
LinkDB: P63055
Original site: P63055 
ID   PCP4_RAT                Reviewed;          62 AA.
AC   P63055; P07734; Q63890;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=Calmodulin regulator protein PCP4 {ECO:0000305};
DE   AltName: Full=Brain-specific polypeptide PEP-19 {ECO:0000303|PubMed:2748608};
DE   AltName: Full=Purkinje cell protein 4 {ECO:0000312|RGD:3271};
GN   Name=Pcp4 {ECO:0000312|RGD:3271}; Synonyms=Pep19;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Brain;
RX   PubMed=2748608; DOI=10.1073/pnas.86.14.5651;
RA   Sangameswaran L., Hempstead J., Morgan J.I.;
RT   "Molecular cloning of a neuron-specific transcript and its regulation
RT   during normal and aberrant cerebellar development.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:5651-5655(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pituitary;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 2-62.
RC   TISSUE=Brain;
RX   PubMed=3464961; DOI=10.1073/pnas.83.21.8420;
RA   Ziai R., Pan Y.-C.E., Hulmes J.D., Sangameswaran L., Morgan J.I.;
RT   "Isolation, sequence, and developmental profile of a brain-specific
RT   polypeptide, PEP-19.";
RL   Proc. Natl. Acad. Sci. U.S.A. 83:8420-8423(1986).
CC   -!- FUNCTION: Functions as a modulator of calcium-binding by calmodulin.
CC       Thereby, regulates calmodulin activity and the different processes it
CC       controls. For instance, may play a role in neuronal differentiation
CC       through activation of calmodulin-dependent kinase signaling pathways.
CC       {ECO:0000250|UniProtKB:P48539}.
CC   -!- SUBUNIT: Binds to both calcium-free and calcium-bound calmodulin. The
CC       affinity for the calcium-bound form is 50-fold greater.
CC       {ECO:0000250|UniProtKB:P48539}.
CC   -!- TISSUE SPECIFICITY: Restricted to the nervous system. Expressed
CC       throughout the brain, in particular forebrain regions, including the
CC       granular layer of the olfactory bulb, and pyriform cortex. Also
CC       expressed in the hippocampus, caudate putamen and the cerebellum, where
CC       it is associated predominantly with Purkinje cells.
CC       {ECO:0000269|PubMed:2748608}.
CC   -!- DEVELOPMENTAL STAGE: Detectable in the brain at embryonic day 17. The
CC       levels increase to reach a maximal value at postnatal day 18.
CC       {ECO:0000269|PubMed:2748608}.
CC   -!- DOMAIN: Mostly intrinsically disordered, with residual structure
CC       localized to the IQ domain which mediates the interaction with
CC       calmodulin. {ECO:0000250|UniProtKB:P48539}.
CC   -!- SIMILARITY: Belongs to the PCP4 family. {ECO:0000305}.
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DR   EMBL; M24852; AAA41828.1; -; mRNA.
DR   EMBL; BC059147; AAH59147.1; -; mRNA.
DR   PIR; A33915; A33915.
DR   RefSeq; NP_037134.1; NM_013002.4.
DR   AlphaFoldDB; P63055; -.
DR   SMR; P63055; -.
DR   BioGRID; 247542; 1.
DR   STRING; 10116.ENSRNOP00000002221; -.
DR   PhosphoSitePlus; P63055; -.
DR   PaxDb; 10116-ENSRNOP00000002221; -.
DR   Ensembl; ENSRNOT00000061047.4; ENSRNOP00000057764.2; ENSRNOG00000001628.7.
DR   Ensembl; ENSRNOT00055028716; ENSRNOP00055023130; ENSRNOG00055016900.
DR   Ensembl; ENSRNOT00060037606; ENSRNOP00060031000; ENSRNOG00060021646.
DR   Ensembl; ENSRNOT00065022899; ENSRNOP00065017791; ENSRNOG00065013889.
DR   GeneID; 25510; -.
DR   KEGG; rno:25510; -.
DR   UCSC; RGD:3271; rat.
DR   AGR; RGD:3271; -.
DR   CTD; 5121; -.
DR   RGD; 3271; Pcp4.
DR   GeneTree; ENSGT00530000064267; -.
DR   HOGENOM; CLU_202697_1_0_1; -.
DR   InParanoid; P63055; -.
DR   OMA; FQIDMDA; -.
DR   OrthoDB; 5358936at2759; -.
DR   PRO; PR:P63055; -.
DR   Proteomes; UP000002494; Chromosome 11.
DR   Bgee; ENSRNOG00000001628; Expressed in cerebellum and 19 other cell types or tissues.
DR   ExpressionAtlas; P63055; baseline and differential.
DR   Genevisible; P63055; RN.
DR   GO; GO:0030424; C:axon; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005883; C:neurofilament; IDA:RGD.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0005516; F:calmodulin binding; IDA:RGD.
DR   GO; GO:0003723; F:RNA binding; IDA:RGD.
DR   GO; GO:0099004; P:calmodulin dependent kinase signaling pathway; ISS:UniProtKB.
DR   GO; GO:1905232; P:cellular response to L-glutamate; IEP:RGD.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:RGD.
DR   GO; GO:0001649; P:osteoblast differentiation; IEP:RGD.
DR   GO; GO:0033603; P:positive regulation of dopamine secretion; IMP:RGD.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR   PANTHER; PTHR15359:SF7; CALMODULIN REGULATOR PROTEIN PCP4; 1.
DR   PANTHER; PTHR15359; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
PE   1: Evidence at protein level;
KW   Calcium; Calmodulin-binding; Direct protein sequencing; Reference proteome.
FT   CHAIN           1..62
FT                   /note="Calmodulin regulator protein PCP4"
FT                   /id="PRO_0000058308"
FT   DOMAIN          39..62
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          1..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          28..40
FT                   /note="Acidic; binds calcium and is required for modulating
FT                   the calcium-binding kinetics of calmodulin"
FT                   /evidence="ECO:0000250|UniProtKB:P48539"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..38
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="Blocked amino end (Ser)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
SQ   SEQUENCE   62 AA;  6807 MW;  8DF93078A15EE79D CRC64;
     MSERQSAGAT NGKDKTSGDN DGQKKVQEEF DIDMDAPETE RAAVAIQSQF RKFQKKKAGS
     QS
//
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