CAYP1_CANLF
ID CAYP1_CANLF Reviewed; 189 AA.
AC P10463;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Calcyphosin;
DE AltName: Full=Calcyphosine;
DE AltName: Full=Protein 5;
DE AltName: Full=Thyroid protein p24;
DE Short=TPP;
GN Name=CAPS;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CALCIUM-BINDING, PHOSPHORYLATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=2540953; DOI=10.1002/j.1460-2075.1989.tb03354.x;
RA Lefort A., Lecocq R., Libert F., Lamy F., Swillens S., Vassart G.,
RA Dumont J.E.;
RT "Cloning and sequencing of a calcium-binding protein regulated by cyclic
RT AMP in the thyroid.";
RL EMBO J. 8:111-116(1989).
CC -!- FUNCTION: Calcium-binding protein. May play a role in cellular
CC signaling events (Potential). {ECO:0000305}.
CC -!- SUBUNIT: Monomer. Does not form oligomers in the presence of calcium
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Detected in thyroid, salivary gland, lung, brain
CC and cerebellum (at protein level). {ECO:0000269|PubMed:2540953}.
CC -!- PTM: Phosphorylated in response to thyrotropin and cAMP.
CC {ECO:0000269|PubMed:2540953}.
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DR EMBL; X14479; CAA32641.1; -; mRNA.
DR EMBL; X14047; CAA32205.1; -; mRNA.
DR PIR; S03635; S03635.
DR RefSeq; NP_001003282.1; NM_001003282.1.
DR AlphaFoldDB; P10463; -.
DR SMR; P10463; -.
DR STRING; 9612.ENSCAFP00000027658; -.
DR PaxDb; P10463; -.
DR Ensembl; ENSCAFT00000029761; ENSCAFP00000027658; ENSCAFG00000018746.
DR Ensembl; ENSCAFT00040046870; ENSCAFP00040040913; ENSCAFG00040025138.
DR Ensembl; ENSCAFT00845021759; ENSCAFP00845017110; ENSCAFG00845012225.
DR GeneID; 403965; -.
DR KEGG; cfa:403965; -.
DR CTD; 828; -.
DR VEuPathDB; HostDB:ENSCAFG00845012225; -.
DR VGNC; VGNC:54265; CAPS.
DR eggNOG; KOG0032; Eukaryota.
DR GeneTree; ENSGT00940000162442; -.
DR InParanoid; P10463; -.
DR OrthoDB; 1377102at2759; -.
DR Proteomes; UP000002254; Chromosome 20.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Metal-binding; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..189
FT /note="Calcyphosin"
FT /id="PRO_0000073537"
FT DOMAIN 21..56
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 57..92
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 93..128
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 136..172
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 36
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 38
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 45
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 74
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 76
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 106
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 108
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 40
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
SQ SEQUENCE 189 AA; 21132 MW; D49CD36C8F1EB65A CRC64;
MDAVDATVEK LRAQCLSRGA LGIQGLARFF RRLDRDRSRS LDSRELQRGL AELGLVLDTA
EAEGVCRRWD RDGSGTLDLE EFLRALRPPM SQAREAVIAA AFAKLDRSGD GVVTVDDLRG
VYSGRTHPKV QSGEWTEEEV LRRFLDNFDS SEKDGQVTLA EFQDYYSGVS ASMDTDEEFV
AMMTSAWQL
