CAYP1_RABIT
ID CAYP1_RABIT Reviewed; 189 AA.
AC P41150;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Calcyphosin;
DE AltName: Full=Calcyphosine;
DE AltName: Full=R2D5 antigen;
GN Name=CAPS;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 52-63; 104-149 AND 153-168,
RP FUNCTION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC STRAIN=Japanese white; TISSUE=Olfactory epithelium;
RX PubMed=8227152; DOI=10.1083/jcb.123.4.963;
RA Nemoto Y., Ikeda J., Katoh K., Koshimoto H., Yoshihara Y., Mori K.;
RT "R2D5 antigen: a calcium-binding phosphoprotein predominantly expressed in
RT olfactory receptor neurons.";
RL J. Cell Biol. 123:963-976(1993).
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: Abundant in the olfactory epithelium and the
CC olfactory bulb. Low levels are seen in nasal respiratory epithelium,
CC lung, kidney, cerebrum, cerebellum, brain stem, thyroid gland, heart
CC and stomach. {ECO:0000269|PubMed:8227152}.
CC -!- PTM: Phosphorylated in vitro by CaM-kinase II and CAPK.
CC {ECO:0000269|PubMed:8227152}.
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DR EMBL; X72874; CAA51388.1; -; mRNA.
DR PIR; A49020; A49020.
DR RefSeq; NP_001076113.1; NM_001082644.1.
DR AlphaFoldDB; P41150; -.
DR SMR; P41150; -.
DR GeneID; 100009340; -.
DR KEGG; ocu:100009340; -.
DR CTD; 828; -.
DR InParanoid; P41150; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; 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; Direct protein sequencing; Metal-binding;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..189
FT /note="Calcyphosin"
FT /id="PRO_0000073539"
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 38
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000255"
FT MOD_RES 40
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 74
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000255"
SQ SEQUENCE 189 AA; 20865 MW; 453B99F31538FE07 CRC64;
MDTADAIVEK LRAQCLARGA AGIQGLARFF RRLDRDGSRS LDAGELRQGL AKLGLALDEA
EAQSVCRRWD RNGSGTLDLE EFLRALRPPM SQAREAVIAA AFAKLDRSGD GVVTLGDLRG
VYSGRNHPKV RTGEWTEDEV LRRFLDNFDS SEKDGQVTLA EFQDYYSGLS ASVDTDEEFV
AMMSSAWQL
