CALM_RABIT
ID CALM_RABIT Reviewed; 149 AA.
AC P62160; P02593; P70667; P99014; Q61379; Q61380;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Calmodulin;
DE Short=CaM;
GN Name=CALM; Synonyms=CAM;
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 PROTEIN SEQUENCE OF 2-149, AND METHYLATION AT LYS-116.
RC TISSUE=Skeletal muscle;
RX PubMed=7202416; DOI=10.1111/j.1432-1033.1981.tb05074.x;
RA Grand R.J.A., Shenolikar S., Cohen P.;
RT "The amino acid sequence of the delta subunit (calmodulin) of rabbit
RT skeletal muscle phosphorylase kinase.";
RL Eur. J. Biochem. 113:359-367(1981).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels, aquaporins and other proteins by Ca(2+). Among the
CC enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number
CC of protein kinases and phosphatases. Together with CCP110 and centrin,
CC is involved in a genetic pathway that regulates the centrosome cycle
CC and progression through cytokinesis (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CEP97, CCP110, TTN/titin and SRY. Interacts
CC with MYO5A and RRAD (By similarity). Interacts with USP6; the
CC interaction is calcium dependent (By similarity). Interacts with
CC CDK5RAP2. Interacts with SCN5A. Interacts with RYR1 and RYR2 (By
CC similarity). Interacts with FCHO1. Interacts with MIP in a 1:2
CC stoichiometry; the interaction with the cytoplasmic domains from two
CC MIP subunits promotes MIP water channel closure. Interacts with ORAI1;
CC this may play a role in the regulation of ORAI1-mediated calcium
CC transport. Interacts with SYT7 (By similarity). Interacts with MYO10
CC and MYO1C (By similarity). Interacts with SLC9A1 in a calcium-dependent
CC manner (By similarity). Interacts with HINT1; interaction increases in
CC the presence of calcium ions (By similarity). Interacts with HINT3 (By
CC similarity). {ECO:0000250|UniProtKB:P0DP23,
CC ECO:0000250|UniProtKB:P0DP26, ECO:0000250|UniProtKB:P62157,
CC ECO:0000250|UniProtKB:P62158, ECO:0000250|UniProtKB:P62204}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle pole {ECO:0000250}. Note=Distributed
CC throughout the cell during interphase, but during mitosis becomes
CC dramatically localized to the spindle poles and the spindle
CC microtubules. {ECO:0000250}.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Ubiquitination results in a strongly decreased activity.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation results in a decreased activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR PIR; A91104; MCRB.
DR RefSeq; NP_001182569.1; NM_001195640.1.
DR RefSeq; XP_008270147.1; XM_008271925.2.
DR AlphaFoldDB; P62160; -.
DR SMR; P62160; -.
DR DIP; DIP-48335N; -.
DR IntAct; P62160; 4.
DR STRING; 9986.ENSOCUP00000001814; -.
DR Ensembl; ENSOCUT00000002104; ENSOCUP00000001814; ENSOCUG00000002107.
DR Ensembl; ENSOCUT00000011656; ENSOCUP00000010025; ENSOCUG00000011659.
DR GeneID; 100350107; -.
DR GeneID; 100352392; -.
DR KEGG; ocu:100350107; -.
DR KEGG; ocu:100352392; -.
DR CTD; 801; -.
DR CTD; 805; -.
DR eggNOG; KOG0027; Eukaryota.
DR GeneTree; ENSGT00950000182980; -.
DR HOGENOM; CLU_061288_2_0_1; -.
DR InParanoid; P62160; -.
DR OMA; SCDRHPP; -.
DR OrthoDB; 1386217at2759; -.
DR TreeFam; TF300912; -.
DR Proteomes; UP000001811; Chromosome 2.
DR Proteomes; UP000001811; Chromosome 20.
DR Bgee; ENSOCUG00000002107; Expressed in prefrontal cortex and 15 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00051; EFh; 2.
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; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Isopeptide bond; Metal-binding; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7202416"
FT CHAIN 2..149
FT /note="Calmodulin"
FT /id="PRO_0000198226"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 117..149
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P62157, ECO:0000305"
FT MOD_RES 22
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 45
FT /note="Phosphothreonine; by CaMK4"
FT /evidence="ECO:0000250|UniProtKB:P0DP29"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 100
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000269|PubMed:7202416"
FT MOD_RES 116
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP23"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62157"
SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK
