CALU_RABIT
ID CALU_RABIT Reviewed; 315 AA.
AC Q6XLQ7; Q6XLQ6;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Calumenin;
DE Flags: Precursor;
GN Name=CALU;
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], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH RYR1, AND TISSUE SPECIFICITY.
RC TISSUE=Heart muscle, and Skeletal muscle;
RX PubMed=16527250; DOI=10.1016/j.bbrc.2006.02.115;
RA Jung D.H., Mo S.H., Kim D.H.;
RT "Calumenin, a multiple EF-hands Ca2+-binding protein, interacts with
RT ryanodine receptor-1 in rabbit skeletal sarcoplasmic reticulum.";
RL Biochem. Biophys. Res. Commun. 343:34-42(2006).
CC -!- FUNCTION: Involved in regulation of vitamin K-dependent carboxylation
CC of multiple N-terminal glutamate residues. Seems to inhibit gamma-
CC carboxylase GGCX. Binds 7 calcium ions with a low affinity (By
CC similarity). May modulate calcium release from the sarcoplasmic
CC reticulum. {ECO:0000250, ECO:0000269|PubMed:16527250}.
CC -!- SUBUNIT: Interacts with GGCX (By similarity). Interacts with RYR1 in
CC the presence of calcium ions, but not in the presence of EDTA.
CC {ECO:0000250, ECO:0000269|PubMed:16527250}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:O43852}. Golgi apparatus
CC {ECO:0000250|UniProtKB:O43852}. Secreted
CC {ECO:0000250|UniProtKB:O43852}. Melanosome
CC {ECO:0000250|UniProtKB:O43852}. Sarcoplasmic reticulum lumen
CC {ECO:0000269|PubMed:16527250}.
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:16527250}.
CC -!- SIMILARITY: Belongs to the CREC family. {ECO:0000305}.
CC -!- CAUTION: PubMed:16527250 attributed the differences between their
CC clones to the existence of two separate genes. This seems rather
CC unlikely, considering that the cDNAs are 100% identical outside of this
CC clearly delimited zone. {ECO:0000305}.
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DR EMBL; AY225335; AAO47344.1; -; mRNA.
DR EMBL; AY225336; AAO47345.1; -; mRNA.
DR RefSeq; NP_001075623.1; NM_001082154.1.
DR RefSeq; NP_001076203.1; NM_001082734.1.
DR RefSeq; XP_008256389.1; XM_008258167.2.
DR RefSeq; XP_008256390.1; XM_008258168.2.
DR AlphaFoldDB; Q6XLQ7; -.
DR STRING; 9986.ENSOCUP00000018782; -.
DR GeneID; 100008903; -.
DR KEGG; ocu:100008903; -.
DR CTD; 813; -.
DR eggNOG; KOG4223; Eukaryota.
DR InParanoid; Q6XLQ7; -.
DR OrthoDB; 909079at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0033018; C:sarcoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR InterPro; IPR027239; Calumenin.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR10827:SF76; PTHR10827:SF76; 1.
DR Pfam; PF13202; EF-hand_5; 2.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 6.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Endoplasmic reticulum; Glycoprotein; Golgi apparatus;
KW Membrane; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Sarcoplasmic reticulum; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..315
FT /note="Calumenin"
FT /id="PRO_0000364192"
FT DOMAIN 68..103
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 104..139
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 151..186
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 188..223
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 229..264
FT /note="EF-hand 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 265..300
FT /note="EF-hand 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOTIF 312..315
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 83
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 85
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 92
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 117
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 121
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 128
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 166
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 168
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 175
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000305"
FT BINDING 201
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 203
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 242
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000305"
FT BINDING 244
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000305"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000305"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000305"
FT BINDING 253
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="5"
FT /evidence="ECO:0000305"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 289
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 44
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43852"
FT MOD_RES 47
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O43852"
FT MOD_RES 65
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43852"
FT MOD_RES 69
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43852"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35887"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O43852"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43852"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43852"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 75
FT /note="K -> M (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="S -> D (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..84
FT /note="ADK -> GDD (in Ref. 1; AAO47344)"
FT /evidence="ECO:0000305"
FT CONFLICT 90..91
FT /note="VD -> EG (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 95
FT /note="D -> S (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="F -> H (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 103..104
FT /note="RW -> KY (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 107..108
FT /note="ED -> DN (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 111..120
FT /note="RQWKGHDLNE -> NQWQEFDMNQ (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="V -> I (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="E -> D (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 130..132
FT /note="KNA -> RNV (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
FT CONFLICT 136..137
FT /note="YV -> TY (in Ref. 1; AAO47345)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 315 AA; 37078 MW; E2CC4EAD0CFA31FB CRC64;
MDLRQFLMCL SLCTAFALSK PTEKKDRVHH EPQLSDKVHD DAQSFDYDHD AFLGAEEAKT
FDQLTPEESK ERLGKIVSKI DADKDGFVTV DELKDWIKFA QKRWIYEDVE RQWKGHDLNE
DGLVSWEEYK NATYGYVLDD PDPDDGFNYK QMMVRDERRF KMADKDGDLI ATKEEFTAFL
HPEEYDYMKD IVVQETMEDI DKNGDGFIDL EEYIGDMYSH DGNADEPEWV KTEREQFVEF
RDKNRDGKMD KEETKDWILP SDYDHAEAEA RHLVYESDQN KDGKLTKEEI VDKYDLFVGS
QATDFGEALV RHDEF
