CAVP_BRALA
ID CAVP_BRALA Reviewed; 162 AA.
AC P04573; O01308;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Calcium vector protein;
DE Short=CAVP;
OS Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7740;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SEQUENCE REVISION TO 154-155.
RX PubMed=10467174; DOI=10.1093/oxfordjournals.jbchem.a022488;
RA Yuasa H.J., Cox J.A., Takagi T.;
RT "Genomic structure of the amphioxus calcium vector protein.";
RL J. Biochem. 126:572-577(1999).
RN [2]
RP PROTEIN SEQUENCE OF 2-162, ACETYLATION AT ALA-2, AND METHYLATION AT LYS-96
RP AND LYS-117.
RX PubMed=3818612; DOI=10.1016/s0021-9258(18)61550-9;
RA Kobayashi T., Takagi T., Konishi K., Cox J.A.;
RT "The primary structure of a new Mr 18,000 calcium vector protein from
RT amphioxus.";
RL J. Biol. Chem. 262:2613-2623(1987).
RN [3]
RP STRUCTURE BY NMR OF 82-161, AND CALCIUM-BINDING.
RX PubMed=10891072; DOI=10.1021/bi000360z;
RA Theret I., Baladi S., Cox J.A., Sakamoto H., Craescu C.T.;
RT "Sequential calcium binding to the regulatory domain of calcium vector
RT protein reveals functional asymmetry and a novel mode of structural
RT rearrangement.";
RL Biochemistry 39:7920-7926(2000).
RN [4]
RP STRUCTURE BY NMR OF 2-86, ABSENCE OF CALCIUM-BINDING, AND ABSENCE OF
RP DISULFIDE BOND.
RX PubMed=11705378; DOI=10.1021/bi011444q;
RA Theret I., Baladi S., Cox J.A., Gallay J., Sakamoto H., Craescu C.T.;
RT "Solution structure and backbone dynamics of the defunct domain of calcium
RT vector protein.";
RL Biochemistry 40:13888-13897(2001).
CC -!- FUNCTION: The exact function of this protein is not yet known. It
CC interacts with CAVPT, a protein also of unknown function, in a calcium-
CC dependent way. This protein binds two calcium ions.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- CAUTION: Was originally thought to have an internal disulfide bond.
CC {ECO:0000305|PubMed:3818612}.
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DR EMBL; AB001688; BAA19428.1; -; mRNA.
DR PIR; A29557; A29557.
DR PIR; JC7157; JC7157.
DR PDB; 1C7V; NMR; -; A=82-162.
DR PDB; 1C7W; NMR; -; A=82-162.
DR PDB; 1J7Q; NMR; -; A=2-87.
DR PDB; 1J7R; NMR; -; A=2-87.
DR PDBsum; 1C7V; -.
DR PDBsum; 1C7W; -.
DR PDBsum; 1J7Q; -.
DR PDBsum; 1J7R; -.
DR AlphaFoldDB; P04573; -.
DR BMRB; P04573; -.
DR SMR; P04573; -.
DR iPTMnet; P04573; -.
DR PRIDE; P04573; -.
DR EnsemblMetazoa; BL01156_evm4; BL01156_evm4; BL01156.
DR EvolutionaryTrace; P04573; -.
DR Bgee; BL01156; Expressed in muscle tissue and 9 other tissues.
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; 1.
DR SMART; SM00054; EFh; 2.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Calcium; Cytoplasm; Direct protein sequencing;
KW Metal-binding; Methylation; Muscle protein; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3818612"
FT CHAIN 2..162
FT /note="Calcium vector protein"
FT /id="PRO_0000073578"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 49..84
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 86..121
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 123..158
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 99
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 101
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 103
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 110
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 138
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:3818612"
FT MOD_RES 96
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:3818612"
FT MOD_RES 117
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000269|PubMed:3818612"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:1J7R"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:1J7Q"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:1J7Q"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:1J7Q"
FT HELIX 50..61
FT /evidence="ECO:0007829|PDB:1J7Q"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:1J7Q"
FT HELIX 89..98
FT /evidence="ECO:0007829|PDB:1C7V"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1C7V"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:1C7V"
FT TURN 117..120
FT /evidence="ECO:0007829|PDB:1C7V"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:1C7V"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:1C7V"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:1C7V"
FT HELIX 145..153
FT /evidence="ECO:0007829|PDB:1C7V"
SQ SEQUENCE 162 AA; 18356 MW; D26139A009D6A042 CRC64;
MAAPKARALG PEEKDECMKI FDIFDRNAEN IAPVSDTMDM LTKLGQTYTK RETEAIMKEA
RGPKGDKKNI GPEEWLTLCS KWVRQDDEEE ILRAFKVFDA NGDGVIDFDE FKFIMQKVGE
EPLTDAEVEE AMKEADEDGN GVIDIPEFMD LIKKSKNALK ES
