CAVP_BRAFL
ID CAVP_BRAFL Reviewed; 162 AA.
AC O01305;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Calcium vector protein;
DE Short=CAVP;
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Embryo;
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).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR EMBL; AB001689; BAA19429.1; -; mRNA.
DR EMBL; AB023073; BAA74697.1; -; Genomic_DNA.
DR EMBL; AB023072; BAA74696.1; -; Genomic_DNA.
DR EMBL; AB023071; BAA74695.1; -; Genomic_DNA.
DR AlphaFoldDB; O01305; -.
DR BMRB; O01305; -.
DR SMR; O01305; -.
DR STRING; 7739.XP_002598456.1; -.
DR eggNOG; KOG0027; Eukaryota.
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 2: Evidence at transcript level;
KW Acetylation; Calcium; Cytoplasm; Metal-binding; Methylation;
KW Muscle protein; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..162
FT /note="Calcium vector protein"
FT /id="PRO_0000073579"
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:0000250"
FT MOD_RES 96
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
FT MOD_RES 117
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 162 AA; 18338 MW; 3A543BF20C801044 CRC64;
MAAPKARALG PEEKDECMKI FDIFDRNAEN IAPVSDTMDM LTKLGQTYTK RETEAIMKEA
RGPKGDKKNL GPEEWLVLCS KWVRQDDEEE ILRAFKVFDA NGDGVIDFDE FKFIMQKVGE
EPLTDAEVEE AMKEADEDGN GVIDIPEFMD LIKKSKNALK EA
