SCP2_BRALA
ID SCP2_BRALA Reviewed; 185 AA.
AC P04570;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Sarcoplasmic calcium-binding proteins II, V, VI, and VII;
DE Short=SCP II;
DE Short=SCP V;
DE Short=SCP VI;
DE Short=SCP VII;
OS Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomidae; Branchiostoma.
OX NCBI_TaxID=7740;
RN [1]
RP PROTEIN SEQUENCE.
RA Takagi T., Konishi K., Cox J.A.;
RT "Amino acid sequence of two sarcoplasmic calcium-binding proteins from the
RT protochordate amphioxus.";
RL Biochemistry 25:3585-3592(1986).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=2209593; DOI=10.1111/j.1432-1033.1990.tb19239.x;
RA Takagi T., Cox J.A.;
RT "Amino acid sequences of four isoforms of amphioxus sarcoplasmic calcium-
RT binding proteins.";
RL Eur. J. Biochem. 192:387-399(1990).
RN [3]
RP PROTEIN SEQUENCE (SCP V TO VII).
RX PubMed=1633848; DOI=10.1016/0014-5793(92)80429-k;
RA Takagi T., Valette-Talbi L., Cox J.A.;
RT "Primary structure of three minor isoforms of amphioxus sarcoplasmic
RT calcium-binding proteins.";
RL FEBS Lett. 302:159-160(1992).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
RX PubMed=8429557; DOI=10.1006/jmbi.1993.1046;
RA Cook W.J., Jeffrey L.C., Cox J.A., Vijay-Kumar S.;
RT "Structure of a sarcoplasmic calcium-binding protein from amphioxus refined
RT at 2.4-A resolution.";
RL J. Mol. Biol. 229:461-471(1993).
CC -!- FUNCTION: Like parvalbumins, SCPs seem to be more abundant in fast
CC contracting muscles, but no functional relationship can be established
CC from this distribution.
CC -!- MISCELLANEOUS: The sarcoplasmic calcium-binding proteins are abundant
CC in the muscle of arthropods, mollusks, annelids, and protochordates.
CC -!- MISCELLANEOUS: This protein has three functional calcium-binding sites;
CC potential site 4 has lost affinity for calcium.
CC -!- MISCELLANEOUS: There are 7 different SCP's in amphioxus. The sequence
CC shown here is that of SCP II.
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DR PIR; S13183; S13183.
DR PIR; S21153; S21153.
DR PDB; 2SAS; X-ray; 2.40 A; A=1-185.
DR PDBsum; 2SAS; -.
DR AlphaFoldDB; P04570; -.
DR SMR; P04570; -.
DR EvolutionaryTrace; P04570; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Direct protein sequencing; Metal-binding;
KW Muscle protein; Repeat.
FT CHAIN 1..185
FT /note="Sarcoplasmic calcium-binding proteins II, V, VI, and
FT VII"
FT /id="PRO_0000073633"
FT DOMAIN 5..41
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 102..137
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 138..173
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 19
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
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 30
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 81
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 115
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 BINDING 119
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 126
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT VARIANT 25
FT /note="S -> A (in SCP V)"
FT VARIANT 28
FT /note="D -> W (in SCP V, VI and VII)"
FT VARIANT 29
FT /note="N -> E (in SCP VI)"
FT HELIX 4..17
FT /evidence="ECO:0007829|PDB:2SAS"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:2SAS"
FT HELIX 28..42
FT /evidence="ECO:0007829|PDB:2SAS"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:2SAS"
FT HELIX 48..69
FT /evidence="ECO:0007829|PDB:2SAS"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:2SAS"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2SAS"
FT HELIX 103..114
FT /evidence="ECO:0007829|PDB:2SAS"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2SAS"
FT HELIX 124..130
FT /evidence="ECO:0007829|PDB:2SAS"
FT HELIX 141..149
FT /evidence="ECO:0007829|PDB:2SAS"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:2SAS"
FT HELIX 158..170
FT /evidence="ECO:0007829|PDB:2SAS"
FT HELIX 176..181
FT /evidence="ECO:0007829|PDB:2SAS"
SQ SEQUENCE 185 AA; 21286 MW; 76E3307B55C7595B CRC64;
GLNDFQKQKI KFTFDFFLDM NHDGSIQDND FEDMMTRYKE VNKGSLSDAD YKSMQASLED
EWRDLKGRAD INKDDVVSWE EYLAMWEKTI ATCKSVADLP AWCQNRIPFL FKGMDVSGDG
IVDLEEFQNY CKNFQLQCAD VPAVYNVITD GGKVTFDLNR YKELYYRLLT SPAADAGNTL
MGQKP