S10A1_MISFO
ID S10A1_MISFO Reviewed; 95 AA.
AC Q7LZT1;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein S100-A1;
DE AltName: Full=S-100 protein alpha chain;
DE AltName: Full=S-100 protein subunit alpha;
DE AltName: Full=S100 calcium-binding protein A1;
GN Name=s100a1;
OS Misgurnus fossilis (Weatherfish) (Cobitis fossilis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cobitidae; Cobitinae; Misgurnus.
OX NCBI_TaxID=7984;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Egg;
RX PubMed=8217841; DOI=10.1016/0925-4773(93)90004-h;
RA Ivanenkov V.V., Gerke V., Minin A.A., Plessmann U., Weber K.;
RT "Transduction of Ca(2+) signals upon fertilization of eggs; identification
RT of an S-100 protein as a major Ca(2+)-binding protein.";
RL Mech. Dev. 42:151-158(1993).
CC -!- FUNCTION: Small calcium binding protein that plays important roles in
CC several biological processes such as Ca(2+) homeostasis, chondrocyte
CC biology and cardiomyocyte regulation. In response to an increase in
CC intracellular Ca(2+) levels, binds calcium which triggers
CC conformational changes. These changes allow interactions with specific
CC target proteins and modulate their activity. Regulates a network in
CC cardiomyocytes controlling sarcoplasmic reticulum Ca(2+) cycling and
CC mitochondrial function through interaction with the ryanodine receptors
CC RYR1 and RYR2, sarcoplasmic reticulum Ca(2+)-ATPase/ATP2A2 and
CC mitochondrial F1-ATPase. Facilitates diastolic Ca(2+) dissociation and
CC myofilament mechanics in order to improve relaxation during diastole.
CC {ECO:0000250|UniProtKB:P23297}.
CC -!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one
CC alpha and one beta chain. Also forms heterodimers with S100P (By
CC similarity). Interacts with AGER (By similarity). Interacts with CAPZA1
CC (By similarity). Interacts with FKBP4. Interacts with RYR1 and RYR2.
CC Interacts with CACYBP in a calcium-dependent manner. Interacts with
CC PPP5C (via TPR repeats); the interaction is calcium-dependent and
CC modulates PPP5C activity. Interacts with ATP2A2 and PLN in a Ca(2+)-
CC dependent manner (By similarity). Interacts with mitochondrial F1-
CC ATPase subunits ATP5F1A and ATP5F1B; these interactions increase F1-
CC ATPase activity (By similarity). {ECO:0000250|UniProtKB:P23297,
CC ECO:0000250|UniProtKB:P35467, ECO:0000250|UniProtKB:P56565}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23297}.
CC Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P23297}. Mitochondrion
CC {ECO:0000250|UniProtKB:P56565}.
CC -!- PTM: Glutathionylated; glutathionylation increases affinity to calcium
CC about 10-fold. {ECO:0000250|UniProtKB:P23297}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR PIR; S35985; S35985.
DR AlphaFoldDB; Q7LZT1; -.
DR SMR; Q7LZT1; -.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell.
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 InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF01023; S_100; 1.
DR SMART; SM00054; EFh; 1.
DR SMART; SM01394; S_100; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS00303; S100_CABP; 1.
PE 1: Evidence at protein level;
KW Calcium; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Mitochondrion; Repeat; Sarcoplasmic reticulum; Zinc.
FT CHAIN 1..95
FT /note="Protein S100-A1"
FT /id="PRO_0000143964"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 49..84
FT /note="EF-hand 2"
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 /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P35467"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /ligand_note="low affinity"
FT /evidence="ECO:0000250|UniProtKB:P35467"
FT BINDING 62
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 64
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
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 /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 73
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /ligand_note="high affinity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
SQ SEQUENCE 95 AA; 10672 MW; 0AC884EB75993A9E CRC64;
VSQLESAMES LIKVFHTYSS KEGDKYKLSK AELKSLLQGE LNDFLSASKD PMVVEKIMSD
LDENQDGEVD FQEFVVLVAA LTVACNEFFI ESMKN
