S10A1_BOVIN
ID S10A1_BOVIN Reviewed; 94 AA.
AC P02639; A5PJ73;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 165.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=3755105; DOI=10.1016/0014-5793(86)80656-1;
RA Kuwano R., Maeda T., Usui H., Araki K., Yamakuni T., Ohshima Y.,
RA Kurihara T., Takahashi Y.;
RT "Molecular cloning of cDNA of S100 alpha subunit mRNA.";
RL FEBS Lett. 202:97-101(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal cerebellum, and Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-94.
RX PubMed=7250124; DOI=10.1111/j.1432-1033.1981.tb05303.x;
RA Isobe T., Okuyama T.;
RT "The amino-acid sequence of the alpha subunit in bovine brain S-100a
RT protein.";
RL Eur. J. Biochem. 116:79-86(1981).
RN [4]
RP METAL ION-BINDING PROPERTIES.
RX PubMed=6615778; DOI=10.1021/bi00283a009;
RA Baudier J., Gerard D.;
RT "Ions binding to S100 proteins: structural changes induced by calcium and
RT zinc on S100a and S100b proteins.";
RL Biochemistry 22:3360-3369(1983).
RN [5]
RP STRUCTURE BY NMR OF 2-94.
RX PubMed=18088104; DOI=10.1021/bi701762v;
RA Zhukov I., Ejchart A., Bierzynski A.;
RT "Structural and motional changes induced in apo-S100A1 protein by the
RT disulfide formation between its Cys 85 residue and beta-mercaptoethanol.";
RL Biochemistry 47:640-650(2008).
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 -!- INTERACTION:
CC P02639; Q9TRY0: FKBP4; NbExp=2; IntAct=EBI-6477285, EBI-6477371;
CC P02639; Q76LV2: HSP90AA1; NbExp=2; IntAct=EBI-6477285, EBI-6477314;
CC P02639; Q27975: HSPA1A; NbExp=2; IntAct=EBI-6477285, EBI-6477341;
CC P02639; P26882: PPID; NbExp=2; IntAct=EBI-6477285, EBI-6477155;
CC P02639; Q9CXW3: Cacybp; Xeno; NbExp=4; IntAct=EBI-6477285, EBI-767146;
CC P02639; P11716: RYR1; Xeno; NbExp=3; IntAct=EBI-6477285, EBI-6477441;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P23297}.
CC Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P23297}. Mitochondrion
CC {ECO:0000250|UniProtKB:P56565}.
CC -!- TISSUE SPECIFICITY: Although predominant among the water-soluble brain
CC proteins, S100 is also found in a variety of other tissues.
CC {ECO:0000269|PubMed:3755105}.
CC -!- PTM: Glutathionylated; glutathionylation increases affinity to calcium
CC about 10-fold. {ECO:0000250|UniProtKB:P23297}.
CC -!- MISCELLANEOUS: Able to bind zinc in vitro; the binding sites are
CC different from the calcium binding sites. The physiological relevance
CC of zinc binding is unclear. Physiological concentrations of potassium
CC antagonize the binding of both divalent cations, especially affecting
CC the high-affinity calcium-binding sites. {ECO:0000269|PubMed:6615778}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; BC141991; AAI41992.1; -; mRNA.
DR EMBL; BC148019; AAI48020.1; -; mRNA.
DR PIR; A24156; BCBOIA.
DR RefSeq; NP_001092512.1; NM_001099042.2.
DR RefSeq; XP_005203778.1; XM_005203721.3.
DR RefSeq; XP_010801217.1; XM_010802915.2.
DR PDB; 2JPT; NMR; -; A/B=2-94.
DR PDBsum; 2JPT; -.
DR AlphaFoldDB; P02639; -.
DR BMRB; P02639; -.
DR SMR; P02639; -.
DR IntAct; P02639; 6.
DR STRING; 9913.ENSBTAP00000044226; -.
DR PaxDb; P02639; -.
DR Ensembl; ENSBTAT00000006806; ENSBTAP00000006806; ENSBTAG00000005163.
DR GeneID; 528735; -.
DR KEGG; bta:528735; -.
DR CTD; 6271; -.
DR VEuPathDB; HostDB:ENSBTAG00000005163; -.
DR VGNC; VGNC:34236; S100A1.
DR eggNOG; ENOG502SSF0; Eukaryota.
DR GeneTree; ENSGT00940000160475; -.
DR HOGENOM; CLU_138624_2_1_1; -.
DR InParanoid; P02639; -.
DR OMA; NEFFVDS; -.
DR OrthoDB; 1283969at2759; -.
DR EvolutionaryTrace; P02639; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000005163; Expressed in pons and 102 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0016529; C:sarcoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0044548; F:S100 protein binding; IBA:GO_Central.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0008016; P:regulation of heart contraction; IEA:InterPro.
DR CDD; cd05025; S-100A1; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028486; S100-A1.
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 3D-structure; Calcium; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Mitochondrion; Reference proteome; Repeat; S-nitrosylation;
KW Sarcoplasmic reticulum.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7250124"
FT CHAIN 2..94
FT /note="Protein S100-A1"
FT /id="PRO_0000143960"
FT DOMAIN 13..48
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 50..85
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 28
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 33
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 63
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 65
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 67
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 69
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 74
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 MOD_RES 2
FT /note="Blocked amino end (Gly)"
FT /evidence="ECO:0000269|PubMed:7250124"
FT MOD_RES 86
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P23297"
FT CONFLICT 65
FT /note="N -> D (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:2JPT"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:2JPT"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2JPT"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:2JPT"
FT HELIX 54..64
FT /evidence="ECO:0007829|PDB:2JPT"
FT HELIX 75..90
FT /evidence="ECO:0007829|PDB:2JPT"
SQ SEQUENCE 94 AA; 10518 MW; AD5E400DB85025D2 CRC64;
MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKELLQT ELSGFLDAQK DADAVDKVMK
ELDENGDGEV DFQEYVVLVA ALTVACNNFF WENS
