S100B_BOVIN
ID S100B_BOVIN Reviewed; 92 AA.
AC P02638; A4IFR6; Q3ZBY1;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Protein S100-B;
DE AltName: Full=S-100 protein beta chain;
DE AltName: Full=S-100 protein subunit beta;
DE AltName: Full=S100 calcium-binding protein B;
GN Name=S100B;
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].
RC TISSUE=Retina;
RA Burczynska B.B., Duda T., Venkataraman V., Sharma R.K.;
RT "Cloning, molecular and biochemical characterization of S100B from bovine
RT retina.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons, and Hypothalamus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 2-92.
RX PubMed=710399; DOI=10.1111/j.1432-1033.1978.tb12539.x;
RA Isobe T., Okuyama T.;
RT "The amino-acid sequence of S-100 protein (PAP I-b protein) and its
RT relation to the calcium-binding proteins.";
RL Eur. J. Biochem. 89:379-388(1978).
RN [4]
RP SEQUENCE REVISION TO 1-5.
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 [5]
RP PROTEIN SEQUENCE OF 2-92, AND ACETYLATION AT SER-2.
RX PubMed=4026304; DOI=10.1016/0003-9861(85)90086-4;
RA Marshak D.R., Umekawa H., Watterson D.M., Hidaka H.;
RT "Structural characterization of the calcium binding protein s100 from
RT adipose tissue.";
RL Arch. Biochem. Biophys. 240:777-780(1985).
RN [6]
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 [7]
RP CADMIUM-BINDING STUDIES.
RX PubMed=2039467; DOI=10.1042/bj2760013;
RA Donato H. Jr., Mani R.S., Kay C.M.;
RT "Spectral studies on the cadmium-ion-binding properties of bovine brain S-
RT 100b protein.";
RL Biochem. J. 276:13-18(1991).
RN [8]
RP STRUCTURE BY NMR.
RX PubMed=8805590; DOI=10.1016/s0969-2126(96)00111-6;
RA Kilby P.M., van Eldik L.J., Roberts G.C.K.;
RT "The solution structure of the bovine S100B protein dimer in the calcium-
RT free state.";
RL Structure 4:1041-1052(1996).
RN [9]
RP STRUCTURE BY NMR, FUNCTION, AND INTERACTION WITH STK38.
RX PubMed=14661952; DOI=10.1021/bi035089a;
RA Bhattacharya S., Large E., Heizmann C.W., Hemmings B.A., Chazin W.J.;
RT "Structure of the Ca2+/S100B/NDR kinase peptide complex: insights into S100
RT target specificity and activation of the kinase.";
RL Biochemistry 42:14416-14426(2003).
CC -!- FUNCTION: Weakly binds calcium but binds zinc very tightly-distinct
CC binding sites with different affinities exist for both ions on each
CC monomer. Physiological concentrations of potassium ion antagonize the
CC binding of both divalent cations, especially affecting high-affinity
CC calcium-binding sites. Binds to and initiates the activation of STK38
CC by releasing autoinhibitory intramolecular interactions within the
CC kinase. Interaction with AGER after myocardial infarction may play a
CC role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling.
CC Could assist ATAD3A cytoplasmic processing, preventing aggregation and
CC favoring mitochondrial localization. May mediate calcium-dependent
CC regulation on many physiological processes by interacting with other
CC proteins, such as TPR-containing proteins, and modulating their
CC activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:14661952}.
CC -!- SUBUNIT: Dimer of either two alpha chains, or two beta chains, or one
CC alpha and one beta chain. The S100B dimer binds two molecules of STK38.
CC Interacts with CACYBP in a calcium-dependent manner. Interacts with
CC ATAD3A; this interaction probably occurs in the cytosol prior to ATAD3A
CC mitochondrial targeting. Interacts with S100A6. The S100B dimer
CC interacts with two molecules of CAPZA1. Interacts with AGER. Interacts
CC with PPP5C (via TPR repeats); the interaction is calcium-dependent and
CC modulates PPP5C activity. Interacts with TPPP; this interaction
CC inhibits TPPP dimerization (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P02638; Q9CXW3: Cacybp; Xeno; NbExp=4; IntAct=EBI-458452, EBI-767146;
CC P02638; O95259: KCNH1; Xeno; NbExp=3; IntAct=EBI-458452, EBI-2909270;
CC P02638; Q15208: STK38; Xeno; NbExp=3; IntAct=EBI-458452, EBI-458376;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Although predominant among the water-soluble brain
CC proteins, S100 is also found in a variety of other tissues.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; DQ195377; ABA39829.1; -; mRNA.
DR EMBL; BC103041; AAI03042.1; -; mRNA.
DR EMBL; BC134727; AAI34728.1; -; mRNA.
DR PIR; A91254; BCBOIB.
DR RefSeq; NP_001029727.1; NM_001034555.3.
DR PDB; 1CFP; NMR; -; A/B=1-92.
DR PDB; 1MHO; X-ray; 2.00 A; A=2-89.
DR PDB; 1PSB; NMR; -; A/B=2-92.
DR PDB; 3CR2; X-ray; 1.88 A; A=1-92.
DR PDB; 3CR4; X-ray; 2.15 A; X=1-92.
DR PDB; 3CR5; X-ray; 1.85 A; X=1-92.
DR PDB; 3GK1; X-ray; 2.10 A; A=1-92.
DR PDB; 3GK2; X-ray; 1.98 A; A=1-92.
DR PDB; 3GK4; X-ray; 1.90 A; X=1-92.
DR PDB; 3IQO; X-ray; 1.50 A; A/B=1-92.
DR PDB; 3IQQ; X-ray; 2.01 A; A=1-92.
DR PDB; 3LK0; X-ray; 2.04 A; A/B/C/D=1-90.
DR PDB; 3LK1; X-ray; 1.79 A; A=1-90.
DR PDB; 3LLE; X-ray; 1.85 A; A/B=1-92.
DR PDB; 3RLZ; X-ray; 2.01 A; A/B=1-92.
DR PDB; 3RM1; X-ray; 1.24 A; A=1-92.
DR PDB; 4FQO; X-ray; 1.65 A; A=1-89.
DR PDB; 4PDZ; X-ray; 1.73 A; A/B=1-92.
DR PDB; 4PE0; X-ray; 1.08 A; A/X=1-92.
DR PDB; 4PE1; X-ray; 1.58 A; A/B=1-92.
DR PDB; 4PE4; X-ray; 2.18 A; A/X=1-92.
DR PDB; 4PE7; X-ray; 1.65 A; A=1-92.
DR PDB; 5DKN; X-ray; 1.53 A; A=1-92.
DR PDB; 5DKQ; X-ray; 1.59 A; A=1-92.
DR PDB; 5DKR; X-ray; 1.74 A; A/B=1-92.
DR PDB; 5ER4; X-ray; 1.81 A; X=1-92.
DR PDB; 5ER5; X-ray; 1.26 A; A=1-92.
DR PDBsum; 1CFP; -.
DR PDBsum; 1MHO; -.
DR PDBsum; 1PSB; -.
DR PDBsum; 3CR2; -.
DR PDBsum; 3CR4; -.
DR PDBsum; 3CR5; -.
DR PDBsum; 3GK1; -.
DR PDBsum; 3GK2; -.
DR PDBsum; 3GK4; -.
DR PDBsum; 3IQO; -.
DR PDBsum; 3IQQ; -.
DR PDBsum; 3LK0; -.
DR PDBsum; 3LK1; -.
DR PDBsum; 3LLE; -.
DR PDBsum; 3RLZ; -.
DR PDBsum; 3RM1; -.
DR PDBsum; 4FQO; -.
DR PDBsum; 4PDZ; -.
DR PDBsum; 4PE0; -.
DR PDBsum; 4PE1; -.
DR PDBsum; 4PE4; -.
DR PDBsum; 4PE7; -.
DR PDBsum; 5DKN; -.
DR PDBsum; 5DKQ; -.
DR PDBsum; 5DKR; -.
DR PDBsum; 5ER4; -.
DR PDBsum; 5ER5; -.
DR AlphaFoldDB; P02638; -.
DR BMRB; P02638; -.
DR SMR; P02638; -.
DR BioGRID; 182329; 3.
DR IntAct; P02638; 3.
DR MINT; P02638; -.
DR STRING; 9913.ENSBTAP00000006275; -.
DR iPTMnet; P02638; -.
DR PaxDb; P02638; -.
DR PeptideAtlas; P02638; -.
DR PRIDE; P02638; -.
DR Ensembl; ENSBTAT00000006275; ENSBTAP00000006275; ENSBTAG00000004777.
DR Ensembl; ENSBTAT00000086647; ENSBTAP00000063447; ENSBTAG00000004777.
DR GeneID; 525716; -.
DR KEGG; bta:525716; -.
DR CTD; 6285; -.
DR VEuPathDB; HostDB:ENSBTAG00000004777; -.
DR VGNC; VGNC:34248; S100B.
DR eggNOG; ENOG502S4HJ; Eukaryota.
DR GeneTree; ENSGT00940000161997; -.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P02638; -.
DR OMA; VTMVTIC; -.
DR OrthoDB; 1574989at2759; -.
DR TreeFam; TF332727; -.
DR SABIO-RK; P02638; -.
DR EvolutionaryTrace; P02638; -.
DR PRO; PR:P02638; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000004777; Expressed in midbrain and 102 other tissues.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0001726; C:ruffle; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IBA:GO_Central.
DR GO; GO:0019210; F:kinase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0050786; F:RAGE receptor binding; IBA:GO_Central.
DR GO; GO:0044548; F:S100 protein binding; ISS:UniProtKB.
DR GO; GO:0048156; F:tau protein binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0048143; P:astrocyte activation; NAS:UniProtKB.
DR GO; GO:0007409; P:axonogenesis; NAS:UniProtKB.
DR GO; GO:0007611; P:learning or memory; ISS:UniProtKB.
DR GO; GO:0007613; P:memory; IEA:Ensembl.
DR GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IGI:GO_Central.
DR GO; GO:0016310; P:phosphorylation; NAS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IBA:GO_Central.
DR GO; GO:0045917; P:positive regulation of complement activation; NAS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0048168; P:regulation of neuronal synaptic plasticity; IEA:Ensembl.
DR GO; GO:0006417; P:regulation of translation; NAS:UniProtKB.
DR CDD; cd05027; S-100B; 1.
DR IDEAL; IID50022; -.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028481; S100-B.
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; Acetylation; Calcium; Cytoplasm; Direct protein sequencing;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:4026304,
FT ECO:0000269|PubMed:710399"
FT CHAIN 2..92
FT /note="Protein S100-B"
FT /id="PRO_0000143965"
FT DOMAIN 13..48
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:0000305"
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:0000305"
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"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|PubMed:4026304"
FT HELIX 3..19
FT /evidence="ECO:0007829|PDB:4PE0"
FT STRAND 21..24
FT /evidence="ECO:0007829|PDB:4PE0"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1PSB"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:4PE0"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:4PE0"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1CFP"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:4PE0"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4PE0"
FT HELIX 71..88
FT /evidence="ECO:0007829|PDB:4PE0"
SQ SEQUENCE 92 AA; 10668 MW; 589BF1DAA0AF6DA7 CRC64;
MSELEKAVVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET
LDSDGDGECD FQEFMAFVAM ITTACHEFFE HE
