S100B_RABIT
ID S100B_RABIT Reviewed; 92 AA.
AC Q6YNR6;
DT 12-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 105.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RA Qian Z., Barmack N.H.;
RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
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}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY050568; AAL12231.1; -; mRNA.
DR RefSeq; NP_001076199.1; NM_001082730.1.
DR AlphaFoldDB; Q6YNR6; -.
DR BMRB; Q6YNR6; -.
DR SMR; Q6YNR6; -.
DR STRING; 9986.ENSOCUP00000001267; -.
DR ABCD; Q6YNR6; 1 sequenced antibody.
DR GeneID; 100009495; -.
DR KEGG; ocu:100009495; -.
DR CTD; 6285; -.
DR eggNOG; ENOG502S4HJ; Eukaryota.
DR InParanoid; Q6YNR6; -.
DR OrthoDB; 1574989at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd05027; S-100B; 1.
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 3: Inferred from homology;
KW Acetylation; Calcium; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P02638"
FT CHAIN 2..92
FT /note="Protein S100-B"
FT /id="PRO_0000143968"
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:0000250|UniProtKB:P02638"
SQ SEQUENCE 92 AA; 10713 MW; 43815AC212A3AD6B CRC64;
MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET
LDNDGDGECD FQEFMAFVAM VTTACHEFFE HE
