S10A2_BOVIN
ID S10A2_BOVIN Reviewed; 97 AA.
AC P10462; Q3T043;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Protein S100-A2;
DE AltName: Full=Protein S-100L;
DE AltName: Full=S100 calcium-binding protein A2;
GN Name=S100A2;
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 PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Kidney, and Lung;
RX PubMed=2521861; DOI=10.1083/jcb.108.2.569;
RA Glenney J.R. Jr., Kindy M.S., Zokas L.;
RT "Isolation of a new member of the S100 protein family: amino acid sequence,
RT tissue, and subcellular distribution.";
RL J. Cell Biol. 108:569-578(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May function as calcium sensor and modulator, contributing to
CC cellular calcium signaling. May function by interacting with other
CC proteins, such as TPR-containing proteins, and indirectly play a role
CC in many physiological processes. May also play a role in suppressing
CC tumor cell growth (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Interacts with FKBP4. Interacts with PPP5C (via TPR
CC repeats); the interaction is calcium-dependent and modulates PPP5C
CC activity (By similarity). Interacts with TPPP; this interaction
CC inhibits TPPP dimerization (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein binds two calcium ions.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; BC102570; AAI02571.1; -; mRNA.
DR PIR; A30129; A30129.
DR RefSeq; NP_001029539.1; NM_001034367.2.
DR AlphaFoldDB; P10462; -.
DR SMR; P10462; -.
DR IntAct; P10462; 1.
DR STRING; 9913.ENSBTAP00000000589; -.
DR PaxDb; P10462; -.
DR PeptideAtlas; P10462; -.
DR PRIDE; P10462; -.
DR Ensembl; ENSBTAT00000000589; ENSBTAP00000000589; ENSBTAG00000037651.
DR Ensembl; ENSBTAT00000072619; ENSBTAP00000071742; ENSBTAG00000037651.
DR Ensembl; ENSBTAT00000084523; ENSBTAP00000067363; ENSBTAG00000037651.
DR GeneID; 509860; -.
DR KEGG; bta:509860; -.
DR CTD; 6273; -.
DR VEuPathDB; HostDB:ENSBTAG00000037651; -.
DR VGNC; VGNC:34242; S100A2.
DR eggNOG; ENOG502S4AU; Eukaryota.
DR GeneTree; ENSGT00940000163114; -.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P10462; -.
DR OMA; TMMCNDF; -.
DR OrthoDB; 1560865at2759; -.
DR TreeFam; TF332727; -.
DR Proteomes; UP000009136; Chromosome 3.
DR Bgee; ENSBTAG00000037651; Expressed in urethra and 104 other tissues.
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:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0043542; P:endothelial cell migration; IBA:GO_Central.
DR CDD; cd00213; S-100; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR034325; S-100_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR Pfam; PF01023; S_100; 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; Direct protein sequencing; Metal-binding; Reference proteome;
KW Repeat.
FT CHAIN 1..97
FT /note="Protein S100-A2"
FT /id="PRO_0000143970"
FT DOMAIN 12..47
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:0000305"
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:0000305"
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"
SQ SEQUENCE 97 AA; 10893 MW; 55ACC9F60CF9C9E6 CRC64;
MSSPLEQALA VMVATFHKYS GQEGDKFKLS KGEMKELLHK ELPSFVGEKV DEEGLKKLMG
DLDENSDQQV DFQEYAVFLA LITIMCNDFF QGSPARS
