S10A6_RABIT
ID S10A6_RABIT Reviewed; 90 AA.
AC P30801;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Protein S100-A6;
DE AltName: Full=Calcyclin;
DE AltName: Full=Lung 10 kDa protein;
DE AltName: Full=S100 calcium-binding protein A6;
GN Name=S100A6;
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].
RX PubMed=1459239; DOI=10.1016/0014-5793(92)80953-e;
RA Ando Y., Watanabe M., Akatsuka H., Tokumitsu H., Hidaka H.;
RT "Site-directed mutation makes rabbit calcyclin dimer.";
RL FEBS Lett. 314:109-113(1992).
RN [2]
RP PROTEIN SEQUENCE OF 23-31; 36-48 AND 57-89.
RC TISSUE=Lung;
RX PubMed=1898017; DOI=10.1016/0003-9861(91)90184-k;
RA Tokumitsu H., Kobayashi R., Hidaka H.;
RT "A calcium-binding protein from rabbit lung cytosol identified as the
RT product of growth-regulated gene (2A9) and its binding proteins.";
RL Arch. Biochem. Biophys. 288:202-207(1991).
RN [3]
RP ERRATUM OF PUBMED:1898017.
RX PubMed=1952954; DOI=10.1016/0003-9861(91)90153-a;
RA Tokumitsu H., Kobayashi R., Hidaka H.;
RL Arch. Biochem. Biophys. 291:401-401(1991).
RN [4]
RP INTERACTION WITH ANXA11.
RX PubMed=9497364; DOI=10.1074/jbc.273.11.6351;
RA Sudo T., Hidaka H.;
RT "Regulation of calcyclin (S100A6) binding by alternative splicing in the N-
RT terminal regulatory domain of annexin XI isoforms.";
RL J. Biol. Chem. 273:6351-6357(1998).
RN [5]
RP STRUCTURE BY NMR, AND SUBUNIT.
RC TISSUE=Lung;
RX PubMed=7552751; DOI=10.1038/nsb0995-790;
RA Potts B.C.M., Smith J., Akke M., Macke T.J., Okazaki K., Hikada H.,
RA Case D.A., Chazin W.J.;
RT "The structure of calcyclin reveals a novel homodimeric fold for S100
RT Ca(2+)-binding proteins.";
RL Nat. Struct. Biol. 2:790-796(1995).
RN [6]
RP STRUCTURE BY NMR, CALCIUM-BINDING, AND SUBUNIT.
RX PubMed=9519412; DOI=10.1016/s0969-2126(98)00023-9;
RA Sastry M., Ketchem R.R., Crescenzi O., Weber C., Lubienski M.J., Hikada H.,
RA Chazin W.J.;
RT "The three-dimensional structure of Ca(2+)-bound calcyclin: implications
RT for Ca(2+)-signal transduction by S100 proteins.";
RL Structure 6:223-231(1998).
RN [7]
RP STRUCTURE BY NMR, SUBUNIT, AND CALCIUM-BINDING.
RX PubMed=11902843; DOI=10.1006/jmbi.2002.5421;
RA Maeler L., Sastry M., Chazin W.J.;
RT "A structural basis for S100 protein specificity derived from comparative
RT analysis of apo and Ca(2+)-calcyclin.";
RL J. Mol. Biol. 317:279-290(2002).
RN [8]
RP STRUCTURE BY NMR IN COMPLEX WITH CACYBP, SUBUNIT, AND INTERACTION WITH
RP CACYBP.
RX PubMed=18803400; DOI=10.1021/bi801233z;
RA Lee Y.-T., Dimitrova Y.N., Schneider G., Ridenour W.B., Bhattacharya S.,
RA Soss S.E., Caprioli R.M., Filipek A., Chazin W.J.;
RT "Structure of the S100A6 complex with a fragment from the C-terminal domain
RT of Siah-1 interacting protein: a novel mode for S100 protein target
RT recognition.";
RL Biochemistry 47:10921-10932(2008).
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 such as the reorganization of the actin
CC cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium
CC binding is cooperative (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; head to tail assembly of 2 subunits. Interacts with
CC CACYBP in a calcium-dependent manner. Interacts with ANXA2 and ANXA11
CC (via N-terminus). Interacts with SUGT1. Interacts with TP53; has higher
CC affinity for TP53 that is phosphorylated on its N-terminal domain, and
CC lower affinity for TP53 that is phosphorylated on its C-terminal
CC domain. Interacts with tropomyosin. Interacts with FKBP4. 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: Nucleus envelope {ECO:0000250}. Cytoplasm
CC {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
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DR EMBL; D10885; BAA01707.1; -; mRNA.
DR PIR; S27011; S27011.
DR RefSeq; NP_001182671.1; NM_001195742.1.
DR PDB; 1A03; NMR; -; A/B=1-90.
DR PDB; 1CNP; NMR; -; A/B=1-90.
DR PDB; 1JWD; NMR; -; A/B=1-90.
DR PDB; 2CNP; NMR; -; A/B=1-90.
DR PDB; 2JTT; NMR; -; A/B=1-90.
DR PDBsum; 1A03; -.
DR PDBsum; 1CNP; -.
DR PDBsum; 1JWD; -.
DR PDBsum; 2CNP; -.
DR PDBsum; 2JTT; -.
DR AlphaFoldDB; P30801; -.
DR BMRB; P30801; -.
DR SMR; P30801; -.
DR STRING; 9986.ENSOCUP00000017711; -.
DR GeneID; 100348755; -.
DR KEGG; ocu:100348755; -.
DR CTD; 6277; -.
DR eggNOG; ENOG502S6IN; Eukaryota.
DR HOGENOM; CLU_138624_2_0_1; -.
DR InParanoid; P30801; -.
DR OMA; MVYNEAL; -.
DR OrthoDB; 1581517at2759; -.
DR TreeFam; TF332727; -.
DR EvolutionaryTrace; P30801; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR CDD; cd05029; S-100A6; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR034118; S-100A6.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
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; Cell membrane; Cytoplasm;
KW Direct protein sequencing; Membrane; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..90
FT /note="Protein S100-A6"
FT /id="PRO_0000143986"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 48..83
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 /evidence="ECO:0000305"
FT BINDING 33
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 67
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 40
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P06703"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P06703"
FT MOD_RES 47
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14069"
FT MOD_RES 47
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P14069"
FT HELIX 4..19
FT /evidence="ECO:0007829|PDB:1A03"
FT TURN 20..23
FT /evidence="ECO:0007829|PDB:1A03"
FT STRAND 27..30
FT /evidence="ECO:0007829|PDB:1A03"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:1A03"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:1A03"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:1A03"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:1JWD"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1A03"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1A03"
FT HELIX 85..89
FT /evidence="ECO:0007829|PDB:1A03"
SQ SEQUENCE 90 AA; 10154 MW; 9B23EC724B9E771F CRC64;
MASPLDQAIG LLIGIFHKYS GKEGDKHTLS KKELKELIQK ELTIGSKLQD AEIVKLMDDL
DRNKDQEVNF QEYITFLGAL AMIYNEALKG
