S10AB_RABIT
ID S10AB_RABIT Reviewed; 102 AA.
AC P24480;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein S100-A11;
DE AltName: Full=Calgizzarin;
DE AltName: Full=Protein S100-C;
DE AltName: Full=S100 calcium-binding protein A11;
GN Name=S100A11; Synonyms=PCALG, S100C;
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=Lung;
RX PubMed=1836726; DOI=10.1016/0006-291x(91)91239-9;
RA Watanabe M., Ando Y., Todoroki H., Minami H., Hiroyoshi H.;
RT "Molecular cloning and sequencing of a cDNA clone encoding a new calcium
RT binding protein, named calgizzarin, from rabbit lung.";
RL Biochem. Biophys. Res. Commun. 181:644-649(1991).
RN [2]
RP PROTEIN SEQUENCE OF 35-49 AND 53-62.
RC TISSUE=Lung;
RX PubMed=1917990; DOI=10.1016/s0021-9258(18)55115-2;
RA Todoroki H., Kobayashi R., Watanabe M., Minami H., Hidaka H.;
RT "Purification, characterization, and partial sequence analysis of a newly
RT identified EF-hand type 13-kDa Ca(2+)-binding protein from smooth muscle
RT and non-muscle tissues.";
RL J. Biol. Chem. 266:18668-18673(1991).
CC -!- FUNCTION: Facilitates the differentiation and the cornification of
CC keratinocytes. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Smooth muscle and non-muscle tissues.
CC -!- PTM: Phosphorylation at Thr-7 significantly suppresses homodimerization
CC and promotes association with NCL/nucleolin which induces nuclear
CC translocation. {ECO:0000250}.
CC -!- MISCELLANEOUS: Binds two calcium ions per molecule with an affinity
CC similar to that of the S100 proteins. {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; D10586; BAA01443.1; -; mRNA.
DR PIR; JQ1300; JQ1300.
DR RefSeq; NP_001075656.1; NM_001082187.1.
DR PDB; 1NSH; NMR; -; A/B=2-102.
DR PDBsum; 1NSH; -.
DR AlphaFoldDB; P24480; -.
DR BMRB; P24480; -.
DR SMR; P24480; -.
DR PRIDE; P24480; -.
DR GeneID; 100008975; -.
DR KEGG; ocu:100008975; -.
DR CTD; 6282; -.
DR eggNOG; ENOG502SS6H; Eukaryota.
DR InParanoid; P24480; -.
DR OrthoDB; 1549220at2759; -.
DR EvolutionaryTrace; P24480; -.
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:0048306; F:calcium-dependent protein binding; IEA:InterPro.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:InterPro.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR001751; S100/CaBP7/8-like_CS.
DR InterPro; IPR013787; S100_Ca-bd_sub.
DR InterPro; IPR028482; S100A11.
DR PANTHER; PTHR11639:SF60; PTHR11639:SF60; 1.
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 Disulfide bond; Metal-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat.
FT CHAIN 1..102
FT /note="Protein S100-A11"
FT /id="PRO_0000144012"
FT DOMAIN 12..47
FT /note="EF-hand 1"
FT /evidence="ECO:0000305"
FT DOMAIN 52..87
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 30
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 35
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 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 71
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 76
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="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P31949"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31949"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50543"
FT DISULFID 10
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CONFLICT 59
FT /note="R -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 6..21
FT /evidence="ECO:0007829|PDB:1NSH"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:1NSH"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1NSH"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:1NSH"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1NSH"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:1NSH"
FT HELIX 75..86
FT /evidence="ECO:0007829|PDB:1NSH"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1NSH"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:1NSH"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1NSH"
SQ SEQUENCE 102 AA; 11429 MW; 66D1FFBBA4F8DF45 CRC64;
MSRPTETERC IESLIAVFQK YAGKDGHSVT LSKTEFLSFM NTELAAFTKN QKDPGVLDRM
MKKLDLNSDG QLDFQEFLNL IGGLAVACHE SFVKAAPPQK RF
