S10AB_RAT
ID S10AB_RAT Reviewed; 98 AA.
AC Q6B345;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Protein S100-A11;
DE AltName: Full=Calgizzarin;
DE AltName: Full=S100 calcium-binding protein A11;
GN Name=S100a11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Brown Norway; TISSUE=Brain;
RA Hesse E.M.M., Wiehler W.B., Pho M.V.C., Walsh M.P.;
RT "Rat S100 calcium-binding protein A11 (calgizzarin) mRNA.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
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 -!- PTM: Phosphorylation at Thr-5 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}.
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DR EMBL; AY688465; AAT91807.1; -; mRNA.
DR RefSeq; NP_001004095.1; NM_001004095.1.
DR RefSeq; XP_006232867.1; XM_006232805.2.
DR AlphaFoldDB; Q6B345; -.
DR SMR; Q6B345; -.
DR BioGRID; 268753; 2.
DR IntAct; Q6B345; 1.
DR STRING; 10116.ENSRNOP00000013393; -.
DR jPOST; Q6B345; -.
DR PaxDb; Q6B345; -.
DR PRIDE; Q6B345; -.
DR Ensembl; ENSRNOT00000013393; ENSRNOP00000013393; ENSRNOG00000010105.
DR GeneID; 445415; -.
DR KEGG; rno:445415; -.
DR UCSC; RGD:1303295; rat.
DR CTD; 6282; -.
DR RGD; 1303295; S100a11.
DR eggNOG; ENOG502SS6H; Eukaryota.
DR GeneTree; ENSGT00940000154172; -.
DR HOGENOM; CLU_138624_1_0_1; -.
DR InParanoid; Q6B345; -.
DR OMA; MACEKCY; -.
DR OrthoDB; 1549220at2759; -.
DR PhylomeDB; Q6B345; -.
DR TreeFam; TF332727; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q6B345; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000010105; Expressed in lung and 19 other tissues.
DR Genevisible; Q6B345; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0001726; C:ruffle; ISO:RGD.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:RGD.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0044548; F:S100 protein binding; ISO:RGD.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:RGD.
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 3: Inferred from homology;
KW Acetylation; Calcium; Cytoplasm; Disulfide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..98
FT /note="Protein S100-A11"
FT /id="PRO_0000144013"
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 26
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 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"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P31949"
FT MOD_RES 22
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P50543"
FT DISULFID 8
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 98 AA; 11065 MW; 4693F1B07281DCBD CRC64;
MPTETERCIE SLIAVFQKYS GKDGNSCHLS KTEFLSFMNT ELAAFTKNQK DPGVLDRMMK
KLDLNSDGQL DFQEFLNLIG GLAIACHESF LQTSQKRI
