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 24-JAN-2024, entry version 131. 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}. 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; 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 PhosphoSitePlus; Q6B345; -. DR jPOST; Q6B345; -. DR PaxDb; 10116-ENSRNOP00000013393; -. DR Ensembl; ENSRNOT00000013393.7; ENSRNOP00000013393.4; ENSRNOG00000010105.7. DR Ensembl; ENSRNOT00055054735; ENSRNOP00055045242; ENSRNOG00055031612. DR Ensembl; ENSRNOT00060021712; ENSRNOP00060017179; ENSRNOG00060012775. DR Ensembl; ENSRNOT00065040256; ENSRNOP00065032759; ENSRNOG00065023539. DR GeneID; 445415; -. DR KEGG; rno:445415; -. DR UCSC; RGD:1303295; rat. DR AGR; RGD:1303295; -. 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; 5310603at2759; -. 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 cell types or tissues. 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 CDD; cd05023; S-100A11; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. 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; PROTEIN S100-A11; 1. DR PANTHER; PTHR11639; S100 CALCIUM-BINDING PROTEIN; 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; EF-hand; 1. DR PROSITE; PS00018; EF_HAND_1; 1. DR PROSITE; PS50222; EF_HAND_2; 1. DR PROSITE; PS00303; S100_CABP; 1. DR Genevisible; Q6B345; RN. 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 //