ID   S10AB_PIG               Reviewed;          99 AA.
AC   P31950;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   24-JAN-2024, entry version 162.
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=S100C;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND ACETYLATION AT MET-1.
RC   TISSUE=Heart muscle;
RX   PubMed=1722468; DOI=10.1016/0014-5793(91)81393-m;
RA   Ohta H., Sasaki T., Naka M., Hiraoka O., Miyamoto C., Furuichi Y.,
RA   Tanaka T.;
RT   "Molecular cloning and expression of the cDNA coding for a new member of
RT   the S100 protein family from porcine cardiac muscle.";
RL   FEBS Lett. 295:93-96(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9500989; DOI=10.1006/bbrc.1998.8158;
RA   Nakamura T., Hayashi M., Kato A., Sawazaki T., Yasue H., Nakano T.,
RA   Tanaka T.;
RT   "A unique exon-intron organization of a porcine S100C gene: close
RT   evolutionary relationship to calmodulin genes.";
RL   Biochem. Biophys. Res. Commun. 243:647-652(1998).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=10673436; DOI=10.1016/s0969-2126(00)00093-9;
RA   Rety S., Osterloh D., Arie J.-P., Tabaries S., Seeman J., Russo-Marie F.,
RA   Gerke V., Lewit-Bentley A.;
RT   "Structural basis of the Ca(2+)-dependent association between S100C
RT   (S100A11) and its target, the N-terminal part of annexin I.";
RL   Structure 8:175-184(2000).
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-8 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; AB004800; BAA20521.1; -; mRNA.
DR   EMBL; AB003363; BAA25189.1; -; Genomic_DNA.
DR   PIR; S20342; S20342.
DR   RefSeq; NP_001004045.1; NM_001004045.1.
DR   RefSeq; XP_003361619.1; XM_003361571.2.
DR   PDB; 1QLS; X-ray; 2.30 A; A=1-99.
DR   PDBsum; 1QLS; -.
DR   AlphaFoldDB; P31950; -.
DR   SMR; P31950; -.
DR   STRING; 9823.ENSSSCP00000067377; -.
DR   iPTMnet; P31950; -.
DR   PaxDb; 9823-ENSSSCP00000021681; -.
DR   PeptideAtlas; P31950; -.
DR   Ensembl; ENSSSCT00000035409.3; ENSSSCP00000028457.1; ENSSSCG00000006610.6.
DR   Ensembl; ENSSSCT00005021974.1; ENSSSCP00005013139.1; ENSSSCG00005014065.1.
DR   Ensembl; ENSSSCT00015101194.1; ENSSSCP00015041913.1; ENSSSCG00015075165.1.
DR   Ensembl; ENSSSCT00025069103.1; ENSSSCP00025029763.1; ENSSSCG00025050557.1.
DR   Ensembl; ENSSSCT00030096642.1; ENSSSCP00030044556.1; ENSSSCG00030069067.1.
DR   Ensembl; ENSSSCT00035072787.1; ENSSSCP00035029530.1; ENSSSCG00035054556.1.
DR   Ensembl; ENSSSCT00040102009.1; ENSSSCP00040046035.1; ENSSSCG00040073855.1.
DR   Ensembl; ENSSSCT00045013805.1; ENSSSCP00045009550.1; ENSSSCG00045008211.1.
DR   Ensembl; ENSSSCT00050001666.1; ENSSSCP00050000475.1; ENSSSCG00050001387.1.
DR   Ensembl; ENSSSCT00055051545.1; ENSSSCP00055041194.1; ENSSSCG00055026074.1.
DR   Ensembl; ENSSSCT00060072493.1; ENSSSCP00060031279.1; ENSSSCG00060053238.1.
DR   Ensembl; ENSSSCT00065062219.1; ENSSSCP00065026971.1; ENSSSCG00065045455.1.
DR   Ensembl; ENSSSCT00070056208.1; ENSSSCP00070047742.1; ENSSSCG00070028026.1.
DR   GeneID; 445534; -.
DR   KEGG; ssc:445534; -.
DR   CTD; 6282; -.
DR   VGNC; VGNC:92537; S100A11.
DR   eggNOG; ENOG502SS6H; Eukaryota.
DR   GeneTree; ENSGT00940000154172; -.
DR   HOGENOM; CLU_138624_1_0_1; -.
DR   InParanoid; P31950; -.
DR   OMA; MACEKCY; -.
DR   OrthoDB; 5310603at2759; -.
DR   TreeFam; TF332727; -.
DR   Reactome; R-SSC-6798695; Neutrophil degranulation.
DR   EvolutionaryTrace; P31950; -.
DR   Proteomes; UP000008227; Chromosome 4.
DR   Proteomes; UP000314985; Chromosome 4.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   Bgee; ENSSSCG00000006610; Expressed in hindlimb bud and 43 other cell types or tissues.
DR   ExpressionAtlas; P31950; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0044548; F:S100 protein binding; IBA:GO_Central.
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   IDEAL; IID50073; -.
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; 2.
DR   PROSITE; PS00303; S100_CABP; 1.
DR   Genevisible; P31950; SS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Calcium; Cytoplasm; Disulfide bond;
KW   Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..99
FT                   /note="Protein S100-A11"
FT                   /id="PRO_0000144011"
FT   DOMAIN          10..47
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   DOMAIN          53..88
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         29
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         31
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         36
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         66
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         68
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         70
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         72
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         77
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         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000269|PubMed:1722468"
FT   MOD_RES         8
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P31949"
FT   DISULFID        11
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   HELIX           7..23
FT                   /evidence="ECO:0007829|PDB:1QLS"
FT   HELIX           34..41
FT                   /evidence="ECO:0007829|PDB:1QLS"
FT   HELIX           46..51
FT                   /evidence="ECO:0007829|PDB:1QLS"
FT   HELIX           56..65
FT                   /evidence="ECO:0007829|PDB:1QLS"
FT   STRAND          70..73
FT                   /evidence="ECO:0007829|PDB:1QLS"
FT   HELIX           75..97
FT                   /evidence="ECO:0007829|PDB:1QLS"
SQ   SEQUENCE   99 AA;  11180 MW;  C0688AF40F908558 CRC64;
     MAKRPTETER CIESLIAIFQ KHAGRDGNNT KISKTEFLIF MNTELAAFTQ NQKDPGVLDR
     MMKKLDLDSD GQLDFQEFLN LIGGLAIACH DSFIKSTQK
//