S10AB_PIG
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 03-AUG-2022, entry version 155.
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.ENSSSCP00000021681; -.
DR iPTMnet; P31950; -.
DR PaxDb; P31950; -.
DR PeptideAtlas; P31950; -.
DR PRIDE; P31950; -.
DR Ensembl; ENSSSCT00000035409; ENSSSCP00000028457; ENSSSCG00000006610.
DR Ensembl; ENSSSCT00000088301; ENSSSCP00000073301; ENSSSCG00000006610.
DR Ensembl; ENSSSCT00005021974; ENSSSCP00005013139; ENSSSCG00005014065.
DR Ensembl; ENSSSCT00015101194; ENSSSCP00015041913; ENSSSCG00015075165.
DR Ensembl; ENSSSCT00025069103; ENSSSCP00025029763; ENSSSCG00025050557.
DR Ensembl; ENSSSCT00030096642; ENSSSCP00030044556; ENSSSCG00030069067.
DR Ensembl; ENSSSCT00035072787; ENSSSCP00035029530; ENSSSCG00035054556.
DR Ensembl; ENSSSCT00040102009; ENSSSCP00040046035; ENSSSCG00040073855.
DR Ensembl; ENSSSCT00045013805; ENSSSCP00045009550; ENSSSCG00045008211.
DR Ensembl; ENSSSCT00050001666; ENSSSCP00050000475; ENSSSCG00050001387.
DR Ensembl; ENSSSCT00055051545; ENSSSCP00055041194; ENSSSCG00055026074.
DR Ensembl; ENSSSCT00060072493; ENSSSCP00060031279; ENSSSCG00060053238.
DR Ensembl; ENSSSCT00065062219; ENSSSCP00065026971; ENSSSCG00065045455.
DR Ensembl; ENSSSCT00070056208; ENSSSCP00070047742; ENSSSCG00070028026.
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; 1549220at2759; -.
DR TreeFam; TF332727; -.
DR Reactome; R-SSC-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; P31950; -.
DR Proteomes; UP000008227; Chromosome 4.
DR Proteomes; UP000314985; Chromosome 4.
DR Bgee; ENSSSCG00000006610; Expressed in hindlimb bud and 43 other tissues.
DR ExpressionAtlas; P31950; baseline and differential.
DR Genevisible; P31950; SS.
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 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; 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; 2.
DR PROSITE; PS00303; S100_CABP; 1.
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
