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Protein

Protein S100-A6

Gene

S100A6

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May function as calcium sensor and modulator, contributing to cellular calcium signaling. May function by interacting with other proteins, such as TPR-containing proteins, and indirectly play a role in many physiological processes such as the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi20 – 33141Add
BLAST
Calcium bindingi61 – 72122Add
BLAST

GO - Molecular functioni

  • calcium ion binding Source: UniProtKB
  • protein N-terminus binding Source: UniProtKB
  • zinc ion binding Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein S100-A6
Alternative name(s):
Calcyclin
Lung 10 kDa protein
S100 calcium-binding protein A6
Gene namesi
Name:S100A6
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
Proteomesi
  • UP000001811 Componenti: Chromosome 13

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9090Protein S100-A6PRO_0000143986Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei40 – 401N6-acetyllysineBy similarity
Modified residuei46 – 461PhosphoserineBy similarity
Modified residuei47 – 471N6-acetyllysine; alternateBy similarity
Modified residuei47 – 471N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Interactioni

Subunit structurei

Homodimer; head to tail assembly of 2 subunits. Interacts with CACYBP in a calcium-dependent manner. Interacts with ANXA2 and ANXA11 (via N-terminus). Interacts with SUGT1. Interacts with TP53; has higher affinity for TP53 that is phosphorylated on its N-terminal domain, and lower affinity for TP53 that is phosphorylated on its C-terminal domain. Interacts with tropomyosin. Interacts with FKBP4. Interacts with PPP5C (via TPR repeats); the interaction is calcium-dependent and modulates PPP5C activity (By similarity).By similarity

GO - Molecular functioni

  • protein N-terminus binding Source: UniProtKB

Protein-protein interaction databases

MINTiMINT-265917.
STRINGi9986.ENSOCUP00000017711.

Structurei

Secondary structure

1
90
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1916Combined sources
Turni20 – 234Combined sources
Beta strandi27 – 304Combined sources
Helixi31 – 4212Combined sources
Turni43 – 453Combined sources
Helixi48 – 6013Combined sources
Turni62 – 643Combined sources
Beta strandi66 – 683Combined sources
Helixi70 – 8314Combined sources
Helixi85 – 895Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A03NMR-A/B1-90[»]
1CNPNMR-A/B1-90[»]
1JWDNMR-A/B1-90[»]
2CNPNMR-A/B1-90[»]
2JTTNMR-A/B1-90[»]
ProteinModelPortaliP30801.
SMRiP30801. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30801.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 4736EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini48 – 8336EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the S-100 family.Curated
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IYT5. Eukaryota.
ENOG410Z6I6. LUCA.
GeneTreeiENSGT00760000119034.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP30801.
OMAiQVVNFQE.
OrthoDBiEOG78WKVD.
TreeFamiTF332727.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PfamiPF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 1 hit.
SM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P30801-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASPLDQAIG LLIGIFHKYS GKEGDKHTLS KKELKELIQK ELTIGSKLQD
60 70 80 90
AEIVKLMDDL DRNKDQEVNF QEYITFLGAL AMIYNEALKG
Length:90
Mass (Da):10,154
Last modified:November 1, 1995 - v2
Checksum:i9B23EC724B9E771F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10885 mRNA. Translation: BAA01707.1.
PIRiS27011.
RefSeqiNP_001182671.1. NM_001195742.1.
UniGeneiOcu.1714.

Genome annotation databases

EnsembliENSOCUT00000025782; ENSOCUP00000017711; ENSOCUG00000024096.
GeneIDi100348755.
KEGGiocu:100348755.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10885 mRNA. Translation: BAA01707.1.
PIRiS27011.
RefSeqiNP_001182671.1. NM_001195742.1.
UniGeneiOcu.1714.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A03NMR-A/B1-90[»]
1CNPNMR-A/B1-90[»]
1JWDNMR-A/B1-90[»]
2CNPNMR-A/B1-90[»]
2JTTNMR-A/B1-90[»]
ProteinModelPortaliP30801.
SMRiP30801. Positions 1-90.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-265917.
STRINGi9986.ENSOCUP00000017711.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSOCUT00000025782; ENSOCUP00000017711; ENSOCUG00000024096.
GeneIDi100348755.
KEGGiocu:100348755.

Organism-specific databases

CTDi6277.

Phylogenomic databases

eggNOGiENOG410IYT5. Eukaryota.
ENOG410Z6I6. LUCA.
GeneTreeiENSGT00760000119034.
HOGENOMiHOG000246968.
HOVERGENiHBG001479.
InParanoidiP30801.
OMAiQVVNFQE.
OrthoDBiEOG78WKVD.
TreeFamiTF332727.

Miscellaneous databases

EvolutionaryTraceiP30801.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]
PfamiPF01023. S_100. 1 hit.
[Graphical view]
SMARTiSM00054. EFh. 1 hit.
SM01394. S_100. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Site-directed mutation makes rabbit calcyclin dimer."
    Ando Y., Watanabe M., Akatsuka H., Tokumitsu H., Hidaka H.
    FEBS Lett. 314:109-113(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A calcium-binding protein from rabbit lung cytosol identified as the product of growth-regulated gene (2A9) and its binding proteins."
    Tokumitsu H., Kobayashi R., Hidaka H.
    Arch. Biochem. Biophys. 288:202-207(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-31; 36-48 AND 57-89.
    Tissue: Lung.
  3. "Regulation of calcyclin (S100A6) binding by alternative splicing in the N-terminal regulatory domain of annexin XI isoforms."
    Sudo T., Hidaka H.
    J. Biol. Chem. 273:6351-6357(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ANXA11.
  4. "The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins."
    Potts B.C.M., Smith J., Akke M., Macke T.J., Okazaki K., Hikada H., Case D.A., Chazin W.J.
    Nat. Struct. Biol. 2:790-796(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBUNIT.
    Tissue: Lung.
  5. "The three-dimensional structure of Ca(2+)-bound calcyclin: implications for Ca(2+)-signal transduction by S100 proteins."
    Sastry M., Ketchem R.R., Crescenzi O., Weber C., Lubienski M.J., Hikada H., Chazin W.J.
    Structure 6:223-231(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, CALCIUM-BINDING, SUBUNIT.
  6. "A structural basis for S100 protein specificity derived from comparative analysis of apo and Ca(2+)-calcyclin."
    Maeler L., Sastry M., Chazin W.J.
    J. Mol. Biol. 317:279-290(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBUNIT, CALCIUM-BINDING.
  7. "Structure of the S100A6 complex with a fragment from the C-terminal domain of Siah-1 interacting protein: a novel mode for S100 protein target recognition."
    Lee Y.-T., Dimitrova Y.N., Schneider G., Ridenour W.B., Bhattacharya S., Soss S.E., Caprioli R.M., Filipek A., Chazin W.J.
    Biochemistry 47:10921-10932(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR IN COMPLEX WITH CACYBP, SUBUNIT, INTERACTION WITH CACYBP.

Entry informationi

Entry nameiS10A6_RABIT
AccessioniPrimary (citable) accession number: P30801
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: November 1, 1995
Last modified: July 6, 2016
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.