Protein S100-A1 - Rattus norvegicus (Rat)

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P35467 (S10A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Protein S100-A1

Alternative name(s):
S-100 protein alpha chain
S-100 protein subunit alpha
S100 calcium-binding protein A1

Gene names

Name:

S100a1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	94 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites.
Subunit structure	Dimer of either two alpha chains, or two beta chains, or one alpha and one beta chain. Interacts with FKBP4 By similarity. Interacts with AGER and CAPZA1. Interacts with RYR1 and RYR2. Interacts with CACYBP in a calcium-dependent manner By similarity. Ref.3 Ref.5 Ref.6
Subcellular location	Cytoplasm.
Tissue specificity	Although predominant among the water-soluble brain proteins, S100 is also found in a variety of other tissues.
Sequence similarities	Belongs to the S-100 family. Contains 2 EF-hand domains.

Ontologies

Keywords
Cellular component	Cytoplasm
Domain	Repeat
Ligand	Calcium Metal-binding Zinc
PTM	S-nitrosylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 12619862. Source: RGD positive regulation of voltage-gated calcium channel activity Inferred from direct assay PubMed 19657060. Source: RGD
Cellular_component	M band Inferred from direct assay PubMed 11156445. Source: RGD Z disc Inferred from direct assay PubMed 11156445. Source: RGD cytosol Traceable author statement PubMed 16129693. Source: RGD neuron projection Inferred from direct assay PubMed 19657060. Source: RGD nucleus Inferred from electronic annotation. Source: Compara sarcoplasmic reticulum Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Inferred from direct assay PubMed 16169012. Source: RGD protein homodimerization activity Inferred from direct assay PubMed 16169012. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 94

Protein S100-A1

PRO_0000143963

Regions

Domain

13 – 48

EF-hand 1

Domain

50 – 85

EF-hand 2

Calcium binding

20 – 33

1; low affinity

Calcium binding

63 – 74

2; high affinity

Amino acid modifications

Modified residue

S-nitrosocysteine By similarity

Experimental info

Sequence conflict

N → H in AAB20539. Ref.2

Sequence conflict

K → R in AAB20539. Ref.2

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P35467 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7B9C0A6C1C4FCCE0
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FASTA

10,560

        10         20         30         40         50         60 
MGSELETAME TLINVFHAHS GKEGDKYKLS KKELKDLLQT ELSSFLDVQK DADAVDKIMK 

        70         80         90 
ELDENGDGEV DFQEFVVLVA ALTVACNNFF WENS

« Hide

References

[1]	Song W. Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sprague-Dawley.
[2]	"Isolation of a rat S100 alpha cDNA and distribution of its mRNA in rat tissues." Zimmer D.B., Song W., Zimmer W.E. Brain Res. Bull. 27:157-162(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-94. Tissue: Kidney.
[3]	"S100B interaction with the receptor for advanced glycation end products (RAGE): a novel receptor-mediated mechanism for myocyte apoptosis postinfarction." Tsoporis J.N., Izhar S., Leong-Poi H., Desjardins J.F., Huttunen H.J., Parker T.G. Circ. Res. 106:93-101(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH AGER.
[4]	"Three-dimensional solution structure of the calcium-signaling protein apo-S100A1 as determined by NMR." Rustandi R.R., Baldisseri D.M., Inman K.G., Nizner P., Hamilton S.M., Landar A., Landar A., Zimmer D.B., Weber D.J. Biochemistry 41:788-796(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR.
[5]	"Solution structure of S100A1 bound to the CapZ peptide (TRTK12)." Wright N.T., Cannon B.R., Wilder P.T., Morgan M.T., Varney K.M., Zimmer D.B., Weber D.J. J. Mol. Biol. 386:1265-1277(2009) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR IN COMPLEX WITH CALCIUM IONS AND CAPZA1, SUBUNIT.
[6]	"S100A1 and calmodulin compete for the same binding site on ryanodine receptor." Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J. J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR IN COMPLEX WITH RYR1, INTERACTION WITH RYR1 AND RYR2.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U26358, U26357 Genomic DNA. Translation: AAB53657.1.
S68809 mRNA. Translation: AAB20539.2.

IPI

IPI00230855.

RefSeq

NP_001007637.1. NM_001007636.2.

UniGene

Rn.11091.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K2H	NMR	-	A/B	2-94	[»]
1ZFS	NMR	-	A/B	2-93	[»]
2K2F	NMR	-	A/B	2-94	[»]
2KBM	NMR	-	A/B	2-94	[»]

ProteinModelPortal

P35467.

SMR

P35467. Positions 2-94.

ModBase

Search...

Proteomic databases

PaxDb

P35467.

PRIDE

P35467.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000017000; ENSRNOP00000017000; ENSRNOG00000012410.

GeneID

295214.

KEGG

rno:295214.

UCSC

RGD:3614. rat.

Organism-specific databases

CTD

6271.

RGD

3614. S100a1.

Phylogenomic databases

eggNOG

NOG277258.

GeneTree

ENSGT00690000101829.

HOGENOM

HOG000246968.

HOVERGEN

HBG001479.

InParanoid

P35467.

OMA

INVFHTH.

OrthoDB

EOG4Z8XZ3.

Gene expression databases

Genevestigator

P35467.

GermOnline

ENSRNOG00000012410. Rattus norvegicus.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

InterPro

IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]

Pfam

PF00036. efhand. 1 hit.
PF01023. S_100. 1 hit.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00303. S100_CABP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P35467.

NextBio

639119.

Entry information

Entry name

S10A1_RAT

Accession

Primary (citable) accession number: P35467

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents