Protein S100-G - Bos taurus (Bovine)

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P02633 (S100G_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 105. 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-G

Alternative name(s):
Calbindin-D9k
S100 calcium-binding protein G
Vitamin D-dependent calcium-binding protein, intestinal
Short name=CABP

Gene names

Name:	S100G
Synonyms:	CALB3, S100D

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	79 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)

Sequence similarities

Belongs to the S-100 family.

Contains 2 EF-hand domains.

Ontologies

Keywords
Domain	Repeat
Ligand	Calcium Vitamin D
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro vitamin D binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 79

Protein S100-G

PRO_0000144026

Regions

Domain

13 – 48

EF-hand 1

Domain

45 – 79

EF-hand 2

Calcium binding

18 – 31

1; low affinity

Calcium binding

58 – 69

2; high affinity

Amino acid modifications

Modified residue

N-acetylserine Ref.4

Secondary structure

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P02633 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 80A5B2AA11D4E74B
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FASTA

8,918

        10         20         30         40         50         60 
MSAKKSPEEL KGIFEKYAAK EGDPNQLSKE ELKLLLQTEF PSLLKGPSTL DELFEELDKN 

        70 
GDGEVSFEEF QVLVKKISQ

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The molecular cloning of the complementary deoxyribonucleic acid for bovine vitamin D-dependent calcium-binding protein: structure of the full-length protein and evidence for homologies with other calcium-binding proteins of the troponin-C superfamily of proteins." Kumar R., Wieben E., Beecher S.J. Mol. Endocrinol. 3:427-432(1989) [PubMed: 2710141] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	NIH - Mammalian Gene Collection (MGC) project Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Placenta.
[3]	"The amino acid sequence of bovine intestinal calcium-binding protein." Fullmer C.S., Wasserman R.H. J. Biol. Chem. 256:5669-5674(1981) [PubMed: 7240164] [Abstract] Cited for: PROTEIN SEQUENCE OF 5-79.
[4]	"Structure of vitamin D-dependent calcium-binding protein from bovine intestine." Szebenyi D.M.E., Obendorf S.K., Moffat K. Nature 294:327-332(1981) [PubMed: 7312031] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[5]	"The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. Molecular details, ion binding, and implications for the structure of other calcium-binding proteins." Szebenyi D.M.E., Moffat K. J. Biol. Chem. 261:8761-8777(1986) [PubMed: 3722173] [Abstract] Cited for: X-RAY STRUCTURE REFINEMENT.
[6]	"Structural basis for the negative allostery between Ca(2+)- and Mg(2+)-binding in the intracellular Ca(2+)-receptor calbindin D9k." Andersson M., Malmendal A., Linse S., Ivarsson I., Forsen S., Svensson L.A. Protein Sci. 6:1139-1147(1997) [PubMed: 9194174] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
[7]	"The rate and structural consequences of proline cis-trans isomerization in calbindin D9k: NMR studies of the minor (cis-Pro43) isoform and the Pro43Gly mutant." Kordel J., Forsen S., Drakenberg T., Chazin W.J. Biochemistry 29:4400-4409(1990) [PubMed: 2350544] [Abstract] Cited for: STRUCTURE BY NMR.
[8]	"1H NMR resonance assignments, secondary structure, and global fold of Apo bovine calbindin D9k." Skelton N.J., Forsen S., Chazin W.J. Biochemistry 29:5752-5761(1990) [PubMed: 2200514] [Abstract] Cited for: STRUCTURE BY NMR.
[9]	"Molecular basis for co-operativity in Ca2+ binding to calbindin D9k. 1H nuclear magnetic resonance studies of (Cd2+)1-bovine calbindin D9k." Akke M., Forsen S., Chazin W.J. J. Mol. Biol. 220:173-189(1991) [PubMed: 2067016] [Abstract] Cited for: STRUCTURE BY NMR.
[10]	"Solution structure of (Cd2+)1-calbindin D9k reveals details of the stepwise structural changes along the Apo-->(Ca2+)II1-->(Ca2+)I,II2 binding pathway." Akke M., Forsen S., Chazin W.J. J. Mol. Biol. 252:102-121(1995) [PubMed: 7666423] [Abstract] Cited for: STRUCTURE BY NMR.
[11]	"Protein solution structure calculations in solution: solvated molecular dynamics refinement of calbindin D9k." Kordel J., Pearlman D.A., Chazin W.J. J. Biomol. NMR 10:231-243(1997) [PubMed: 9390401] [Abstract] Cited for: STRUCTURE BY NMR.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M18344 mRNA. Translation: AAA30420.1.
BC118480 mRNA. Translation: AAI18481.1.

IPI

IPI00712685.

PIR

KLBOI. A40151.

RefSeq

NP_776682.1. NM_174257.2.

UniGene

Bt.390.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B1G	NMR	-	A	5-79	[»]
1BOC	NMR	-	A	5-78	[»]
1BOD	NMR	-	A	5-78	[»]
1CDN	NMR	-	A	5-79	[»]
1CLB	NMR	-	A	5-78	[»]
1D1O	NMR	-	A	5-79	[»]
1HT9	X-ray	1.76	A/B	5-78	[»]
1IG5	X-ray	1.50	A	5-79	[»]
1IGV	X-ray	1.85	A	5-79	[»]
1KCY	NMR	-	A	5-78	[»]
1KQV	NMR	-	A	1-79	[»]
1KSM	NMR	-	A	1-79	[»]
1N65	NMR	-	A	5-78	[»]
1QX2	X-ray	1.44	A/B	5-78	[»]
1RT0	NMR	-	A	58-69	[»]
2BCA	NMR	-	A	5-78	[»]
2BCB	NMR	-	A	5-78	[»]
3ICB	X-ray	2.30	A	5-79	[»]
4ICB	X-ray	1.60	A	5-78	[»]

ProteinModelPortal

P02633.

SMR

P02633. Positions 5-79.

ModBase

Search...

Protein-protein interaction databases

STRING

P02633.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000022630; ENSBTAP00000022630; ENSBTAG00000017020.

GeneID

281658.

KEGG

bta:281658.

Organism-specific databases

CTD

795.

Phylogenomic databases

eggNOG

maNOG21121.

GeneTree

ENSGT00530000064238.

HOVERGEN

HBG001479.

InParanoid

P02633.

OMA

KGPSTLD.

OrthoDB

EOG4NP754.

PhylomeDB

P02633.

Family and domain databases

InterPro

IPR018248. EF-hand.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR001751. S100/CaBP-9k_CS.
IPR013787. S100_Ca-bd_sub.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

K14734.

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...

Entry information

Entry name

S100G_BOVIN

Accession

Primary (citable) accession number: P02633
Secondary accession number(s): Q17Q94

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 105 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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents