P33763 (S10A5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein S100-A5

Alternative name(s):
Protein S-100D
S100 calcium-binding protein A5

Gene names

Name:	S100A5
Synonyms:	S100D

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	92 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds calcium, zinc and copper. One subunit can simultaneously bind 2 calcium ions or 2 copper ions plus 1 zinc ion. Calcium and copper ions compete for the same binding sites. Ref.3
Subunit structure	Homodimer. Ref.4
Sequence similarities	Belongs to the S-100 family. Contains 2 EF-hand domains.
Sequence caution	The sequence CAA79472.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA79475.1 differs from that shown. Reason: Erroneous initiation. The sequence CAA79479.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	Calcium Copper Metal-binding Zinc
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	nucleus Inferred from direct assay. Source: UniProtKB
Molecular function	calcium ion binding Inferred from direct assay Ref.4. Source: UniProtKB copper ion binding Inferred from direct assay Ref.4. Source: UniProtKB protein homodimerization activity Inferred from physical interaction Ref.4. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 92

92

Protein S100-A5

PRO_0000143980

Regions

Domain

12 – 47

36

EF-hand 1

Domain

47 – 82

36

EF-hand 2

Calcium binding

20 – 33

14

1; low affinity Potential

Calcium binding

60 – 71

12

2; high affinity Potential

Natural variations

Natural variant

54

1

D → G.

VAR_001305

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

92

Helix Strand Turn

Details...

Helix

4 – 17

14

Beta strand

27 – 30

4

Helix

31 – 41

11

Helix

52 – 59

8

Turn

60 – 62

3

Beta strand

64 – 68

5

Helix

69 – 81

13

Helix

84 – 88

5

Sequences

	Sequence		Length	Mass (Da)
	P33763 [UniParc]. Last modified April 16, 2002. Version 2. Checksum: 49C2B1DAEC481561	FASTA	92	10,744
	10 20 30 40 50 60 METPLEKALT TMVTTFHKYS GREGSKLTLS RKELKELIKK ELCLGEMKES SIDDLMKSLD 70 80 90 KNSDQEIDFK EYSVFLTMLC MAYNDFFLED NK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Six S100 genes are clustered on human chromosome 1q21: identification of two genes coding for the two previously unreported calcium-binding proteins S100D and S100E." Engelkamp D., Schaefer B.W., Mattei M.-G., Erne P., Heizmann C.W. Proc. Natl. Acad. Sci. U.S.A. 90:6547-6551(1993) [PubMed: 8341667] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Kidney.
[2]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Brain S100A5 is a novel calcium-, zinc-, and copper ion-binding protein of the EF-hand superfamily." Schaefer B.W., Fritschy J.-M., Murmann P., Troxler H., Durussel I., Heizmann C.W., Cox J.A. J. Biol. Chem. 275:30623-30630(2000) [PubMed: 10882717] [Abstract] Cited for: FUNCTION.
[4]	"Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states." Bertini I., Das Gupta S., Hu X., Karavelas T., Luchinat C., Parigi G., Yuan J. J. Biol. Inorg. Chem. 14:1097-1107(2009) [PubMed: 19536568] [Abstract] Cited for: STRUCTURE BY NMR IN COMPLEX WITH CALCIUM IONS, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z18954 mRNA. Translation: CAA79479.1. Different initiation.
Z18949 Genomic DNA. Translation: CAA79472.1. Different initiation.
Z18950 Genomic DNA. Translation: CAA79475.1. Different initiation.
BX470102 Genomic DNA. Translation: CAI14753.1.

IPI

IPI00219805.

RefSeq

NP_002953.2. NM_002962.1.

UniGene

Hs.2960.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KAX	NMR	-	A/B	1-92	[»]
2KAY	NMR	-	A/B	1-92	[»]

ProteinModelPortal

P33763.

SMR

P33763. Positions 1-92.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-7256702.

STRING

P33763.

PTM databases

PhosphoSite

P33763.

Polymorphism databases

DMDM

20178321.

Proteomic databases

PRIDE

P33763.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359215; ENSP00000352148; ENSG00000196420.
ENST00000368717; ENSP00000357706; ENSG00000196420.
ENST00000368718; ENSP00000357707; ENSG00000196420.

GeneID

6276.

KEGG

hsa:6276.

UCSC

uc001fbx.1. human.

Organism-specific databases

CTD

6276.

GeneCards

GC01M153509.

HGNC

HGNC:10495. S100A5.

MIM

176991. gene.

neXtProt

NX_P33763.

PharmGKB

PA34907.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG21159.

GeneTree

ENSGT00600000084162.

HOVERGEN

HBG001479.

InParanoid

P33763.

OrthoDB

EOG4M0F38.

Gene expression databases

ArrayExpress

P33763.

Bgee

P33763.

CleanEx

HS_S100A5.

Genevestigator

P33763.

GermOnline

ENSG00000196420. Homo sapiens.

Family and domain databases

InterPro

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.

Pfam

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

NextBio

24361.

SOURCE

Search...

Entry information

Entry name

S10A5_HUMAN

Accession

Primary (citable) accession number: P33763
Secondary accession number(s): Q5RHS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	April 16, 2002
Last modified:	January 25, 2012
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.