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P22629 (SAV_STRAV) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Streptavidin
OrganismStreptomyces avidinii
Taxonomic identifier1895 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length183 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).

Subunit structure

Homotetramer.

Subcellular location

Secreted.

Sequence similarities

Belongs to the avidin/streptavidin family.

Contains 1 avidin-like domain.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   LigandBiotin
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Ref.1
Chain25 – 183159Streptavidin
PRO_0000002729

Regions

Domain37 – 159123Avidin-like
Motif83 – 853Cell attachment site; atypical

Sites

Binding site671Biotin
Binding site781Biotin
Binding site1161Biotin
Binding site1321Biotin
Binding site1441Biotin

Secondary structure

................................... 183
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22629 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 4652D8AE018468F5

FASTA18318,834
        10         20         30         40         50         60 
MRKIVVAAIA VSLTTVSITA SASADPSKDS KAQVSAAEAG ITGTWYNQLG STFIVTAGAD 

        70         80         90        100        110        120 
GALTGTYESA VGNAESRYVL TGRYDSAPAT DGSGTALGWT VAWKNNYRNA HSATTWSGQY 

       130        140        150        160        170        180 
VGGAEARINT QWLLTSGTTE ANAWKSTLVG HDTFTKVKPS AASIDAAKKA GVNNGNPLDA 


VQQ 

« Hide

References

[1]"Molecular cloning and nucleotide sequence of the streptavidin gene."
Argarana C.E., Kuntz I.D., Birken S., Axel R., Cantor C.R.
Nucleic Acids Res. 14:1871-1882(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-64.
[2]"Studies on the biotin-binding site of streptavidin. Tryptophan residues involved in the active site."
Gitlin G., Bayer E.A., Wilchek M.
Biochem. J. 256:279-282(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: IMPORTANCE OF TRP IN BIOTIN-BINDING.
[3]"Studies on the biotin-binding sites of avidin and streptavidin. Tyrosine residues are involved in the binding site."
Gitlin G., Bayer E.A., Wilchek M.
Biochem. J. 269:527-530(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: IMPORTANCE OF TYR IN BIOTIN-BINDING.
[4]"Streptavidin contains an RYD sequence which mimics the RGD receptor domain of fibronectin."
Alon R., Bayer E.A., Wilchek M.
Biochem. Biophys. Res. Commun. 170:1236-1241(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: CELL-BINDING.
[5]"Structural origins of high-affinity biotin binding to streptavidin."
Weber P.C., Ohlendorf D.H., Wendoloski J.J., Salemme F.R.
Science 243:85-88(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 37-157.
[6]"Structural studies of the streptavidin binding loop."
Freitag S., le Trong I., Klumb L., Stayton P.S., Stenkamp R.E.
Protein Sci. 6:1157-1166(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 40-157.
[7]"In crystals of complexes of streptavidin with peptide ligands containing the HPQ sequence the pKa of the peptide histidine is less than 3.0."
Katz B.A., Cass R.T.
J. Biol. Chem. 272:13220-13228(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 37-157.
[8]"Binding of biotin to streptavidin stabilizes intersubunit salt bridges between Asp61 and His87 at low pH."
Katz B.A.
J. Mol. Biol. 274:776-800(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 37-157.
[9]"Structural studies of binding site tryptophan mutants in the high-affinity streptavidin-biotin complex."
Freitag S., le Trong I., Chilkoti A., Klumb L.A., Stayton P.S., Stenkamp R.E.
J. Mol. Biol. 279:211-221(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 37-157 OF MUTANTS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03591 Genomic DNA. Translation: CAA27265.1.
PIRA23513.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DF8X-ray1.51A/B37-163[»]
1HQQX-ray1.70A/B/C/D36-163[»]
1HXLX-ray1.80A/B36-163[»]
1HXZX-ray1.80A/B36-163[»]
1HY2X-ray2.00A/B/C/D36-163[»]
1I9HX-ray2.40A/B25-163[»]
1KFFX-ray1.90A/B/C/D38-163[»]
1KL3X-ray1.70A/B/C/D38-163[»]
1KL4X-ray1.70A/B/C/D38-163[»]
1KL5X-ray1.80A/B/C/D38-163[»]
1LCVX-ray2.30A/B39-159[»]
1LCWX-ray2.20A/B39-159[»]
1LCZX-ray1.95A/B25-159[»]
1LUQX-ray0.96A/B37-163[»]
1MEPX-ray1.65A/B/C/D37-163[»]
1MK5X-ray1.40A/B37-163[»]
1MM9X-ray1.66A37-163[»]
1MOYX-ray1.55A37-163[»]
1N43X-ray1.89A/B/C/D37-163[»]
1N4JX-ray2.18A37-163[»]
1N7YX-ray1.96A/B/C/D37-163[»]
1N9MX-ray1.60A/B/C/D37-163[»]
1N9YX-ray1.53A/B/C/D37-163[»]
1NBXX-ray1.70A/B/C/D37-163[»]
1NC9X-ray1.80A/B/C/D37-163[»]
1NDJX-ray1.81A/B/C/D37-163[»]
1NQMX-ray1.70A/B/C/D24-159[»]
1PTSX-ray2.00A/B37-157[»]
1RSTX-ray1.70B38-163[»]
1RSUX-ray1.70B38-163[»]
1RXHX-ray2.90A/B37-163[»]
1RXJX-ray1.14A/B/C/D39-159[»]
1RXKX-ray1.70A/B38-159[»]
1SLDX-ray2.50B25-159[»]
1SLEX-ray2.00B/D25-159[»]
1SLFX-ray1.76B/D25-159[»]
1SLGX-ray1.76B/D25-159[»]
1SREX-ray1.78A/B37-157[»]
1SRFX-ray2.00A/B37-157[»]
1SRGX-ray1.80A/B37-157[»]
1SRHX-ray2.20A/B37-157[»]
1SRIX-ray1.65A/B37-157[»]
1SRJX-ray1.80A/B37-157[»]
1STPX-ray2.60A25-183[»]
1STRX-ray1.80B/D37-159[»]
1STSX-ray1.95B/D37-159[»]
1SWAX-ray1.90A/B/C/D37-163[»]
1SWBX-ray1.85A/B/C/D37-163[»]
1SWCX-ray1.80A/B/C/D37-163[»]
1SWDX-ray1.90A/B/C/D37-163[»]
1SWEX-ray2.06A/B/C/D37-163[»]
1SWFX-ray2.00A/B/C/D37-163[»]
1SWGX-ray1.80A/B/C/D37-163[»]
1SWHX-ray1.70A/B/C/D37-163[»]
1SWJX-ray2.00A/B/C/D37-163[»]
1SWKX-ray2.00A/B/C/D37-163[»]
1SWLX-ray1.80A/B/C/D37-163[»]
1SWNX-ray2.20A/B/C/D37-163[»]
1SWOX-ray1.95A/B/C/D37-163[»]
1SWPX-ray2.00A/B/C/D37-163[»]
1SWQX-ray1.90A/B/C/D37-163[»]
1SWRX-ray1.90A/B/C/D37-163[»]
1SWSX-ray2.00A/B/C/D37-163[»]
1SWTX-ray2.00A/B37-163[»]
1SWUX-ray1.14A/B/C/D37-163[»]
1VWAX-ray1.85B/D37-159[»]
1VWBX-ray1.82B37-159[»]
1VWCX-ray1.86B37-159[»]
1VWDX-ray1.87B37-159[»]
1VWEX-ray1.50B37-159[»]
1VWFX-ray1.92B37-159[»]
1VWGX-ray1.46B37-159[»]
1VWHX-ray1.48B37-159[»]
1VWIX-ray1.50B/D37-159[»]
1VWJX-ray1.45B/D37-159[»]
1VWKX-ray1.45B/D37-159[»]
1VWLX-ray1.45B/D37-159[»]
1VWMX-ray1.60B37-159[»]
1VWNX-ray1.85B37-159[»]
1VWOX-ray1.65B37-159[»]
1VWPX-ray1.75B37-159[»]
1VWQX-ray1.70B37-159[»]
1VWRX-ray1.50B37-159[»]
2BC3X-ray1.54A/B38-183[»]
2F01X-ray0.85A/B37-163[»]
2G5LX-ray1.15A/B37-163[»]
2GH7X-ray1.00A/B37-163[»]
2IZAX-ray1.46A37-157[»]
2IZBX-ray1.20A37-158[»]
2IZCX-ray1.40B/D37-159[»]
2IZDX-ray1.60B/D37-159[»]
2IZEX-ray1.57B/D37-159[»]
2IZFX-ray1.58B/D37-159[»]
2IZGX-ray1.36B/D37-159[»]
2IZHX-ray1.36B/D37-159[»]
2IZIX-ray1.50A37-159[»]
2IZJX-ray1.30A37-159[»]
2IZKX-ray1.30A37-159[»]
2IZLX-ray1.48B/D37-159[»]
2QCBX-ray1.65A38-183[»]
2RTAX-ray1.39A25-159[»]
2RTBX-ray1.50B/D25-159[»]
2RTCX-ray1.50B/D25-159[»]
2RTDX-ray1.65B/D25-159[»]
2RTEX-ray1.50B/D25-159[»]
2RTFX-ray1.47B/D25-159[»]
2RTGX-ray1.39B/D25-159[»]
2RTHX-ray1.56B/D25-159[»]
2RTIX-ray1.40B/D25-159[»]
2RTJX-ray1.40A25-159[»]
2RTKX-ray1.82A25-159[»]
2RTLX-ray1.41A25-159[»]
2RTMX-ray1.30A25-159[»]
2RTNX-ray1.80B/D25-159[»]
2RTOX-ray1.58B/D25-159[»]
2RTPX-ray1.50B/D25-159[»]
2RTQX-ray1.39B/D25-159[»]
2RTRX-ray1.62B/D25-159[»]
2WPUX-ray1.92A38-183[»]
2Y3EX-ray1.45A/B37-163[»]
2Y3FX-ray1.49A37-163[»]
3MG5X-ray1.30A/B/C/D37-163[»]
3PK2X-ray1.90A38-183[»]
3RDMX-ray1.60A37-164[»]
3RDOX-ray1.40A37-164[»]
3RDQX-ray1.60A37-164[»]
3RDSX-ray1.50A37-164[»]
3RDUX-ray1.50A37-164[»]
3RDXX-ray2.10A/B37-164[»]
3RE5X-ray1.95A37-164[»]
3RE6X-ray1.82A37-164[»]
3RY1X-ray1.03A/B/C/D37-163[»]
3RY2X-ray0.95A/B37-163[»]
3T6FX-ray1.22A/B37-163[»]
3T6LX-ray1.30A37-163[»]
4BX5X-ray1.43A/C37-72[»]
B/D37-163[»]
4BX6X-ray1.60A/B/C/D37-163[»]
4BX7X-ray2.26A/B37-163[»]
4DNEX-ray1.88A/B1-183[»]
4EKVX-ray2.00A25-183[»]
4GD9X-ray1.50A/B/C/D37-163[»]
4GDAX-ray1.00A/B37-163[»]
4GJSX-ray1.85A/B38-183[»]
4GJVX-ray2.40A38-183[»]
4IRWX-ray1.40A36-163[»]
4JO6X-ray1.75A/B/C/D25-183[»]
ProteinModelPortalP22629.
SMRP22629. Positions 38-159.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL1075026.

Proteomic databases

PRIDEP22629.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP22629.

Family and domain databases

Gene3D2.40.128.30. 1 hit.
InterProIPR005469. Avidin.
IPR017889. Avidin-like_CS.
IPR005468. Avidin/str.
[Graphical view]
PfamPF01382. Avidin. 1 hit.
[Graphical view]
PRINTSPR00709. AVIDIN.
SUPFAMSSF50876. SSF50876. 1 hit.
PROSITEPS00577. AVIDIN_1. 1 hit.
PS51326. AVIDIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22629.

Entry information

Entry nameSAV_STRAV
AccessionPrimary (citable) accession number: P22629
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: March 19, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references