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Protein

Alkaline phosphatase

Gene

sap

Organism
Pandalus borealis (Northern red shrimp)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

A phosphate monoester + H2O = an alcohol + phosphate.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi34 – 341MagnesiumCombined sources
Metal bindingi34 – 341Zinc 1Combined sources
Metal bindingi34 – 341Zinc 2Combined sources
Metal bindingi83 – 831Zinc 1Combined sources
Metal bindingi146 – 1461Zinc 2; via tele nitrogenCombined sources
Metal bindingi148 – 1481MagnesiumCombined sources
Metal bindingi148 – 1481Zinc 2Combined sources
Metal bindingi307 – 3071MagnesiumCombined sources
Metal bindingi307 – 3071Zinc 2Combined sources
Metal bindingi312 – 3121Zinc 3Combined sources
Metal bindingi316 – 3161Zinc 3; via tele nitrogenCombined sources
Metal bindingi353 – 3531Zinc 1Combined sources
Metal bindingi354 – 3541Zinc 1; via tele nitrogenCombined sources
Metal bindingi429 – 4291Zinc 3; via tele nitrogenCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

HydrolaseUniRule annotationImported

Keywords - Ligandi

MagnesiumUniRule annotationCombined sources, Metal-bindingCombined sources, ZincUniRule annotationCombined sources

Names & Taxonomyi

Protein namesi
Recommended name:
Alkaline phosphataseUniRule annotation (EC:3.1.3.1UniRule annotation)
Gene namesi
Name:sapImported
OrganismiPandalus borealis (Northern red shrimp)Imported
Taxonomic identifieri6703 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaCrustaceaMalacostracaEumalacostracaEucaridaDecapodaPleocyemataCarideaPandaloideaPandalidaePandalus

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi111 – 1111N-linked (GlcNAc...)Combined sourcesCAR_5005390106
Disulfide bondi112 ↔ 177Combined sources
Disulfide bondi464 ↔ 472Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K7HX-ray1.92A/B1-473[»]
1SHNX-ray2.15A/B1-475[»]
1SHQX-ray2.00A/B1-475[»]
ProteinModelPortaliQ9BHT8.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BHT8.

Family & Domainsi

Sequence similaritiesi

Belongs to the alkaline phosphatase family.UniRule annotation

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamiPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00113. ALKPHPHTASE.
SMARTiSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q9BHT8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
KAYWNKDAQD ALDKQLGIKL REKQAKNVIF FLGDGMSLST VTAARIYKGG
60 70 80 90 100
LTGKFEREKI SWEEFDFAAL SKTYNTDKQV TDSAASATAY LTGVKTNQGV
110 120 130 140 150
IGLDANTVRT NCSYQLDESL FTYSIAHWFQ EAGRSTGVVT STRVTHATPA
160 170 180 190 200
GTYAHVADRD WENDSDVVHD REDPEICDDI AEQLVFREPG KNFKVIMGGG
210 220 230 240 250
RRGFFPEEAL DIEDGIPGER EDGKHLITDW LDDKASQGAT ASYVWNRDDL
260 270 280 290 300
LAVDIRNTDY LMGLFSYTHL DTVLTRDAEM DPTLPEMTKV AIEMLTKDEN
310 320 330 340 350
GFFLLVEGGR IDHMHHANQI RQSLAETLDM EEAVSMALSM TDPEETIILV
360 370 380 390 400
TADHGHTLTI TGYADRNTDI LDFAGISDLD DRRYTILDYG SGPGYHITED
410 420 430 440 450
GKRYEPTEED LKDINFRYAS AAPKHSVTHD GTDVGIWVNG PFAHLFTGVY
460 470
EENYIPHALA YAACVGTGRT FCDEK
Length:475
Mass (Da):52,971
Last modified:June 1, 2001 - v1
Checksum:i6BD14B64CE0D706D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11Imported

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ296089 mRNA. Translation: CAC35697.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ296089 mRNA. Translation: CAC35697.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K7HX-ray1.92A/B1-473[»]
1SHNX-ray2.15A/B1-475[»]
1SHQX-ray2.00A/B1-475[»]
ProteinModelPortaliQ9BHT8.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BHT8.

Family and domain databases

Gene3Di3.40.720.10. 1 hit.
InterProiIPR017849. Alkaline_Pase-like_a/b/a.
IPR001952. Alkaline_phosphatase.
IPR018299. Alkaline_phosphatase_AS.
IPR017850. Alkaline_phosphatase_core.
[Graphical view]
PfamiPF00245. Alk_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00113. ALKPHPHTASE.
SMARTiSM00098. alkPPc. 1 hit.
[Graphical view]
SUPFAMiSSF53649. SSF53649. 1 hit.
PROSITEiPS00123. ALKALINE_PHOSPHATASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Thermolabile alkaline phosphatase from Northern shrimp (Pandalus borealis): protein and cDNA sequence analyses."
    Nilsen I.W., Oeverboe K., Olsen R.
    Comp. Biochem. Physiol. 129:853-861(2001)
    Cited for: NUCLEOTIDE SEQUENCE.
    Tissue: HepatopancreasImported.
  2. "The 1.9 A crystal structure of heat-labile shrimp alkaline phosphatase."
    de Backer M., McSweeney S., Rasmussen H.B., Riise B.W., Lindley P., Hough E.
    J. Mol. Biol. 318:1265-1274(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 1-473 IN COMPLEX WITH ZINC, DISULFIDE BONDS.
  3. "Ligand-binding and metal-exchange crystallographic studies on shrimp alkaline phosphatase."
    de Backer M.M., McSweeney S., Lindley P.F., Hough E.
    Acta Crystallogr. D 60:1555-1561(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND ZINC, GLYCOSYLATION AT ASN-111, DISULFIDE BONDS.

Entry informationi

Entry nameiQ9BHT8_PANBO
AccessioniPrimary (citable) accession number: Q9BHT8
Entry historyi
Integrated into UniProtKB/TrEMBL: June 1, 2001
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.