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Reviewed, UniProtKB/Swiss-Prot O73884 (PHOP1_CHICK)

Last modified March 3, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoethanolamine/phosphocholine phosphatase
    EC=3.1.3.75
Alternative name(s):
    3X11A
Gene names
Name: PHOSPHO1
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Phosphatase that has a high activity toward phosphoethanolamine (PEA) and phosphocholine (PCho). May be involved in the generation of inorganic phosphate for bone mineralization. Ref.2

Catalytic activity

O-phosphoethanolamine + H2O = ethanolamine + phosphate.

Phosphocholine + H2O = choline + phosphate.

Cofactor

Magnesium By similarity.

Tissue specificity

Expressed at sites of mineralization in bone and cartilage. Highly expressed in hypertrophic chondrocytes compared to non-chondrogenic tissues. Expressed in chondrocytes but not in heart, liver, lung, kidney, spleen, muscle, adipose tissues not duodenum. In diaphyseal cortical bone, it is expressed in the osteoid layer of the periosteum, forming surfaces of growing osteons, and newly formed osteocytes, whereas it is not expressed in the endosteum and closed osteons. In growth plate cartilage, it is limited to the early hypertrophic chondrocytes and the ossification groove of Ranvier. Highly expressed on the mineralization surfaces of the cartilage remnants and trabecular bone within the primary spongiosa. Expressed in 17-day-old embryonic calvaria, the osteoid present on the intramembranous and periosteal bone surfaces but not in soft tissues examined. Ref.2 Ref.1

Induction

Up-regulated 5-fold during chondrocyte terminal differentiation. Ref.1

Sequence similarities

Belongs to the HAD-like hydrolase superfamily. PHOSPHO family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 268268Phosphoethanolamine/phosphocholine phosphatase
PRO_0000068831

Sites

Active site321Nucleophile By similarity
Active site341Proton donor By similarity
Metal binding321Magnesium By similarity
Metal binding341Magnesium By similarity
Metal binding2031Magnesium By similarity
Binding site431Substrate By similarity
Binding site1231Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O73884-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 68852F21D9EE0024

FASTA26830,443
        10         20         30         40         50         60 
MKRCCEGVGL PCLFKGVGMA SSRPPKYLLV FDFDGTIINE SSDDSIVRAA PGQALPEHIR 

        70         80         90        100        110        120 
QSFREGFYNE YMQRVLAYMG DQGVKMGDFK AVYENIPLSP GMPDLFQFLS KNHELFEIIL 

       130        140        150        160        170        180 
ISDANMFGIE CKLRAAGFYS LFRKIFSNPS SFDKRGYFTL GPYHSHKCLD CPANTCKRKI 

       190        200        210        220        230        240 
LTEYLAERAQ EEVEFERVFY VGDGANDFCP SVTLTSADVA FPRKGYPMHQ MTQEMEKKQP 

       250        260 
GTFQATVVPW ESATEVARYL QELLKKKC 

« Hide

References

[1]"Identification and cloning of a novel phosphatase expressed at high levels in differentiating growth plate chondrocytes."
Houston B., Seawright E., Jefferies D., Hoogland E., Lester D., Whitehead C., Farquharson C.
Biochim. Biophys. Acta 1448:500-506(1999) [PubMed: 9990301] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
[2]"PHOSPHO1 -- a novel phosphatase specifically expressed at sites of mineralisation in bone and cartilage."
Houston B., Stewart A.J., Farquharson C.
Bone 34:629-637(2004) [PubMed: 15050893] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

AJ006529 mRNA. Translation: CAA07090.1.
IPIIPI00577667.
RefSeqNP_990176.1.
UniGeneGga.2334

3D structure databases

ModBaseSearch...

Genome annotation databases

EnsemblENSGALG00000001281. Gallus gallus. [Contig view]
GeneID395650.
KEGGgga:395650.

Phylogenomic databases

HOVERGENO73884.

Enzyme and pathway databases

BRENDA3.1.3.75. 4.

Family and domain databases

InterProIPR006383. HAD-SF_hydro_IB_PSP-like.
IPR006384. PyrdxlP_Pase-rel.
IPR016965. PyrdxlP_Pase_PHOSPHO2.
[Graphical view]
PfamPF06888. Put_Phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF031051. PyrdxlP_Pase_PHOSPHO2. 1 hit.
TIGRFAMsTIGR01489. DKMTPPase-SF. 1 hit.
TIGR01488. HAD-SF-IB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePHOP1_CHICK
AccessionPrimary (citable) accession number: O73884
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: August 1, 1998
Last modified: March 3, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents