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O88428 (PAPS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
Short name=PAPS synthase 2
Short name=PAPSS 2
Alternative name(s):
Sulfurylase kinase 2
Short name=SK 2
Short name=SK2

Including the following 2 domains:

  1. Sulfate adenylyltransferase
    EC=2.7.7.4
    Alternative name(s):
    ATP-sulfurylase
    Sulfate adenylate transferase
    Short name=SAT
  2. Adenylyl-sulfate kinase
    EC=2.7.1.25
    Alternative name(s):
    3'-phosphoadenosine-5'-phosphosulfate synthase
    APS kinase
    Adenosine-5'-phosphosulfate 3'-phosphotransferase
    Adenylylsulfate 3'-phosphotransferase
Gene names
Name:Papss2
Synonyms:Atpsk2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length621 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate (PAPS: activated sulfate donor used by sulfotransferase). In mammals, PAPS is the sole source of sulfate; APS appears to be only an intermediate in the sulfate-activation pathway. May have a important role in skeletogenesis during postnatal growth.

Catalytic activity

ATP + sulfate = diphosphate + adenylyl sulfate.

ATP + adenylyl sulfate = ADP + 3'-phosphoadenylyl sulfate.

Pathway

Sulfur metabolism; sulfate assimilation.

Tissue specificity

Expressed in liver, cartilage, skin and brain.

Involvement in disease

Defects in Papss2 are the cause of brachymorphism (bm), a autosomal recessive disease, which is characterized by abnormal hepatic detoxification, bleeding times and postnatal growth, such as dome-shaped skull, short thick tail, and shortened but not widened limbs. The abnormal postnatal growth has been attributed to undersulfation of cartilage proteoglycans.

Sequence similarities

In the N-terminal section; belongs to the APS kinase family.

In the C-terminal section; belongs to the sulfate adenylyltransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 621621Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 2
PRO_0000105962

Regions

Nucleotide binding50 – 578ATP Potential
Region1 – ?211211Adenylyl-sulfate kinase
Region?212 – 621410Sulfate adenylyltransferase
Motif517 – 5215PP-motif

Sites

Active site1241Phosphoserine intermediate By similarity

Natural variations

Natural variant791G → R in bm; activity abolished. Ref.1 Ref.2
Natural variant1091R → K. Ref.2

Experimental info

Sequence conflict51F → S in AAC40191. Ref.1
Sequence conflict290 – 2945Missing in AAC98687. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O88428 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 27FD5377A79EFD61

FASTA62170,351
        10         20         30         40         50         60 
MSANFKMNHK RDQQKSTNVV YQAHHVSRNK RGQVVGTRGG FRGCTVWLTG LSGAGKTTIS 

        70         80         90        100        110        120 
FALEEYLVSH AIPCYSLDGD NVRHGLNKNL GFSAGDREEN IRRIAEVARL FADAGLVCIT 

       130        140        150        160        170        180 
SFISPFAKDR ENARKIHESA GLPFFEIFVD APLNICESRD VKGLYKRARA GEIKGFTGID 

       190        200        210        220        230        240 
SDYEKPETPE CVLKTNLSSV SDCVQQVVEL LQEQNIVPHT TIKGIHELFV PENKVDQIRA 

       250        260        270        280        290        300 
EAETLPSLPI TKLDLQWVQI LSEGWATPLK GFMREKEYLQ TLHFDTLLDG VVPRDGVINM 

       310        320        330        340        350        360 
SIPIVLPVSA DDKARLEGCS KFALMYEGRR VALLQDPEFY EHRKEERCSR VWGTATAKHP 

       370        380        390        400        410        420 
HIKMVMESGD WLVGGDLQVL ERIRWDDGLD QYRLTPLELK QKCKDMNADA VFAFQLRNPV 

       430        440        450        460        470        480 
HNGHALLMQD TRRRLLERGY KHPVLLLHPL GGWTKDDDVP LEWRMKQHAA VLEERVLDPK 

       490        500        510        520        530        540 
STIVAIFPSP MLYAGPTEVQ WHCRCRMIAG ANFYIVGRDP AGMPHPETKK DLYEPTHGGK 

       550        560        570        580        590        600 
VLSMAPGLTS VEIIPFRVAA YNKIKKAMDF YDPARHEEFD FISGTRMRKL AREGEDPPDG 

       610        620 
FMAPKAWKVL TDYYRSLEKT N

« Hide

References

« Hide 'large scale' references
[1]"A member of a new family of sulfate activating enzymes causes murine brachymorphism."
Kurima K., Warman M.L., Krishnan S., Domowicz M., Krueger R.C. Jr., Deyrup A., Schwartz N.B.
Proc. Natl. Acad. Sci. U.S.A. 95:8681-8685(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT BM ARG-79.
Tissue: Liver.
[2]"Mutations in orthologous genes in human spondyloepimetaphyseal dysplasia and the brachymorphic mouse."
ul Haque M.F., King L.M., Krakow D., Cantor R.M., Rusiniak M.E., Swank R.T., Superti-Furga A., Haque S., Abbas H., Ahmad W., Ahmad M., Cohn D.H.
Nat. Genet. 20:157-162(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT BM ARG-79, VARIANT LYS-109.
Strain: PWK.
Tissue: Spleen.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF052453 mRNA. Translation: AAC40191.1.
AF085144 mRNA. Translation: AAC98687.1.
BC090997 mRNA. Translation: AAH90997.1.
IPIIPI00754489.
RefSeqNP_035994.2. NM_011864.3.
UniGeneMm.203916.

3D structure databases

ProteinModelPortalO88428.
SMRO88428. Positions 22-619.
ModBaseSearch...

PTM databases

PhosphoSiteO88428.

Proteomic databases

PaxDbO88428.
PRIDEO88428.

Protocols and materials databases

DNASU23972.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000025833; ENSMUSP00000025833; ENSMUSG00000024899.
GeneID23972.
KEGGmmu:23972.

Organism-specific databases

CTD9060.
MGIMGI:1330223. Papss2.

Phylogenomic databases

eggNOGCOG0529.
GeneTreeENSGT00390000009613.
HOGENOMHOG000069045.
HOVERGENHBG053503.
InParanoidQ5BKP4.
KOK13811.
OMARGYKNPV.
OrthoDBEOG4VT5WR.

Enzyme and pathway databases

UniPathwayUPA00097.

Gene expression databases

BgeeO88428.
CleanExMM_PAPSS2.
GenevestigatorO88428.
GermOnlineENSMUSG00000024899. Mus musculus.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR002891. APS_kinase.
IPR025980. ATP-Sase_PUA-like_dom.
IPR015947. PUA-like_domain.
IPR014729. Rossmann-like_a/b/a_fold.
IPR024951. Sulfurylase_cat_dom.
IPR002650. Sulphate_adenylyltransferase.
[Graphical view]
PfamPF01583. APS_kinase. 1 hit.
PF01747. ATP-sulfurylase. 1 hit.
PF14306. PUA_2. 1 hit.
[Graphical view]
SUPFAMSSF88697. PUA-like. 1 hit.
TIGRFAMsTIGR00455. apsK. 1 hit.
TIGR00339. sopT. 1 hit.
ProtoNetSearch...

Other

NextBio303861.
SOURCESearch...

Entry information

Entry namePAPS2_MOUSE
AccessionPrimary (citable) accession number: O88428
Secondary accession number(s): Q5BKP4, Q9Z274
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: April 3, 2013
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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