PAPS1_MOUSE
ID PAPS1_MOUSE Reviewed; 624 AA.
AC Q60967; Q3U647;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1;
DE Short=PAPS synthase 1;
DE Short=PAPSS 1;
DE AltName: Full=Sulfurylase kinase 1;
DE Short=SK 1;
DE Short=SK1;
DE Includes:
DE RecName: Full=Sulfate adenylyltransferase;
DE EC=2.7.7.4 {ECO:0000269|PubMed:7493984};
DE AltName: Full=ATP-sulfurylase;
DE AltName: Full=Sulfate adenylate transferase;
DE Short=SAT;
DE Includes:
DE RecName: Full=Adenylyl-sulfate kinase;
DE EC=2.7.1.25 {ECO:0000269|PubMed:7493984};
DE AltName: Full=3'-phosphoadenosine-5'-phosphosulfate synthase;
DE AltName: Full=APS kinase;
DE AltName: Full=Adenosine-5'-phosphosulfate 3'-phosphotransferase;
DE AltName: Full=Adenylylsulfate 3'-phosphotransferase;
GN Name=Papss1; Synonyms=Asapk, Atpsk1, Papss;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=7493984; DOI=10.1074/jbc.270.49.29453;
RA Li H., Deyrup A., Mensch J.R. Jr., Domowicz M., Konstantinidis A.K.,
RA Schwartz N.B.;
RT "The isolation and characterization of cDNA encoding the mouse bifunctional
RT ATP sulfurylase-adenosine 5'-phosphosulfate kinase.";
RL J. Biol. Chem. 270:29453-29459(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE31878.1};
RC TISSUE=Bone marrow {ECO:0000312|EMBL:BAE31878.1},
RC Heart {ECO:0000312|EMBL:BAE27221.1}, and
RC Kidney {ECO:0000312|EMBL:BAE40904.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase
CC activity, which mediates two steps in the sulfate activation pathway.
CC The first step is the transfer of a sulfate group to ATP to yield
CC adenosine 5'-phosphosulfate (APS), and the second step is the transfer
CC of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate
CC (PAPS: activated sulfate donor used by sulfotransferase). In mammals,
CC PAPS is the sole source of sulfate; APS appears to be only an
CC intermediate in the sulfate-activation pathway (PubMed:7493984).
CC Required for normal biosynthesis of sulfated L-selectin ligands in
CC endothelial cells (By similarity). {ECO:0000250|UniProtKB:O43252,
CC ECO:0000269|PubMed:7493984}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate +
CC diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000269|PubMed:7493984};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate
CC + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339,
CC ChEBI:CHEBI:456216; EC=2.7.1.25;
CC Evidence={ECO:0000269|PubMed:7493984};
CC -!- PATHWAY: Sulfur metabolism; sulfate assimilation.
CC {ECO:0000269|PubMed:7493984}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:O43252}.
CC -!- TISSUE SPECIFICITY: Expressed in the neonatal brain and in cartilage.
CC {ECO:0000269|PubMed:7493984}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the APS kinase
CC family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the sulfate
CC adenylyltransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U34883; AAC52328.1; -; mRNA.
DR EMBL; AK146507; BAE27221.1; -; mRNA.
DR EMBL; AK153296; BAE31878.1; -; mRNA.
DR EMBL; AK168982; BAE40782.1; -; mRNA.
DR EMBL; AK169124; BAE40904.1; -; mRNA.
DR EMBL; CH466532; EDL12198.1; -; Genomic_DNA.
DR CCDS; CCDS38641.1; -.
DR RefSeq; NP_035993.1; NM_011863.2.
DR AlphaFoldDB; Q60967; -.
DR SMR; Q60967; -.
DR BioGRID; 204832; 27.
DR IntAct; Q60967; 28.
DR STRING; 10090.ENSMUSP00000029666; -.
DR iPTMnet; Q60967; -.
DR PhosphoSitePlus; Q60967; -.
DR EPD; Q60967; -.
DR jPOST; Q60967; -.
DR MaxQB; Q60967; -.
DR PaxDb; Q60967; -.
DR PRIDE; Q60967; -.
DR ProteomicsDB; 288058; -.
DR Antibodypedia; 26233; 176 antibodies from 28 providers.
DR DNASU; 23971; -.
DR Ensembl; ENSMUST00000029666; ENSMUSP00000029666; ENSMUSG00000028032.
DR GeneID; 23971; -.
DR KEGG; mmu:23971; -.
DR UCSC; uc008rjr.2; mouse.
DR CTD; 9061; -.
DR MGI; MGI:1330587; Papss1.
DR VEuPathDB; HostDB:ENSMUSG00000028032; -.
DR eggNOG; KOG4238; Eukaryota.
DR GeneTree; ENSGT00390000009613; -.
DR InParanoid; Q60967; -.
DR OMA; ESQCKKV; -.
DR OrthoDB; 528280at2759; -.
DR PhylomeDB; Q60967; -.
DR TreeFam; TF313143; -.
DR Reactome; R-MMU-174362; Transport and synthesis of PAPS.
DR UniPathway; UPA00097; -.
DR BioGRID-ORCS; 23971; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Papss1; mouse.
DR PRO; PR:Q60967; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q60967; protein.
DR Bgee; ENSMUSG00000028032; Expressed in vestibular membrane of cochlear duct and 261 other tissues.
DR ExpressionAtlas; Q60967; baseline and differential.
DR Genevisible; Q60967; MM.
DR GO; GO:0009336; C:sulfate adenylyltransferase complex (ATP); IC:MGI.
DR GO; GO:0004020; F:adenylylsulfate kinase activity; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016779; F:nucleotidyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0004781; F:sulfate adenylyltransferase (ATP) activity; IDA:MGI.
DR GO; GO:0050428; P:3'-phosphoadenosine 5'-phosphosulfate biosynthetic process; IDA:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0000103; P:sulfate assimilation; ISS:UniProtKB.
DR CDD; cd02027; APSK; 1.
DR CDD; cd00517; ATPS; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00065; Adenylyl_sulf_kinase; 1.
DR InterPro; IPR002891; APS_kinase.
DR InterPro; IPR025980; ATP-Sase_PUA-like_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR024951; Sulfurylase_cat_dom.
DR InterPro; IPR002650; Sulphate_adenylyltransferase.
DR Pfam; PF01747; ATP-sulfurylase; 1.
DR Pfam; PF14306; PUA_2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR00455; apsK; 1.
DR TIGRFAMs; TIGR00339; sopT; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..624
FT /note="Bifunctional 3'-phosphoadenosine 5'-phosphosulfate
FT synthase 1"
FT /id="PRO_0000105960"
FT REGION 1..225
FT /note="Adenylyl-sulfate kinase"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT REGION 234..624
FT /note="Sulfate adenylyltransferase"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 62..67
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 89..92
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 101
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 106..109
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 132..133
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 171
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 184..185
FT /ligand="adenosine 5'-phosphosulfate"
FT /ligand_id="ChEBI:CHEBI:58243"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 419..422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 521..525
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O43252"
FT MOD_RES 12
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 624 AA; 70794 MW; B487EFAF9B78BE3E CRC64;
MEIPGSLCKK VKLSNNAQNW GMQRATNVTY QAHHVSRNKR GQVVGTRGGF RGCTVWLTGL
SGAGKTTVSM ALEEYLVCHG IPCYTLDGDN IRQGLNKNLG FSPEDREENV RRIAEVAKLF
ADAGLVCITS FISPYTQDRN NARQIHEGAS LPFFEVFVDA PLHVCEQRDV KGLYKKARAG
EIKGFTGIDS EYEKPEAPEL VLKTDSCDVN DCVQQVVELL QERDIVPVDA SYEVKELYVP
ENKLHLAKTD AEALPALKIN KVDMQWVQVL AEGWATPLNG FMREREYLQC LHFDCLLDGG
VINLSVPIVL TATHEDKERL DGCTAFALVY EGRRVAILRN PEFFEHRKEE RCARQWGTTC
KNHPYIKMVL EQGDWLIGGD LQVLDRIYWN DGLDQYRLTP TELKQKFKDM NADAVFAFQL
RNPVHNGHAL LMQDTHKQLL ERGYRRPVLL LHPLGGWTKD DDVPLMWRMK QHAAVLEEGI
LDPETTVVAI FPSPMMYAGP TEVQWHCRAR MVAGANFYIV GRDPAGMPHP ETGKDLYEPT
HGAKVLTMAP GLITLEIVPF RVAAYNKKKK RMDYYDSEHH EDFEFISGTR MRKLAREGQK
PPEGFMAPKA WTVLVEYYKS LEKA
