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P97355 (SPSY_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Spermine synthase

Short name=SPMSY
EC=2.5.1.22
Alternative name(s):
Spermidine aminopropyltransferase
Gene names
Name:Sms
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length366 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM) By similarity. Required for normal viability, growth and fertility. Ref.9

Catalytic activity

S-adenosyl 3-(methylthio)propylamine + spermidine = S-methyl-5'-thioadenosine + spermine.

Pathway

Amine and polyamine biosynthesis; spermine biosynthesis; spermine from spermidine: step 1/1.

Subunit structure

Homodimer. Dimerization is mediated through the N-terminal domain and seems to be required for activity as deletion of the N-terminal domain causes complete loss of activity By similarity.

Domain

Composed of 3 domains: the N-terminal domain has structural similarity to S-adenosylmethionine decarboxylase, the central domain is made up of four beta strands and the C-terminal domain is similar in structure to spermidine synthase. The N- and C-terminal domains are both required for activity By similarity.

Disruption phenotype

Mouse ES cells lacking Sms display normal growth rates but are sensitive to antiproliferative and DNA damage-inducing drugs. Ref.8 Ref.9

Sequence similarities

Belongs to the spermidine/spermine synthase family.

Contains 1 PABS (polyamine biosynthesis) domain.

Ontologies

Keywords
   Biological processPolyamine biosynthesis
   Molecular functionTransferase
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processspermine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionspermine synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 366365Spermine synthase
PRO_0000156539

Regions

Domain122 – 362241PABS
Region255 – 2562S-adenosylmethioninamine binding By similarity

Sites

Active site2761Proton acceptor By similarity
Binding site1481S-adenosylmethioninamine By similarity
Binding site1771Spermidine By similarity
Binding site2011Spermidine By similarity
Binding site2201S-adenosylmethioninamine By similarity
Binding site3511Spermidine By similarity
Binding site3531Spermidine By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Experimental info

Sequence conflict1881D → H in BAC33920. Ref.3
Sequence conflict2451R → K in BAC33920. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P97355 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: D549F319F51C43C5

FASTA36641,313
        10         20         30         40         50         60 
MAAARHSTLD FKLGAKADGE AILKGLQSIF QEQGMTESVH TWQDHGYLAT YTNKNGSFAN 

        70         80         90        100        110        120 
LRIYPHGLVL LDLQSYDSDV QGKQETDSLL NKIEEKMKEL SQDSTGRVKR LPPIVRGGAI 

       130        140        150        160        170        180 
DRYWPTADGR LVEYDIDEVV YDEDSPYQNI KILHSKQFGN ILILSGDVNL AESDLAYTRA 

       190        200        210        220        230        240 
IMGSGKEDYT GKDVLILGGG DGGILCEIVK LKPKMVTMVE IDQMVIDGCK KYMRRTCGDV 

       250        260        270        280        290        300 
LDNLRGDCYQ VLIEDCIPVL KMYAKEGREF DYVINDLTAV PISTSPEEDS TWDFLRLILD 

       310        320        330        340        350        360 
LSMKVLKQDG KYFTQGNCVN LTEALSLYEE QLGRLYCPVE FSKEIVCVPS YLELWVFYTV 


WKKAKP 

« Hide

References

« Hide 'large scale' references
[1]"Pex gene deletions in Gy and Hyp mice provide mouse models for X-linked hypophosphatemia."
Strom T.M., Francis F., Lorenz B., Boeddrich A., Econs M.J., Lehrach H., Meitinger T.
Hum. Mol. Genet. 6:165-171(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Nucleotide sequence of mouse spermidine aminopropyltransferase cDNA."
Niiranen K., Korhonen V., Janne J.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Diaphragm.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Bone marrow macrophage, Embryo, Embryonic spinal cord and Morula.
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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].
Strain: C57BL/6.
Tissue: Brain and Olfactory epithelium.
[6]"Spermine deficiency resulting from targeted disruption of the spermine synthase gene in embryonic stem cells leads to enhanced sensitivity to antiproliferative drugs."
Korhonen V.-P., Niiranen K., Halmekyto M., Pietila M., Diegelman P., Parkkinen J.J., Eloranta T., Porter C.W., Alhonen L., Janne J.
Mol. Pharmacol. 59:231-238(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-315.
Strain: 129/SvJ.
[7]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 297-307, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[8]"Spermine deficiency in Gy mice caused by deletion of the spermine synthase gene."
Lorenz B., Francis F., Gempel K., Boeddrich A., Josten M., Schmahl W., Schmidt J., Lehrach H., Meitinger T., Strom T.M.
Hum. Mol. Genet. 7:541-547(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 316-366, DISRUPTION PHENOTYPE.
[9]"Spermine synthesis is required for normal viability, growth, and fertility in the mouse."
Wang X., Ikeguchi Y., McCloskey D.E., Nelson P., Pegg A.E.
J. Biol. Chem. 279:51370-51375(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y09419 mRNA. Translation: CAA70573.1.
AF031486 mRNA. Translation: AAB86631.1.
AK049787 mRNA. Translation: BAC33920.1.
AK011542 mRNA. Translation: BAB27685.1.
AK017775 mRNA. Translation: BAB30923.1.
AK149929 mRNA. Translation: BAE29173.1.
AK160637 mRNA. Translation: BAE35931.1.
AK160659 mRNA. Translation: BAE35947.1.
AK166665 mRNA. Translation: BAE38927.1.
AL663072 Genomic DNA. Translation: CAM18089.1.
BC046623 mRNA. Translation: AAH46623.1.
BC058688 mRNA. Translation: AAH58688.1.
AF136179 Genomic DNA. Translation: AAD33057.1.
AJ000093 Genomic DNA. Translation: CAA03919.1.
AJ000087 expand/collapse EMBL AC list , AJ000088, AJ000089, AJ000090, AJ000091, AJ000092 Genomic DNA. Translation: CAA03918.1.
RefSeqNP_033240.3. NM_009214.3.
XP_001473484.1. XM_001473434.4.
XP_006544632.1. XM_006544569.1.
UniGeneMm.18652.

3D structure databases

ProteinModelPortalP97355.
SMRP97355. Positions 3-366.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP97355. 1 interaction.
MINTMINT-4135428.

PTM databases

PhosphoSiteP97355.

Proteomic databases

PaxDbP97355.
PRIDEP97355.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000112529; ENSMUSP00000108148; ENSMUSG00000071708.
GeneID20603.
671878.
KEGGmmu:20603.
mmu:671878.
UCSCuc009urz.1. mouse.

Organism-specific databases

CTD6611.
MGIMGI:109490. Sms.

Phylogenomic databases

eggNOGNOG259013.
GeneTreeENSGT00620000088036.
HOVERGENHBG004512.
InParanoidP97355.
KOK00802.
OMAARHSTLD.
OrthoDBEOG7G1V6F.
PhylomeDBP97355.
TreeFamTF324508.

Enzyme and pathway databases

UniPathwayUPA00249; UER00315.

Gene expression databases

ArrayExpressP97355.
BgeeP97355.
CleanExMM_SMS.
GenevestigatorP97355.

Family and domain databases

InterProIPR001045. Spermidine/spermine_synthase.
IPR015576. Spermine_synthase.
[Graphical view]
PANTHERPTHR11558. PTHR11558. 1 hit.
PTHR11558:SF1. PTHR11558:SF1. 1 hit.
PfamPF01564. Spermine_synth. 1 hit.
[Graphical view]
PROSITEPS01330. PABS_1. 1 hit.
PS51006. PABS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio298937.
PROP97355.
SOURCESearch...

Entry information

Entry nameSPSY_MOUSE
AccessionPrimary (citable) accession number: P97355
Secondary accession number(s): A2AC82 expand/collapse secondary AC list , Q3TL65, Q3TUP0, Q3UDT8, Q8C7P4, Q9CT09, Q9R282
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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