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Protein

Spermine synthase

Gene

Sms

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM) (By similarity). Required for normal viability, growth and fertility.By similarity1 Publication

Catalytic activityi

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

Pathway: spermine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes spermine from spermidine.
Proteins known to be involved in this subpathway in this organism are:
  1. Spermine synthase (Sms)
This subpathway is part of the pathway spermine biosynthesis, which is itself part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes spermine from spermidine, the pathway spermine biosynthesis and in Amine and polyamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei148 – 1481S-adenosylmethioninamineBy similarity
Binding sitei177 – 1771SpermidineBy similarity
Binding sitei201 – 2011SpermidineBy similarity
Binding sitei220 – 2201S-adenosylmethioninamineBy similarity
Active sitei276 – 2761Proton acceptorPROSITE-ProRule annotation
Binding sitei351 – 3511SpermidineBy similarity
Binding sitei353 – 3531SpermidineBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Polyamine biosynthesis

Enzyme and pathway databases

ReactomeiREACT_282719. Metabolism of polyamines.
UniPathwayiUPA00249; UER00315.

Names & Taxonomyi

Protein namesi
Recommended name:
Spermine synthase (EC:2.5.1.22)
Short name:
SPMSY
Alternative name(s):
Spermidine aminopropyltransferase
Gene namesi
Name:Sms
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:109490. Sms.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Mouse ES cells lacking Sms display normal growth rates but are sensitive to antiproliferative and DNA damage-inducing drugs.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 366365Spermine synthasePRO_0000156539Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP97355.
PaxDbiP97355.
PRIDEiP97355.

PTM databases

PhosphoSiteiP97355.

Expressioni

Gene expression databases

BgeeiP97355.
CleanExiMM_SMS.
ExpressionAtlasiP97355. baseline and differential.
GenevisibleiP97355. MM.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

IntActiP97355. 1 interaction.
MINTiMINT-4135428.
STRINGi10090.ENSMUSP00000108148.

Structurei

3D structure databases

ProteinModelPortaliP97355.
SMRiP97355. Positions 3-366.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini122 – 362241PABSPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni255 – 2562S-adenosylmethioninamine bindingBy similarity

Domaini

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).By similarity

Sequence similaritiesi

Contains 1 PABS (polyamine biosynthesis) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG259013.
GeneTreeiENSGT00620000088036.
HOVERGENiHBG004512.
InParanoidiP97355.
KOiK00802.
OMAiQGNCINL.
OrthoDBiEOG7G1V6F.
PhylomeDBiP97355.
TreeFamiTF324508.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR030374. PABS.
IPR030373. PABS_CS.
IPR029063. SAM-dependent_MTases.
IPR015576. Spermine_synthase_animal.
[Graphical view]
PANTHERiPTHR11558:SF27. PTHR11558:SF27. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01330. PABS_1. 1 hit.
PS51006. PABS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P97355-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAARHSTLD FKLGAKADGE AILKGLQSIF QEQGMTESVH TWQDHGYLAT
60 70 80 90 100
YTNKNGSFAN LRIYPHGLVL LDLQSYDSDV QGKQETDSLL NKIEEKMKEL
110 120 130 140 150
SQDSTGRVKR LPPIVRGGAI DRYWPTADGR LVEYDIDEVV YDEDSPYQNI
160 170 180 190 200
KILHSKQFGN ILILSGDVNL AESDLAYTRA IMGSGKEDYT GKDVLILGGG
210 220 230 240 250
DGGILCEIVK LKPKMVTMVE IDQMVIDGCK KYMRRTCGDV LDNLRGDCYQ
260 270 280 290 300
VLIEDCIPVL KMYAKEGREF DYVINDLTAV PISTSPEEDS TWDFLRLILD
310 320 330 340 350
LSMKVLKQDG KYFTQGNCVN LTEALSLYEE QLGRLYCPVE FSKEIVCVPS
360
YLELWVFYTV WKKAKP
Length:366
Mass (Da):41,313
Last modified:May 1, 1997 - v1
Checksum:iD549F319F51C43C5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881D → H in BAC33920 (PubMed:16141072).Curated
Sequence conflicti245 – 2451R → K in BAC33920 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
, AJ000088, AJ000089, AJ000090, AJ000091, AJ000092 Genomic DNA. Translation: CAA03918.1.
CCDSiCCDS41189.1.
RefSeqiNP_033240.3. NM_009214.3.
XP_001473484.1. XM_001473434.5.
XP_006544632.1. XM_006544569.2.
UniGeneiMm.18652.

Genome annotation databases

EnsembliENSMUST00000112529; ENSMUSP00000108148; ENSMUSG00000071708.
GeneIDi20603.
671878.
KEGGimmu:20603.
mmu:671878.
UCSCiuc009urz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
, AJ000088, AJ000089, AJ000090, AJ000091, AJ000092 Genomic DNA. Translation: CAA03918.1.
CCDSiCCDS41189.1.
RefSeqiNP_033240.3. NM_009214.3.
XP_001473484.1. XM_001473434.5.
XP_006544632.1. XM_006544569.2.
UniGeneiMm.18652.

3D structure databases

ProteinModelPortaliP97355.
SMRiP97355. Positions 3-366.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP97355. 1 interaction.
MINTiMINT-4135428.
STRINGi10090.ENSMUSP00000108148.

PTM databases

PhosphoSiteiP97355.

Proteomic databases

MaxQBiP97355.
PaxDbiP97355.
PRIDEiP97355.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000112529; ENSMUSP00000108148; ENSMUSG00000071708.
GeneIDi20603.
671878.
KEGGimmu:20603.
mmu:671878.
UCSCiuc009urz.1. mouse.

Organism-specific databases

CTDi6611.
MGIiMGI:109490. Sms.

Phylogenomic databases

eggNOGiNOG259013.
GeneTreeiENSGT00620000088036.
HOVERGENiHBG004512.
InParanoidiP97355.
KOiK00802.
OMAiQGNCINL.
OrthoDBiEOG7G1V6F.
PhylomeDBiP97355.
TreeFamiTF324508.

Enzyme and pathway databases

UniPathwayiUPA00249; UER00315.
ReactomeiREACT_282719. Metabolism of polyamines.

Miscellaneous databases

NextBioi298937.
PROiP97355.
SOURCEiSearch...

Gene expression databases

BgeeiP97355.
CleanExiMM_SMS.
ExpressionAtlasiP97355. baseline and differential.
GenevisibleiP97355. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR030374. PABS.
IPR030373. PABS_CS.
IPR029063. SAM-dependent_MTases.
IPR015576. Spermine_synthase_animal.
[Graphical view]
PANTHERiPTHR11558:SF27. PTHR11558:SF27. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01330. PABS_1. 1 hit.
PS51006. PABS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSPSY_MOUSE
AccessioniPrimary (citable) accession number: P97355
Secondary accession number(s): A2AC82
, Q3TL65, Q3TUP0, Q3UDT8, Q8C7P4, Q9CT09, Q9R282
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1997
Last modified: June 24, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.