SPEE_MOUSE
ID SPEE_MOUSE Reviewed; 302 AA.
AC Q64674;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Spermidine synthase;
DE Short=SPDSY;
DE EC=2.5.1.16;
DE AltName: Full=Putrescine aminopropyltransferase;
GN Name=Srm;
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].
RC TISSUE=Kidney;
RX PubMed=7803821; DOI=10.3109/10425179409020863;
RA Myoehaenen S., Wahlfors J., Alhonen L., Jaenne J.;
RT "Nucleotide sequence of mouse spermidine synthase cDNA.";
RL DNA Seq. 4:343-346(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=129/SvJ; TISSUE=Liver;
RA Kolu P.V., Kauppinen L., Halmekytoe M., Alhonen L., Jaenne J.;
RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: Catalyzes the production of spermidine from putrescine and
CC decarboxylated S-adenosylmethionine (dcSAM). Has a strong preference
CC for putrescine as substrate, and has very low activity towards 1,3-
CC diaminopropane. Has extremely low activity towards spermidine (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) +
CC S-methyl-5'-thioadenosine + spermidine; Xref=Rhea:RHEA:12721,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:57443,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:326268; EC=2.5.1.16;
CC -!- ACTIVITY REGULATION: The activity is thought to be regulated mainly by
CC the availability of decarboxylated S-adenosylmethionine.
CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine biosynthesis;
CC spermidine from putrescine: step 1/1.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family.
CC {ECO:0000305}.
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DR EMBL; Z67748; CAA91561.1; -; Genomic_DNA.
DR EMBL; L19311; AAC37666.1; -; mRNA.
DR EMBL; BC005566; AAH05566.1; -; mRNA.
DR CCDS; CCDS18940.1; -.
DR RefSeq; NP_033298.1; NM_009272.4.
DR AlphaFoldDB; Q64674; -.
DR SMR; Q64674; -.
DR BioGRID; 203498; 2.
DR STRING; 10090.ENSMUSP00000006611; -.
DR iPTMnet; Q64674; -.
DR PhosphoSitePlus; Q64674; -.
DR SwissPalm; Q64674; -.
DR REPRODUCTION-2DPAGE; Q64674; -.
DR EPD; Q64674; -.
DR jPOST; Q64674; -.
DR MaxQB; Q64674; -.
DR PaxDb; Q64674; -.
DR PRIDE; Q64674; -.
DR ProteomicsDB; 261128; -.
DR Antibodypedia; 13673; 256 antibodies from 28 providers.
DR DNASU; 20810; -.
DR Ensembl; ENSMUST00000006611; ENSMUSP00000006611; ENSMUSG00000006442.
DR GeneID; 20810; -.
DR KEGG; mmu:20810; -.
DR UCSC; uc008vuw.1; mouse.
DR CTD; 6723; -.
DR MGI; MGI:102690; Srm.
DR VEuPathDB; HostDB:ENSMUSG00000006442; -.
DR eggNOG; KOG1562; Eukaryota.
DR GeneTree; ENSGT00870000136521; -.
DR HOGENOM; CLU_048199_3_1_1; -.
DR InParanoid; Q64674; -.
DR OMA; LWPGQSF; -.
DR OrthoDB; 1059849at2759; -.
DR PhylomeDB; Q64674; -.
DR TreeFam; TF314466; -.
DR Reactome; R-MMU-351202; Metabolism of polyamines.
DR UniPathway; UPA00248; UER00314.
DR BioGRID-ORCS; 20810; 12 hits in 73 CRISPR screens.
DR ChiTaRS; Srm; mouse.
DR PRO; PR:Q64674; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q64674; protein.
DR Bgee; ENSMUSG00000006442; Expressed in somite and 276 other tissues.
DR ExpressionAtlas; Q64674; baseline and differential.
DR Genevisible; Q64674; MM.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0004766; F:spermidine synthase activity; ISS:UniProtKB.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0008295; P:spermidine biosynthetic process; ISS:UniProtKB.
DR Gene3D; 2.30.140.10; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_00198; Spermidine_synth; 1.
DR InterPro; IPR030374; PABS.
DR InterPro; IPR030373; PABS_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001045; Spermi_synthase.
DR InterPro; IPR030668; Spermi_synthase_euk.
DR InterPro; IPR035246; Spermidine_synt_N.
DR InterPro; IPR037163; Spermidine_synt_N_sf.
DR PANTHER; PTHR11558; PTHR11558; 1.
DR Pfam; PF17284; Spermine_synt_N; 1.
DR PIRSF; PIRSF000502; Spermidine_synth; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00417; speE; 1.
DR PROSITE; PS01330; PABS_1; 1.
DR PROSITE; PS51006; PABS_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Polyamine biosynthesis; Reference proteome;
KW Spermidine biosynthesis; Transferase.
FT CHAIN 1..302
FT /note="Spermidine synthase"
FT /id="PRO_0000156446"
FT DOMAIN 18..253
FT /note="PABS"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 49
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 104
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 155..156
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 173..176
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT BINDING 173
FT /ligand="S-adenosyl 3-(methylsulfanyl)propylamine"
FT /ligand_id="ChEBI:CHEBI:57443"
FT /evidence="ECO:0000250"
FT BINDING 241
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P19623"
SQ SEQUENCE 302 AA; 33995 MW; 4C19B7AA3518054F CRC64;
MEPGPDGPAA PGPAAIREGW FRETCSLWPG QALSLQVEQL LHHRRSRYQD ILVFRSKTYG
NVLVLDGVIQ CTERDEFSYQ EMIANLPLCS HPNPRKVLII GGGDGGVLRE VVKHPSVESV
VQCEIDEDVI EVSKKFLPGM AVGFSSSKLT LHVGDGFEFM KQNQDAFDVI ITDSSDPMGP
AESLFKESYY QLMKTALKED GILCCQGECQ WLHLDLIKEM RHFCKSLFPV VDYAYCSIPT
YPSGQIGFML CSKNPSTNFR EPVQQLTQAQ VEQMQLKYYN SDMHRAAFVL PEFTRKALND
IS
