DCAM1_MOUSE
ID DCAM1_MOUSE Reviewed; 334 AA.
AC P0DMN7; P31154; P82184; Q58E47;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme 1;
DE Short=AdoMetDC 1;
DE Short=SAMDC 1;
DE EC=4.1.1.50 {ECO:0000250|UniProtKB:P17707};
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase 1 alpha chain;
DE Contains:
DE RecName: Full=S-adenosylmethionine decarboxylase 1 beta chain;
DE Flags: Precursor;
GN Name=Amd1;
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 STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=1449493; DOI=10.1016/0006-291x(92)91575-b;
RA Waris T., Ihalainen R., Keraenen M.-R., Pajunen A.;
RT "Molecular cloning of the mouse S-adenosylmethionine decarboxylase cDNA:
RT specific protein binding to the conserved region of the mRNA 5'-
RT untranslated region.";
RL Biochem. Biophys. Res. Commun. 189:424-429(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8344293; DOI=10.1111/j.1432-1033.1993.tb18029.x;
RA Suzuki T., Sadakata Y., Kashiwagi K., Hoshino K., Kakinuma Y.,
RA Shirahata A., Igarashi K.;
RT "Overproduction of S-adenosylmethionine decarboxylase in ethylglyoxal-
RT bis(guanylhydrazone)-resistant mouse FM3A cells.";
RL Eur. J. Biochem. 215:247-253(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/SvJ; TISSUE=Spleen;
RX PubMed=10570962; DOI=10.1016/s0378-1119(99)00355-8;
RA Nishimura K., Kashiwagi K., Matsuda Y., Jaenne O.A., Igarashi K.;
RT "Gene structure and chromosomal localization of mouse S-adenosylmethionine
RT decarboxylase.";
RL Gene 238:343-350(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Embryonic kidney, and Mammary gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Brain, Eye, and 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 [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=11856372; DOI=10.1046/j.1356-9597.2001.00494.x;
RA Nishimura K., Nakatsu F., Kashiwagi K., Ohno H., Saito T., Igarashi K.;
RT "Essential role of S-adenosylmethionine decarboxylase in mouse embryonic
RT development.";
RL Genes Cells 7:41-47(2002).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=22391449; DOI=10.1101/gad.182998.111;
RA Zhang D., Zhao T., Ang H.S., Chong P., Saiki R., Igarashi K., Yang H.,
RA Vardy L.A.;
RT "AMD1 is essential for ESC self-renewal and is translationally down-
RT regulated on differentiation to neural precursor cells.";
RL Genes Dev. 26:461-473(2012).
CC -!- FUNCTION: Essential for biosynthesis of the polyamines spermidine and
CC spermine. Promotes maintenance and self-renewal of embryonic stem
CC cells, by maintaining spermine levels. {ECO:0000269|PubMed:22391449}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + S-adenosyl-L-methionine = CO2 + S-adenosyl 3-
CC (methylsulfanyl)propylamine; Xref=Rhea:RHEA:15981, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:57443, ChEBI:CHEBI:59789; EC=4.1.1.50;
CC Evidence={ECO:0000250|UniProtKB:P17707};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Note=Binds 1 pyruvoyl group covalently per subunit.;
CC -!- PATHWAY: Amine and polyamine biosynthesis; S-adenosylmethioninamine
CC biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine:
CC step 1/1.
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P0DMN7; P98083: Shc1; NbExp=7; IntAct=EBI-644529, EBI-300201;
CC -!- TISSUE SPECIFICITY: Expressed in embryonic stem cells; subsequently
CC down-regulated in differentiating neural precursor cells.
CC {ECO:0000269|PubMed:22391449}.
CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC the active enzyme involves a self-maturation process in which the
CC active site pyruvoyl group is generated from an internal serine residue
CC via an autocatalytic post-translational modification. Two non-identical
CC subunits are generated from the proenzyme in this reaction, and the
CC pyruvate is formed at the N-terminus of the alpha chain, which is
CC derived from the carboxyl end of the proenzyme. The post-translation
CC cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC in which the side chain hydroxyl group of the serine supplies its
CC oxygen atom to form the C-terminus of the beta chain, while the
CC remainder of the serine residue undergoes an oxidative deamination to
CC produce ammonia and the pyruvoyl group blocking the N-terminus of the
CC alpha chain. {ECO:0000250|UniProtKB:P17707}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal with developmental arrest
CC between E3.5 and E6.5. Arrest of blastocysts cultured in vitro is
CC rescued by the addition of spermidine. {ECO:0000269|PubMed:11856372}.
CC -!- SIMILARITY: Belongs to the eukaryotic AdoMetDC 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; Z14986; CAA78710.1; -; mRNA.
DR EMBL; D12780; BAA02243.1; -; mRNA.
DR EMBL; AB025024; BAA83784.1; -; Genomic_DNA.
DR EMBL; AK146840; BAE27473.1; -; mRNA.
DR EMBL; AK166187; BAE38617.1; -; mRNA.
DR EMBL; AK168165; BAE40126.1; -; mRNA.
DR EMBL; CT010192; CAJ18400.1; -; mRNA.
DR EMBL; CH466540; EDL04951.1; -; Genomic_DNA.
DR EMBL; BC011110; AAH11110.1; -; mRNA.
DR EMBL; BC071220; AAH71220.1; -; mRNA.
DR EMBL; BC080791; AAH80791.1; -; mRNA.
DR EMBL; BC092072; AAH92072.1; -; mRNA.
DR EMBL; BC138696; AAI38697.1; -; mRNA.
DR EMBL; BC138697; AAI38698.1; -; mRNA.
DR CCDS; CCDS48544.1; -.
DR RefSeq; NP_033795.1; NM_009665.5.
DR AlphaFoldDB; P0DMN7; -.
DR SMR; P0DMN7; -.
DR BioGRID; 198087; 1.
DR IntAct; P0DMN7; 3.
DR MINT; P0DMN7; -.
DR STRING; 10090.ENSMUSP00000097528; -.
DR ChEMBL; CHEMBL3584; -.
DR iPTMnet; P0DMN7; -.
DR PhosphoSitePlus; P0DMN7; -.
DR EPD; P0DMN7; -.
DR PaxDb; P0DMN7; -.
DR DNASU; 11702; -.
DR Ensembl; ENSMUST00000099945; ENSMUSP00000097528; ENSMUSG00000075232.
DR Ensembl; ENSMUST00000238969; ENSMUSP00000159133; ENSMUSG00000075232.
DR GeneID; 11702; -.
DR KEGG; mmu:11702; -.
DR CTD; 262; -.
DR MGI; MGI:88004; Amd1.
DR VEuPathDB; HostDB:ENSMUSG00000075232; -.
DR eggNOG; KOG0788; Eukaryota.
DR GeneTree; ENSGT00390000011776; -.
DR HOGENOM; CLU_023050_1_0_1; -.
DR OMA; LEIWFEE; -.
DR OrthoDB; 932490at2759; -.
DR PhylomeDB; P0DMN7; -.
DR BRENDA; 4.1.1.50; 3474.
DR Reactome; R-MMU-351202; Metabolism of polyamines.
DR UniPathway; UPA00331; UER00451.
DR BioGRID-ORCS; 11702; 16 hits in 74 CRISPR screens.
DR ChiTaRS; Amd1; mouse.
DR PRO; PR:P0DMN7; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P0DMN7; protein.
DR Bgee; ENSMUSG00000075232; Expressed in quadriceps femoris and 113 other tissues.
DR ExpressionAtlas; P0DMN7; baseline and differential.
DR Genevisible; P0DMN7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019810; F:putrescine binding; ISO:MGI.
DR GO; GO:0006595; P:polyamine metabolic process; ISO:MGI.
DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0046500; P:S-adenosylmethionine metabolic process; ISO:MGI.
DR GO; GO:0008295; P:spermidine biosynthetic process; ISO:MGI.
DR GO; GO:0006597; P:spermine biosynthetic process; ISO:MGI.
DR InterPro; IPR001985; S-AdoMet_decarboxylase.
DR InterPro; IPR016067; S-AdoMet_deCO2ase_core.
DR InterPro; IPR018166; S-AdoMet_deCO2ase_CS.
DR PANTHER; PTHR11570; PTHR11570; 1.
DR Pfam; PF01536; SAM_decarbox; 1.
DR PIRSF; PIRSF001355; S-AdenosylMet_decarboxylase; 1.
DR SUPFAM; SSF56276; SSF56276; 1.
DR TIGRFAMs; TIGR00535; SAM_DCase; 1.
DR PROSITE; PS01336; ADOMETDC; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Decarboxylase; Lyase; Phosphoprotein;
KW Polyamine biosynthesis; Pyruvate; Reference proteome;
KW S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis; Zymogen.
FT CHAIN 1..67
FT /note="S-adenosylmethionine decarboxylase 1 beta chain"
FT /id="PRO_0000029963"
FT CHAIN 68..334
FT /note="S-adenosylmethionine decarboxylase 1 alpha chain"
FT /id="PRO_0000029964"
FT ACT_SITE 8
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 11
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 68
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 82
FT /note="Proton donor; for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 229
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT ACT_SITE 243
FT /note="Proton acceptor; for processing activity"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 7
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT BINDING 247
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT SITE 67..68
FT /note="Cleavage (non-hydrolytic); by autolysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT MOD_RES 68
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P17707"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17707"
SQ SEQUENCE 334 AA; 38272 MW; 7950A1E9A9ACBD72 CRC64;
MEAAHFFEGT EKLLEVWFSR QQSDASQGSG DLRTIPRSEW DVLLKDVQCS IISVTKTDKQ
EAYVLSESSM FVSKRRFILK TCGTTLLLKA LVPLLKLARD YSGFDSIQSF FYSRKNFMKP
SHQGYPHRNF QEEIEFLNAI FPNGAAYCMG RMNSDCWYLY TLDFPESRVI SQPDQTLEIL
MSELDPAVMD QFYMKDGVTA KDVTRESGIR DLIPGSVIDA TLFNPCGYSM NGMKSDGTYW
TIHITPEPEF SYVSFETNLS QTSYDDLIRK VVEVFKPGKF VTTLFVNQSS KCRTVLSSPQ
KIDGFKRLDC QSAMFNDYNF VFTSFAKKQQ QQQS
