ID   AL4A1_MOUSE             Reviewed;         562 AA.
AC   Q8CHT0; Q7TND0; Q8BXM3; Q8R0N1; Q8R1S2;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   16-JUN-2009, entry version 62.
DE   RecName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial;
DE            Short=P5C dehydrogenase;
DE            EC=1.5.1.12;
DE   AltName: Full=Aldehyde dehydrogenase family 4 member A1;
DE   Flags: Precursor;
GN   Name=Aldh4a1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Retina;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Kidney, and Liver;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98; LYS-113 AND LYS-401, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Liver;
RX   PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
RA   Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
RA   Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
RT   "Substrate and functional diversity of lysine acetylation revealed by
RT   a proteomics survey.";
RL   Mol. Cell 23:607-618(2006).
CC   -!- FUNCTION: Irreversible conversion of delta-1-pyrroline-5-
CC       carboxylate (P5C), derived either from proline or ornithine, to
CC       glutamate. This is a necessary step in the pathway interconnecting
CC       the urea and tricarboxylic acid cycles. The preferred substrate is
CC       glutamic gamma-semialdehyde, other substrates include succinic,
CC       glutaric and adipic semialdehydes (By similarity).
CC   -!- CATALYTIC ACTIVITY: (S)-1-pyrroline-5-carboxylate + NAD(P)(+) + 2
CC       H(2)O = L-glutamate + NAD(P)H.
CC   -!- PATHWAY: Amino-acid degradation; L-proline degradation into L-
CC       glutamate; L-glutamate from L-proline: step 2/2.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- PTM: Acetylation of Lys-98, Lys-113 and Lys-401 is observed in
CC       liver mitochondria from fasted mice but not from fed mice.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
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DR   EMBL; AK044712; BAC32045.1; -; mRNA.
DR   EMBL; BC024133; AAH24133.1; -; mRNA.
DR   EMBL; BC026589; AAH26589.1; -; mRNA.
DR   EMBL; BC039281; AAH39281.2; -; mRNA.
DR   EMBL; BC056226; AAH56226.1; -; mRNA.
DR   IPI; IPI00405699; -.
DR   UniGene; Mm.273571; -.
DR   PhosphoSite; Q8CHT0; -.
DR   PRIDE; Q8CHT0; -.
DR   Ensembl; ENSMUSG00000028737; Mus musculus.
DR   KEGG; mmu:212647; -.
DR   MGI; MGI:2443883; Aldh4a1.
DR   HOGENOM; Q8CHT0; -.
DR   HOVERGEN; Q8CHT0; -.
DR   BRENDA; 1.5.1.12; 244.
DR   NextBio; 373656; -.
DR   ArrayExpress; Q8CHT0; -.
DR   Bgee; Q8CHT0; -.
DR   CleanEx; MM_ALDH4A1; -.
DR   GermOnline; ENSMUSG00000028737; Mus musculus.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase act...; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR005931; d-1-pyrroline-5-COlate_DH-1.
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   TIGRFAMs; TIGR01236; D1pyr5carbox1; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Mitochondrion; NAD; Oxidoreductase; Phosphoprotein;
KW   Proline metabolism; Transit peptide.
FT   TRANSIT       1     23       Mitochondrion (By similarity).
FT   CHAIN        24    562       Delta-1-pyrroline-5-carboxylate
FT                                dehydrogenase, mitochondrial.
FT                                /FTId=PRO_0000007174.
FT   NP_BIND     295    300       NAD (By similarity).
FT   ACT_SITE    313    313       By similarity.
FT   ACT_SITE    347    347       By similarity.
FT   MOD_RES      98     98       N6-acetyllysine.
FT   MOD_RES     113    113       N6-acetyllysine.
FT   MOD_RES     401    401       N6-acetyllysine.
FT   MOD_RES     504    504       Phosphotyrosine (By similarity).
FT   CONFLICT     47     47       D -> G (in Ref. 1; BAC32045).
SQ   SEQUENCE   562 AA;  61811 MW;  0AFBF3FAA0C9C367 CRC64;
     MLPLPSLRRS LLSHAWRSAG LRWKHTSSLK VANEPILAFS QGSPERDALQ KALKDLKGQT
     EAIPCVVGDE EVWTSDIQYQ LSPFNHAHKV AKFCYADKAL LNRAIDAALA ARKEWDLKPM
     ADRAQVFLKA ADMLSGPRRA EVLAKTMVGQ GKTVIQAEID AAAELIDFFR FNAKFAVELE
     GEQPISVPPS TNHTVYRGLE GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA
     SYAVYRILRE AGLPPNIIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWRQVAQN
     LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC SRLYVPKSLW
     PQIKGRLLEE HSRIKVGDPA EDFGTFFSAV IDAKAFARIK KWLEHARSSP SLSILAGGQC
     NESVGYYVEP CIIESKDPQE PIMKEEIFGP VLTVYVYPDD KYRETLKLVD STTSYGLTGA
     VFAQDKAIVQ EATRMLRNAA GNFYINDKST GSVVGQQPFG GARASGTNDK PGGPHYILRW
     TSPQVIKETH KPLGDWRYSY MQ
//