Reviewed, UniProtKB/Swiss-Prot Q8CHT0 (AL4A1_MOUSE)

Names and origin

Protein names

Recommended name:
    Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
      Short name=P5C dehydrogenase
    EC=1.5.1.12
Alternative name(s):
    Aldehyde dehydrogenase family 4 member A1

Gene names

Name:

Aldh4a1

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	562 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes By similarity.
Catalytic activity	(S)-1-pyrroline-5-carboxylate + NAD(P)+ + 2 H2O = L-glutamate + NAD(P)H.
Pathway	Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2.
Subunit structure	Homodimer By similarity.
Subcellular location	Mitochondrion matrix By similarity.
Post-translational modification	Acetylation of Lys-98, Lys-113 and Lys-401 is observed in liver mitochondria from fasted mice but not from fed mice.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Biological process	Proline metabolism
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Phosphoprotein
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW proline biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	1-pyrroline-5-carboxylate dehydrogenase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 23	23	Mitochondrion By similarity
	Chain	24 – 562	539	Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial		PRO_0000007174
Regions
	Nucleotide binding	295 – 300	6	NAD By similarity
Sites
	Active site	313	1	By similarity
	Active site	347	1	By similarity
Amino acid modifications
	Modified residue	98	1	N6-acetyllysine Ref.3
	Modified residue	113	1	N6-acetyllysine Ref.3
	Modified residue	401	1	N6-acetyllysine Ref.3
	Modified residue	504	1	Phosphotyrosine By similarity
Experimental info
	Sequence conflict	47	1	D → G in BAC32045. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8CHT0-1 [UniParc]. Last modified March 1, 2004. Version 2. Checksum: 0AFBF3FAA0C9C367	FASTA	562	61,811
	10 20 30 40 50 60 MLPLPSLRRS LLSHAWRSAG LRWKHTSSLK VANEPILAFS QGSPERDALQ KALKDLKGQT 70 80 90 100 110 120 EAIPCVVGDE EVWTSDIQYQ LSPFNHAHKV AKFCYADKAL LNRAIDAALA ARKEWDLKPM 130 140 150 160 170 180 ADRAQVFLKA ADMLSGPRRA EVLAKTMVGQ GKTVIQAEID AAAELIDFFR FNAKFAVELE 190 200 210 220 230 240 GEQPISVPPS TNHTVYRGLE GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA 250 260 270 280 290 300 SYAVYRILRE AGLPPNIIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWRQVAQN 310 320 330 340 350 360 LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC SRLYVPKSLW 370 380 390 400 410 420 PQIKGRLLEE HSRIKVGDPA EDFGTFFSAV IDAKAFARIK KWLEHARSSP SLSILAGGQC 430 440 450 460 470 480 NESVGYYVEP CIIESKDPQE PIMKEEIFGP VLTVYVYPDD KYRETLKLVD STTSYGLTGA 490 500 510 520 530 540 VFAQDKAIVQ EATRMLRNAA GNFYINDKST GSVVGQQPFG GARASGTNDK PGGPHYILRW 550 560 TSPQVIKETH KPLGDWRYSY MQ

References

[1]	"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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Retina.
[2]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: FVB/N. Tissue: Kidney and Liver.
[3]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98; LYS-113 AND LYS-401, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK044712 mRNA. Translation: BAC32045.1. BC024133 mRNA. Translation: AAH24133.1. BC026589 mRNA. Translation: AAH26589.1. BC039281 mRNA. Translation: AAH39281.2. BC056226 mRNA. Translation: AAH56226.1.
IPI	IPI00405699.
UniGene	Mm.273571
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	Q8CHT0.
Proteomic databases
PRIDE	Q8CHT0.
Genome annotation databases
Ensembl	ENSMUSG00000028737. Mus musculus. [Contig view]
KEGG	mmu:212647.
Organism-specific databases
MGI	MGI:2443883. Aldh4a1.
Phylogenomic databases
HOGENOM	Q8CHT0.
HOVERGEN	Q8CHT0.
Enzyme and pathway databases
BRENDA	1.5.1.12. 244.
Gene expression databases
ArrayExpress	Q8CHT0.
Bgee	Q8CHT0.
CleanEx	MM_ALDH4A1.
GermOnline	ENSMUSG00000028737. Mus musculus.
Family and domain databases
InterPro	IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. IPR005931. d-1-pyrroline-5-COlate_DH-1. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
TIGRFAMs	TIGR01236. D1pyr5carbox1. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	373656.
SOURCE	Search...

Entry information

Entry name

AL4A1_MOUSE

Accession

Primary (citable) accession number: Q8CHT0
Secondary accession number(s): Q7TND0 , Q8BXM3, Q8R0N1, Q8R1S2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	March 1, 2004
Last modified:	June 16, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)