P51650 (SSDH_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Succinate-semialdehyde dehydrogenase, mitochondrial
EC=1.2.1.24

Alternative name(s):
Aldehyde dehydrogenase family 5 member A1
NAD(+)-dependent succinic semialdehyde dehydrogenase

Gene names

Name:	Aldh5a1
Synonyms:	Ssadh

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	523 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	Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) By similarity.
Catalytic activity	Succinate semialdehyde + NAD+ + H2O = succinate + NADH.
Enzyme regulation	Redox-regulated. Inhibited under oxydizing conditions By similarity.
Pathway	Amino-acid degradation; 4-aminobutanoate degradation.
Subunit structure	Homotetramer By similarity.
Subcellular location	Mitochondrion By similarity.
Tissue specificity	Brain, pancreas, heart, liver, skeletal muscle, kidney. Lower in spleen, lung, kidney and testis.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Alternative splicing
Domain	Transit peptide
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation Disulfide bond Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	central nervous system development Inferred from sequence or structural similarity. Source: UniProtKB gamma-aminobutyric acid catabolic process Inferred from sequence or structural similarity. Source: UniProtKB succinate metabolic process Inferred from direct assay PubMed 12527414PubMed 12871571PubMed 7262085. Source: RGD
Cellular_component	mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	NAD binding Inferred from direct assay PubMed 12527414PubMed 12871571PubMed 7262085. Source: RGD carboxylic acid binding Inferred from physical interaction PubMed 12527414PubMed 7262085. Source: RGD succinate-semialdehyde dehydrogenase (NAD+) activity Inferred from direct assay Ref.2. Source: UniProtKB succinate-semialdehyde dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P51650-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Short (identifier: P51650-2)

The sequence of this isoform differs from the canonical sequence as follows:
     107-134: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 35	35	Mitochondrion Ref.2 Ref.3
	Chain	36 – 523	488	Succinate-semialdehyde dehydrogenase, mitochondrial		PRO_0000056567
Regions
	Nucleotide binding	216 – 219	4	NAD By similarity
	Nucleotide binding	272 – 277	6	NAD By similarity
Sites
	Active site	294	1	Proton acceptor By similarity
	Active site	328	1	Nucleophile By similarity
	Binding site	201	1	NAD By similarity
	Binding site	201	1	Substrate By similarity
	Binding site	322	1	Substrate By similarity
	Binding site	486	1	Substrate By similarity
	Site	193	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	67	1	Phosphotyrosine By similarity
	Modified residue	114	1	N6-acetyllysine By similarity
	Disulfide bond	328 ↔ 330		In inhibited form By similarity
Natural variations
	Alternative sequence	107 – 134	28	Missing in isoform Short.		VSP_001284

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified April 8, 2008. Version 2. Checksum: 4CA521139C9FA98F	FASTA	523	56,131
	10 20 30 40 50 60 MATCFLLRNF CAARPALRPP GRLLREPAGA QRRSYVGGPA DLHADLLRGD SFVGGRWLPT 70 80 90 100 110 120 PATFPVYDPA SGAKLGTVAD CGVPEARAAV RAAYDAFSSW KEISVKERSS LLRKWYDLMI 130 140 150 160 170 180 QNKDELAKII TAESGKPLKE AQGEILYSAF FLEWFSEEAR RVYGDIIYTS AKDKRGLVLK 190 200 210 220 230 240 QPVGVASIIT PWNFPSAMIT RKVGAALAAG CTVVVKPAED TPYSALALAQ LANQAGIPPG 250 260 270 280 290 300 VYNVIPCSRT KAKEVGEVLC TDPLVSKISF TGSTATGKIL LHHAANSVKR VSMELGGLAP 310 320 330 340 350 360 FIVFDSANVD QAVAGAMASK FRNAGQTCVC SNRFLVQRGI HDSFVTKFAE AMKKSLRVGN 370 380 390 400 410 420 GFEEGTTQGP LINEKAVEKV EKHVNDAVAK GATVVTGGKR HQSGGNFFEP TLLSNVTRDM 430 440 450 460 470 480 LCITEETFGP VAPVIKFDKE EEAVAIANAA DVGLAGYFYS QDPAQIWRVA EQLEVGMVGV 490 500 510 520 NEGLISSVEC PFGGVKQSGL GREGSKYGID EYLEVKYVCY GGL
	Isoform Short [UniParc]. Checksum: FC69A1D9215CEF5F	FASTA	495	52,798
	10 20 30 40 50 60 MATCFLLRNF CAARPALRPP GRLLREPAGA QRRSYVGGPA DLHADLLRGD SFVGGRWLPT 70 80 90 100 110 120 PATFPVYDPA SGAKLGTVAD CGVPEARAAV RAAYDAFSSW KEISVKGKPL KEAQGEILYS 130 140 150 160 170 180 AFFLEWFSEE ARRVYGDIIY TSAKDKRGLV LKQPVGVASI ITPWNFPSAM ITRKVGAALA 190 200 210 220 230 240 AGCTVVVKPA EDTPYSALAL AQLANQAGIP PGVYNVIPCS RTKAKEVGEV LCTDPLVSKI 250 260 270 280 290 300 SFTGSTATGK ILLHHAANSV KRVSMELGGL APFIVFDSAN VDQAVAGAMA SKFRNAGQTC 310 320 330 340 350 360 VCSNRFLVQR GIHDSFVTKF AEAMKKSLRV GNGFEEGTTQ GPLINEKAVE KVEKHVNDAV 370 380 390 400 410 420 AKGATVVTGG KRHQSGGNFF EPTLLSNVTR DMLCITEETF GPVAPVIKFD KEEEAVAIAN 430 440 450 460 470 480 AADVGLAGYF YSQDPAQIWR VAEQLEVGMV GVNEGLISSV ECPFGGVKQS GLGREGSKYG 490 IDEYLEVKYV CYGGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genome sequence of the Brown Norway rat yields insights into mammalian evolution." Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M. , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S. Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Brown Norway.
[2]	"Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression." Chambliss K.L., Caudle D.L., Hinson D.D., Moomaw C.R., Slaughter C.A., Jakobs C., Gibson K.M. J. Biol. Chem. 270:461-467(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), PROTEIN SEQUENCE OF 36-84; 92-101; 129-153; 162-172; 303-311; 419-425 AND 503-526. Strain: Sprague-Dawley. Tissue: Brain.
[3]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 36-48; 161-172 AND 401-418, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AABR03105019 Genomic DNA. No translation available. L34821 mRNA. Translation: AAA67058.1.
IPI	IPI00231644. IPI00362992.
PIR	I61704.
UniGene	Rn.10070.
3D structure databases
ProteinModelPortal	P51650.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000035601.
PTM databases
PhosphoSite	P51650.
2D gel databases
World-2DPAGE	0004:P51650.
Proteomic databases
PaxDb	P51650.
PRIDE	P51650.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
UCSC	RGD:621422. rat.
Organism-specific databases
RGD	621422. Aldh5a1.
Phylogenomic databases
eggNOG	COG1012.
HOGENOM	HOG000271509.
HOVERGEN	HBG108515.
InParanoid	P51650.
OrthoDB	EOG4255SZ.
Enzyme and pathway databases
SABIO-RK	P51650.
UniPathway	UPA00733.
Gene expression databases
ArrayExpress	P51650.
Genevestigator	P51650.
GermOnline	ENSRNOG00000023538. Rattus norvegicus.
Family and domain databases
Gene3D	3.40.309.10. 1 hit. 3.40.605.10. 1 hit.
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR010102. Succ_semiAld_DH. [Graphical view]
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
TIGRFAMs	TIGR01780. SSADH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SSDH_RAT

Accession

Primary (citable) accession number: P51650

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	April 8, 2008
Last modified:	April 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program