Reviewed, UniProtKB/Swiss-Prot P51650 (SSDH_RAT)

Names and origin

Protein names

Recommended name:
    Succinate-semialdehyde dehydrogenase, mitochondrial
    EC=1.2.1.24
Alternative name(s):
    NAD(+)-dependent succinic semialdehyde dehydrogenase
    Aldehyde dehydrogenase family 5 member A1

Gene names

Name:	Aldh5a1
Synonyms:	Ssadh

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › 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)

Catalytic activity	Succinate semialdehyde + NAD(+) + H(2)O = succinate + NADH.
Pathway	Amino-acid degradation; 4-aminobutanoate degradation.
Subunit structure	Homotetramer By similarity.
Subcellular location	MitochondrionBy 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	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	central nervous system development Ref.2 Traceable author statement. Source: UniProtKB gamma-aminobutyric acid catabolic process Ref.2 Traceable author statement. Source: UniProtKB oxidation reduction Ref.2 Inferred from direct assay. Source: UniProtKB
Cellular component	mitochondrion Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	succinate-semialdehyde dehydrogenase activity Ref.2 Inferred from direct assay. Source: UniProtKB
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.

Notes: 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
	Chain	36 – 523	488	Succinate-semialdehyde dehydrogenase, mitochondrial		PRO_0000056567
Regions
	Nucleotide binding	272 – 277	6	NADP By similarity
Sites
	Active site	294	1	Proton acceptor By similarity
	Active site	328	1	Nucleophile By similarity
	Site	193	1	Transition state stabilizer By similarity
Amino acid modifications
	Modified residue	67	1	Phosphotyrosine 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		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: 15057822] [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: 7814412] [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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AABR03105019 Genomic DNA. No translation available. L34821 mRNA. Translation: AAA67058.1.
PIR	I61704.
UniGene	Rn.10070
3D structure databases
HSSP	HSSP built from PDB template 1BXS based on UniProtKB P51977.
ModBase	Search...
Genome annotation databases
Ensembl	ENSRNOG00000023538. Rattus norvegicus. [Contig view]
Organism-specific databases
RGD	621422. Aldh5a1.
Phylogenomic databases
HOVERGEN	P51650.
Gene expression databases
ArrayExpress	P51650.
GermOnline	ENSRNOG00000023538. Rattus norvegicus.
Family and domain databases
InterPro	IPR016160. Ald_DHase_CS. IPR016162. Ald_DHase_N. IPR015590. Aldehyde_DHase. IPR010102. Succ_semiAld_DHase. [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	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:	July 22, 2008
This is version 67 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)