ID SSDH_RAT Reviewed; 523 AA. AC P51650; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 2. DT 22-JUL-2008, entry version 67. DE RecName: Full=Succinate-semialdehyde dehydrogenase, mitochondrial; DE EC=1.2.1.24; DE AltName: Full=NAD(+)-dependent succinic semialdehyde dehydrogenase; DE AltName: Full=Aldehyde dehydrogenase family 5 member A1; DE Flags: Precursor; GN Name=Aldh5a1; Synonyms=Ssadh; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Brown Norway; RX PubMed=15057822; DOI=10.1038/nature02426; RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., RA Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., RA Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., RA Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., RA Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., RA Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., RA Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., RA Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., RA Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., RA D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., RA Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., RA Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., RA Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., RA Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., RA Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., RA Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., RA Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., RA Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., RA Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., RA Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., RA Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., RA Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., RA Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., RA Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., RA Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., RA Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., RA Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., RA Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., RA Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., RA Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., RA Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., RA Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., RA Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., RA Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., RA Collins F.S.; RT "Genome sequence of the Brown Norway rat yields insights into RT mammalian evolution."; RL Nature 428:493-521(2004). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND PROTEIN RP SEQUENCE OF 36-84; 92-101; 129-153; 162-172; 303-311; 419-425 AND RP 503-526. RC STRAIN=Sprague-Dawley; TISSUE=Brain; RX MEDLINE=95113870; PubMed=7814412; DOI=10.1074/jbc.270.1.461; RA Chambliss K.L., Caudle D.L., Hinson D.D., Moomaw C.R., Slaughter C.A., RA Jakobs C., Gibson K.M.; RT "Molecular cloning of the mature NAD(+)-dependent succinic RT semialdehyde dehydrogenase from rat and human. cDNA isolation, RT evolutionary homology, and tissue expression."; RL J. Biol. Chem. 270:461-467(1995). RN [3] RP PROTEIN SEQUENCE OF 36-48; 161-172 AND 401-418, AND MASS SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord; RA Lubec G., Afjehi-Sadat L.; RL Submitted (NOV-2006) to UniProtKB. CC -!- CATALYTIC ACTIVITY: Succinate semialdehyde + NAD(+) + H(2)O = CC succinate + NADH. CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation. CC -!- SUBUNIT: Homotetramer (By similarity). CC -!- SUBCELLULAR LOCATION: Mitochondrion (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Long; CC IsoId=P51650-1; Sequence=Displayed; CC Name=Short; CC IsoId=P51650-2; Sequence=VSP_001284; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Brain, pancreas, heart, liver, skeletal CC muscle, kidney. Lower in spleen, lung, kidney and testis. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AABR03105019; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L34821; AAA67058.1; -; mRNA. DR PIR; I61704; I61704. DR UniGene; Rn.10070; -. DR HSSP; P51977; 1BXS. DR Ensembl; ENSRNOG00000023538; Rattus norvegicus. DR RGD; 621422; Aldh5a1. DR HOVERGEN; P51650; -. DR ArrayExpress; P51650; -. DR GermOnline; ENSRNOG00000023538; Rattus norvegicus. DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB. DR GO; GO:0004777; F:succinate-semialdehyde dehydrogenase activity; IDA:UniProtKB. DR GO; GO:0007417; P:central nervous system development; TAS:UniProtKB. DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; TAS:UniProtKB. DR GO; GO:0055114; P:oxidation reduction; IDA:UniProtKB. DR InterPro; IPR016160; Ald_DHase_CS. DR InterPro; IPR016162; Ald_DHase_N. DR InterPro; IPR015590; Aldehyde_DHase. DR InterPro; IPR010102; Succ_semiAld_DHase. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR Pfam; PF00171; Aldedh; 1. DR TIGRFAMs; TIGR01780; SSADH; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Alternative splicing; Direct protein sequencing; Mitochondrion; NAD; KW Oxidoreductase; Phosphoprotein; Transit peptide. FT TRANSIT 1 35 Mitochondrion. FT CHAIN 36 523 Succinate-semialdehyde dehydrogenase, FT mitochondrial. FT /FTId=PRO_0000056567. FT NP_BIND 272 277 NADP (By similarity). FT ACT_SITE 294 294 Proton acceptor (By similarity). FT ACT_SITE 328 328 Nucleophile (By similarity). FT SITE 193 193 Transition state stabilizer (By FT similarity). FT MOD_RES 67 67 Phosphotyrosine (By similarity). FT VAR_SEQ 107 134 Missing (in isoform Short). FT /FTId=VSP_001284. SQ SEQUENCE 523 AA; 56131 MW; 4CA521139C9FA98F CRC64; MATCFLLRNF CAARPALRPP GRLLREPAGA QRRSYVGGPA DLHADLLRGD SFVGGRWLPT PATFPVYDPA SGAKLGTVAD CGVPEARAAV RAAYDAFSSW KEISVKERSS LLRKWYDLMI QNKDELAKII TAESGKPLKE AQGEILYSAF FLEWFSEEAR RVYGDIIYTS AKDKRGLVLK QPVGVASIIT PWNFPSAMIT RKVGAALAAG CTVVVKPAED TPYSALALAQ LANQAGIPPG VYNVIPCSRT KAKEVGEVLC TDPLVSKISF TGSTATGKIL LHHAANSVKR VSMELGGLAP FIVFDSANVD QAVAGAMASK FRNAGQTCVC SNRFLVQRGI HDSFVTKFAE AMKKSLRVGN GFEEGTTQGP LINEKAVEKV EKHVNDAVAK GATVVTGGKR HQSGGNFFEP TLLSNVTRDM LCITEETFGP VAPVIKFDKE EEAVAIANAA DVGLAGYFYS QDPAQIWRVA EQLEVGMVGV NEGLISSVEC PFGGVKQSGL GREGSKYGID EYLEVKYVCY GGL //