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Protein

Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

Gene

Aldh4a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.

Pathway:iL-proline degradation into L-glutamate

This protein is involved in step 2 of the subpathway that synthesizes L-glutamate from L-proline.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Probable proline dehydrogenase 2 (Prodh2), Proline dehydrogenase 1, mitochondrial (Prodh)
  2. Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (Aldh4a1)
This subpathway is part of the pathway L-proline degradation into L-glutamate, which is itself part of Amino-acid degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from L-proline, the pathway L-proline degradation into L-glutamate and in Amino-acid degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei207 – 2071NAD
Sitei210 – 2101Transition state stabilizerBy similarity
Binding sitei232 – 2321NAD
Active sitei313 – 3131Proton acceptorPROSITE-ProRule annotation1 Publication
Active sitei347 – 3471NucleophilePROSITE-ProRule annotation1 Publication
Binding sitei446 – 4461NAD
Binding sitei512 – 5121Substrate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi285 – 2895NAD

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Proline metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

ReactomeiREACT_273967. Proline catabolism.
UniPathwayiUPA00261; UER00374.

Names & Taxonomyi

Protein namesi
Recommended name:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (EC:1.2.1.88)
Short name:
P5C dehydrogenase
Alternative name(s):
Aldehyde dehydrogenase family 4 member A1
L-glutamate gamma-semialdehyde dehydrogenase
Gene namesi
Name:Aldh4a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2443883. Aldh4a1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: UniProtKB-SubCell
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323MitochondrionBy similarityAdd
BLAST
Chaini24 – 562539Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrialPRO_0000007174Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei30 – 301N6-succinyllysine1 Publication
Modified residuei43 – 431PhosphoserineBy similarity
Modified residuei51 – 511N6-acetyllysine1 Publication
Modified residuei92 – 921N6-acetyllysine; alternate1 Publication
Modified residuei92 – 921N6-succinyllysine; alternate1 Publication
Modified residuei98 – 981N6-acetyllysine; alternate1 Publication
Modified residuei98 – 981N6-succinyllysine; alternate1 Publication
Modified residuei113 – 1131N6-acetyllysine; alternate1 Publication
Modified residuei113 – 1131N6-succinyllysine; alternate1 Publication
Modified residuei129 – 1291N6-acetyllysine; alternate1 Publication
Modified residuei129 – 1291N6-succinyllysine; alternate1 Publication
Modified residuei174 – 1741N6-acetyllysine; alternate1 Publication
Modified residuei174 – 1741N6-succinyllysine; alternate1 Publication
Modified residuei317 – 3171N6-acetyllysine1 Publication
Modified residuei346 – 3461N6-succinyllysine1 Publication
Modified residuei357 – 3571N6-acetyllysine; alternate1 Publication
Modified residuei357 – 3571N6-succinyllysine; alternate1 Publication
Modified residuei364 – 3641N6-acetyllysine1 Publication
Modified residuei375 – 3751N6-acetyllysine1 Publication
Modified residuei394 – 3941N6-succinyllysine1 Publication
Modified residuei461 – 4611N6-acetyllysine1 Publication
Modified residuei508 – 5081N6-acetyllysine; alternate1 Publication
Modified residuei508 – 5081N6-succinyllysine; alternate1 Publication
Modified residuei530 – 5301N6-acetyllysine1 Publication
Modified residuei551 – 5511N6-acetyllysine1 Publication

Post-translational modificationi

Acetylation of Lys-98, Lys-113 and Lys-401 is observed in liver mitochondria from fasted mice but not from fed mice.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8CHT0.
PaxDbiQ8CHT0.
PRIDEiQ8CHT0.

PTM databases

PhosphoSiteiQ8CHT0.

Expressioni

Gene expression databases

BgeeiQ8CHT0.
CleanExiMM_ALDH4A1.
ExpressionAtlasiQ8CHT0. baseline and differential.
GenevisibleiQ8CHT0. MM.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

IntActiQ8CHT0. 3 interactions.
MINTiMINT-1859863.
STRINGi10090.ENSMUSP00000043821.

Structurei

Secondary structure

1
562
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi44 – 5411Combined sources
Turni55 – 584Combined sources
Beta strandi65 – 673Combined sources
Beta strandi70 – 723Combined sources
Beta strandi77 – 826Combined sources
Beta strandi85 – 9410Combined sources
Helixi98 – 11720Combined sources
Helixi120 – 13516Combined sources
Turni136 – 1383Combined sources
Helixi139 – 15012Combined sources
Helixi154 – 1607Combined sources
Helixi163 – 17917Combined sources
Beta strandi190 – 1956Combined sources
Beta strandi200 – 2067Combined sources
Helixi212 – 22413Combined sources
Beta strandi229 – 2324Combined sources
Helixi235 – 2373Combined sources
Helixi238 – 25013Combined sources
Beta strandi257 – 2604Combined sources
Helixi265 – 2728Combined sources
Beta strandi278 – 2858Combined sources
Helixi287 – 29913Combined sources
Turni300 – 3034Combined sources
Beta strandi309 – 3135Combined sources
Beta strandi318 – 3225Combined sources
Helixi328 – 34013Combined sources
Helixi341 – 3444Combined sources
Beta strandi350 – 3567Combined sources
Helixi357 – 3593Combined sources
Helixi360 – 37213Combined sources
Turni379 – 3813Combined sources
Helixi393 – 40816Combined sources
Beta strandi412 – 4165Combined sources
Beta strandi423 – 4253Combined sources
Beta strandi431 – 4366Combined sources
Helixi441 – 4433Combined sources
Beta strandi449 – 4579Combined sources
Helixi459 – 4613Combined sources
Helixi462 – 47110Combined sources
Beta strandi472 – 48211Combined sources
Helixi486 – 49510Combined sources
Turni496 – 4994Combined sources
Beta strandi501 – 5077Combined sources
Turni514 – 5163Combined sources
Helixi536 – 5405Combined sources
Beta strandi544 – 5496Combined sources
Helixi559 – 5613Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V9JX-ray1.30A/B21-562[»]
3V9KX-ray1.50A/B21-562[»]
3V9LX-ray1.50A/B21-562[»]
4E3XX-ray1.24A/B21-562[»]
4LGZX-ray1.68A/B21-562[»]
4LH0X-ray1.67A/B21-562[»]
4LH1X-ray1.67A/B21-562[»]
4LH2X-ray1.67A/B21-562[»]
4LH3X-ray1.81A/B21-562[»]
ProteinModelPortaliQ8CHT0.
SMRiQ8CHT0. Positions 21-562.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00560000077335.
HOGENOMiHOG000271511.
HOVERGENiHBG050484.
InParanoidiQ8CHT0.
KOiK00294.
OMAiGNMYLND.
OrthoDBiEOG7T1R9D.
TreeFamiTF300481.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005931. P5CDH/ALDH4A1.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01236. D1pyr5carbox1. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8CHT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPLPSLRRS LLSHAWRGAG LRWKHTSSLK VTNEPILAFS QGSPERDALQ
60 70 80 90 100
KALKDLKGQM EAIPCVVGDE EVWTSDIQYQ LSPFNHAHKV AKFCYADKAL
110 120 130 140 150
LNRAIDAALA ARKEWDLKPM ADRAQVFLKA ADMLSGPRRA EVLAKTMVGQ
160 170 180 190 200
GKTVIQAEID AAAELIDFFR FNAKFAVELE GEQPISVPPS TNHTVYRGLE
210 220 230 240 250
GFVAAISPFN FTAIGGNLAG APALMGNVVL WKPSDTAMLA SYAVYRILRE
260 270 280 290 300
AGLPPNIIQF VPADGPTFGD TVTSSEHLCG INFTGSVPTF KHLWRQVAQN
310 320 330 340 350
LDRFRTFPRL AGECGGKNFH FVHSSADVDS VVSGTLRSAF EYGGQKCSAC
360 370 380 390 400
SRLYVPKSLW PQIKGRLLEE HSRIKVGDPA EDFGTFFSAV IDAKAFARIK
410 420 430 440 450
KWLEHARSSP SLSILAGGQC NESVGYYVEP CIIESKDPQE PIMKEEIFGP
460 470 480 490 500
VLTVYVYPDD KYRETLQLVD STTSYGLTGA VFAQDKAIVQ EATRMLRNAA
510 520 530 540 550
GNFYINDKST GSVVGQQPFG GARASGTNDK PGGPHYILRW TSPQVIKETH
560
KPLGDWRYSY MQ
Length:562
Mass (Da):61,841
Last modified:July 27, 2011 - v3
Checksum:i4D8A0C9C68A99478
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181G → S in BAC32045 (PubMed:16141072).Curated
Sequence conflicti18 – 181G → S in AAH56226 (PubMed:15489334).Curated
Sequence conflicti18 – 181G → S in AAH39281 (PubMed:15489334).Curated
Sequence conflicti18 – 181G → S in AAH24133 (PubMed:15489334).Curated
Sequence conflicti32 – 321T → A in BAC32045 (PubMed:16141072).Curated
Sequence conflicti32 – 321T → A in AAH56226 (PubMed:15489334).Curated
Sequence conflicti32 – 321T → A in AAH39281 (PubMed:15489334).Curated
Sequence conflicti32 – 321T → A in AAH24133 (PubMed:15489334).Curated
Sequence conflicti47 – 471D → G in BAC32045 (PubMed:16141072).Curated
Sequence conflicti60 – 601M → T in BAC32045 (PubMed:16141072).Curated
Sequence conflicti60 – 601M → T in AAH56226 (PubMed:15489334).Curated
Sequence conflicti60 – 601M → T in AAH39281 (PubMed:15489334).Curated
Sequence conflicti60 – 601M → T in AAH24133 (PubMed:15489334).Curated
Sequence conflicti467 – 4671Q → K in BAC32045 (PubMed:16141072).Curated
Sequence conflicti467 – 4671Q → K in AAH56226 (PubMed:15489334).Curated
Sequence conflicti467 – 4671Q → K in AAH39281 (PubMed:15489334).Curated
Sequence conflicti467 – 4671Q → K in AAH24133 (PubMed:15489334).Curated
Sequence conflicti467 – 4671Q → K in AAH26589 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044712 mRNA. Translation: BAC32045.1.
AL831790 Genomic DNA. Translation: CAM21310.1.
CH466615 Genomic DNA. Translation: EDL13315.1.
BC024133 mRNA. Translation: AAH24133.1.
BC026589 mRNA. Translation: AAH26589.1.
BC039281 mRNA. Translation: AAH39281.2.
BC056226 mRNA. Translation: AAH56226.1.
CCDSiCCDS18848.1.
RefSeqiNP_780647.3. NM_175438.4.
UniGeneiMm.273571.

Genome annotation databases

EnsembliENSMUST00000039818; ENSMUSP00000043821; ENSMUSG00000028737.
GeneIDi212647.
KEGGimmu:212647.
UCSCiuc012dnu.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK044712 mRNA. Translation: BAC32045.1.
AL831790 Genomic DNA. Translation: CAM21310.1.
CH466615 Genomic DNA. Translation: EDL13315.1.
BC024133 mRNA. Translation: AAH24133.1.
BC026589 mRNA. Translation: AAH26589.1.
BC039281 mRNA. Translation: AAH39281.2.
BC056226 mRNA. Translation: AAH56226.1.
CCDSiCCDS18848.1.
RefSeqiNP_780647.3. NM_175438.4.
UniGeneiMm.273571.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3V9JX-ray1.30A/B21-562[»]
3V9KX-ray1.50A/B21-562[»]
3V9LX-ray1.50A/B21-562[»]
4E3XX-ray1.24A/B21-562[»]
4LGZX-ray1.68A/B21-562[»]
4LH0X-ray1.67A/B21-562[»]
4LH1X-ray1.67A/B21-562[»]
4LH2X-ray1.67A/B21-562[»]
4LH3X-ray1.81A/B21-562[»]
ProteinModelPortaliQ8CHT0.
SMRiQ8CHT0. Positions 21-562.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CHT0. 3 interactions.
MINTiMINT-1859863.
STRINGi10090.ENSMUSP00000043821.

PTM databases

PhosphoSiteiQ8CHT0.

Proteomic databases

MaxQBiQ8CHT0.
PaxDbiQ8CHT0.
PRIDEiQ8CHT0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000039818; ENSMUSP00000043821; ENSMUSG00000028737.
GeneIDi212647.
KEGGimmu:212647.
UCSCiuc012dnu.1. mouse.

Organism-specific databases

CTDi8659.
MGIiMGI:2443883. Aldh4a1.

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00560000077335.
HOGENOMiHOG000271511.
HOVERGENiHBG050484.
InParanoidiQ8CHT0.
KOiK00294.
OMAiGNMYLND.
OrthoDBiEOG7T1R9D.
TreeFamiTF300481.

Enzyme and pathway databases

UniPathwayiUPA00261; UER00374.
ReactomeiREACT_273967. Proline catabolism.

Miscellaneous databases

ChiTaRSiAldh4a1. mouse.
NextBioi373656.
PROiQ8CHT0.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CHT0.
CleanExiMM_ALDH4A1.
ExpressionAtlasiQ8CHT0. baseline and differential.
GenevisibleiQ8CHT0. MM.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR005931. P5CDH/ALDH4A1.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
TIGRFAMsiTIGR01236. D1pyr5carbox1. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Retina.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Kidney and Liver.
  5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-92; LYS-98; LYS-113; LYS-129; LYS-174; LYS-346; LYS-357; LYS-394 AND LYS-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-92; LYS-98; LYS-113; LYS-129; LYS-174; LYS-317; LYS-357; LYS-364; LYS-375; LYS-461; LYS-508; LYS-530 AND LYS-551, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "Proline: Mother Nature's cryoprotectant applied to protein crystallography."
    Pemberton T.A., Still B.R., Christensen E.M., Singh H., Srivastava D., Tanner J.J.
    Acta Crystallogr. D 68:1010-1018(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.24 ANGSTROMS) OF 21-562.
  8. "The three-dimensional structural basis of type II hyperprolinemia."
    Srivastava D., Singh R.K., Moxley M.A., Henzl M.T., Becker D.F., Tanner J.J.
    J. Mol. Biol. 420:176-189(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF 21-562 IN COMPLEXES WITH GLUTAMATE AND NAD, SUBUNIT, ACTIVE SITE.

Entry informationi

Entry nameiAL4A1_MOUSE
AccessioniPrimary (citable) accession number: Q8CHT0
Secondary accession number(s): B1AXW8
, Q7TND0, Q8BXM3, Q8R0N1, Q8R1S2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.