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P08680

- HEM0_MOUSE

UniProt

P08680 - HEM0_MOUSE

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Protein

5-aminolevulinate synthase, erythroid-specific, mitochondrial

Gene

Alas2

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

Functioni

Catalytic activityi

Succinyl-CoA + glycine = 5-aminolevulinate + CoA + CO2.

Cofactori

Pyridoxal phosphate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei163 – 1631SubstrateBy similarity
Binding sitei280 – 2801SubstrateBy similarity
Binding sitei299 – 2991SubstrateBy similarity
Binding sitei332 – 3321Pyridoxal phosphateBy similarity
Binding sitei360 – 3601Pyridoxal phosphateBy similarity
Binding sitei388 – 3881Pyridoxal phosphateBy similarity
Active sitei391 – 3911By similarity
Binding sitei420 – 4201Pyridoxal phosphateBy similarity
Binding sitei421 – 4211Pyridoxal phosphateBy similarity
Binding sitei508 – 5081SubstrateBy similarity

GO - Molecular functioni

  1. 5-aminolevulinate synthase activity Source: UniProtKB
  2. pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  1. cellular iron ion homeostasis Source: MGI
  2. erythrocyte differentiation Source: UniProtKB
  3. heme biosynthetic process Source: UniProtKB
  4. hemoglobin biosynthetic process Source: UniProtKB
  5. protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway
  6. response to hypoxia Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Heme biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_203298. Heme biosynthesis.
UniPathwayiUPA00251; UER00375.

Names & Taxonomyi

Protein namesi
Recommended name:
5-aminolevulinate synthase, erythroid-specific, mitochondrial (EC:2.3.1.37)
Short name:
ALAS-E
Alternative name(s):
5-aminolevulinic acid synthase 2
Delta-ALA synthase 2
Delta-aminolevulinate synthase 2
Gene namesi
Name:Alas2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome X

Organism-specific databases

MGIiMGI:87990. Alas2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: UniProtKB
  2. mitochondrial matrix Source: InterPro
  3. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi391 – 3911K → A or H: Abolishes enzyme activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 4949Mitochondrion1 PublicationAdd
BLAST
Chaini50 – 5875385-aminolevulinate synthase, erythroid-specific, mitochondrialPRO_0000001224Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei391 – 3911N6-(pyridoxal phosphate)lysine

Proteomic databases

PaxDbiP08680.
PRIDEiP08680.

PTM databases

PhosphoSiteiP08680.

Expressioni

Tissue specificityi

Erythroid specific.

Gene expression databases

BgeeiP08680.
CleanExiMM_ALAS2.
ExpressionAtlasiP08680. baseline and differential.
GenevestigatoriP08680.

Interactioni

Subunit structurei

Interacts with SUCLA2 (By similarity). Homodimer.By similarity

Protein-protein interaction databases

BioGridi198059. 1 interaction.

Structurei

Secondary structure

1
587
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni5 – 84
Beta strandi14 – 163
Turni23 – 275
Helixi28 – 325

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1H7DNMR-A1-49[»]
1H7JNMR-A1-26[»]
ProteinModelPortaliP08680.
SMRiP08680. Positions 1-49, 151-540.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08680.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0156.
GeneTreeiENSGT00530000063111.
HOGENOMiHOG000221020.
HOVERGENiHBG005954.
InParanoidiP08680.
KOiK00643.
OMAiHYLQSIN.
OrthoDBiEOG7TQV0F.
PhylomeDBiP08680.
TreeFamiTF300724.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR015118. 5aminolev_synth_preseq.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
PF09029. Preseq_ALAS. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01821. 5aminolev_synth. 1 hit.
PROSITEiPS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P08680-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVAAAMLLRS CPVLSQGPTG LLGKVAKTYQ FLFSIGRCPI LATQGPTCSQ
60 70 80 90 100
IHLKATKAGG DSPSWAKSHC PFMLSELQDR KSKIVQRAAP EVQEDVKTFK
110 120 130 140 150
TDLLSTMDST TRSHSFPSFQ EPEQTEGAVP HLIQNNMTGS QAFGYDQFFR
160 170 180 190 200
DKIMEKKQDH TYRVFKTVNR WANAYPFAQH FSEASMASKD VSVWCSNDYL
210 220 230 240 250
GISRHPRVLQ AIEETLKNHG AGAGGTRNIS GTSKFHVELE QELAELHQKD
260 270 280 290 300
SALLFSSCFV ANDSTLFTLA KLLPGCEIYS DAGNHASMIQ GIRNSGAAKF
310 320 330 340 350
VFRHNDPGHL KKLLEKSDPK TPKIVAFETV HSMDGAICPL EELCDVAHQY
360 370 380 390 400
GALTFVDEVH AVGLYGARGA GIGERDGIMH KLDIISGTLG KAFGCVGGYI
410 420 430 440 450
ASTRDLVDMV RSYAAGFIFT TSLPPMVLSG ALESVRLLKG EEGQALRRAH
460 470 480 490 500
QRNVKHMRQL LMDRGFPVIP CPSHIIPIRV GNAALNSKIC DLLLSKHSIY
510 520 530 540 550
VQAINYPTVP RGEELLRLAP SPHHSPQMME NFVEKLLLAW TEVGLPLQDV
560 570 580
SVAACNFCHR PVHFELMSEW ERSYFGNMGP QYVTTYA
Length:587
Mass (Da):64,753
Last modified:January 23, 2002 - v3
Checksum:iA878D79FAD5B9856
GO

Sequence cautioni

The sequence AAA37207.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti61 – 7515Missing in AAA37207. (PubMed:3557128)CuratedAdd
BLAST
Sequence conflicti66 – 661A → R in BAB22254. (PubMed:16141072)Curated
Sequence conflicti171 – 1711W → R in AAA91866. 1 PublicationCurated
Sequence conflicti338 – 3381C → V in AAA91866. 1 PublicationCurated
Sequence conflicti368 – 3725RGAGI → GVQVS in AAA91866. 1 PublicationCurated
Sequence conflicti427 – 4271V → M in AAA37207. (PubMed:3557128)Curated
Sequence conflicti479 – 4791R → W in AAA91866. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15268 mRNA. Translation: AAA37207.1. Different initiation.
M63244 mRNA. Translation: AAA91866.1.
AK002642 mRNA. Translation: BAB22254.1.
AK077610 mRNA. Translation: BAC36898.1.
CCDSiCCDS41173.1.
PIRiA29040. SYMSAL.
RefSeqiNP_001095916.1. NM_001102446.1.
NP_033783.1. NM_009653.3.
UniGeneiMm.302724.

Genome annotation databases

EnsembliENSMUST00000066337; ENSMUSP00000066040; ENSMUSG00000025270.
GeneIDi11656.
KEGGimmu:11656.
UCSCiuc009uoj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15268 mRNA. Translation: AAA37207.1 . Different initiation.
M63244 mRNA. Translation: AAA91866.1 .
AK002642 mRNA. Translation: BAB22254.1 .
AK077610 mRNA. Translation: BAC36898.1 .
CCDSi CCDS41173.1.
PIRi A29040. SYMSAL.
RefSeqi NP_001095916.1. NM_001102446.1.
NP_033783.1. NM_009653.3.
UniGenei Mm.302724.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1H7D NMR - A 1-49 [» ]
1H7J NMR - A 1-26 [» ]
ProteinModelPortali P08680.
SMRi P08680. Positions 1-49, 151-540.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198059. 1 interaction.

PTM databases

PhosphoSitei P08680.

Proteomic databases

PaxDbi P08680.
PRIDEi P08680.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000066337 ; ENSMUSP00000066040 ; ENSMUSG00000025270 .
GeneIDi 11656.
KEGGi mmu:11656.
UCSCi uc009uoj.1. mouse.

Organism-specific databases

CTDi 212.
MGIi MGI:87990. Alas2.

Phylogenomic databases

eggNOGi COG0156.
GeneTreei ENSGT00530000063111.
HOGENOMi HOG000221020.
HOVERGENi HBG005954.
InParanoidi P08680.
KOi K00643.
OMAi HYLQSIN.
OrthoDBi EOG7TQV0F.
PhylomeDBi P08680.
TreeFami TF300724.

Enzyme and pathway databases

UniPathwayi UPA00251 ; UER00375 .
Reactomei REACT_203298. Heme biosynthesis.

Miscellaneous databases

EvolutionaryTracei P08680.
NextBioi 279269.
PROi P08680.
SOURCEi Search...

Gene expression databases

Bgeei P08680.
CleanExi MM_ALAS2.
ExpressionAtlasi P08680. baseline and differential.
Genevestigatori P08680.

Family and domain databases

Gene3Di 3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProi IPR010961. 4pyrrol_synth_NH2levulA_synth.
IPR015118. 5aminolev_synth_preseq.
IPR001917. Aminotrans_II_pyridoxalP_BS.
IPR004839. Aminotransferase_I/II.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view ]
Pfami PF00155. Aminotran_1_2. 1 hit.
PF09029. Preseq_ALAS. 1 hit.
[Graphical view ]
SUPFAMi SSF53383. SSF53383. 1 hit.
TIGRFAMsi TIGR01821. 5aminolev_synth. 1 hit.
PROSITEi PS00599. AA_TRANSFER_CLASS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of mouse 5-aminolevulinic acid synthase cDNA and expression of its gene in hepatic and erythroid tissues."
    Schoenhaut D.S., Curtis P.J.
    Gene 48:55-63(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Two genes encode Ala synthase in DBA/2 mouse: housekeeping and erythroid-specific."
    Young E.G., Dierks P.M.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: DBA/2.
    Tissue: Erythroleukemia.
  3. "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: Kidney.
  4. "Heme biosynthesis in mammalian systems: evidence of a Schiff base linkage between the pyridoxal 5'-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase."
    Ferreira G.C., Neame P.J., Dailey H.A.
    Protein Sci. 2:1959-1965(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PYRIDOXAL PHOSPHATE AT LYS-391.
  5. "The solution structure and heme binding of the presequence of murine 5-aminolevulinate synthase."
    Goodfellow B.J., Dias J.S., Ferreira G.C., Henklein P., Wray V., Macedo A.L.
    FEBS Lett. 505:325-331(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-49, TRANSIT PEPTIDE CLEAVAGE SITE.

Entry informationi

Entry nameiHEM0_MOUSE
AccessioniPrimary (citable) accession number: P08680
Secondary accession number(s): Q64452, Q9DCN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2002
Last modified: October 29, 2014
This is version 144 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

There are two delta-ALA synthases in vertebrates: an erythroid- specific form and one (housekeeping) which is expressed in all tissues.

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