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Protein

Adenosine deaminase-like protein

Gene

Adal

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Putative nucleoside deaminase. May catalyze the hydrolytic deamination of adenosine or some similar substrate and play a role in purine metabolism (By similarity).By similarity

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi23 – 231Zinc; catalyticBy similarity
Metal bindingi25 – 251Zinc; catalyticBy similarity
Binding sitei25 – 251SubstrateBy similarity
Binding sitei180 – 1801Substrate; via amide nitrogen and carbonyl oxygenBy similarity
Metal bindingi207 – 2071Zinc; catalyticBy similarity
Active sitei210 – 2101Proton donorBy similarity
Sitei231 – 2311Important for catalytic activityBy similarity
Metal bindingi292 – 2921Zinc; catalyticBy similarity
Binding sitei293 – 2931SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-2161541. Abacavir metabolism.
R-MMU-74217. Purine salvage.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosine deaminase-like protein (EC:3.5.4.-)
Gene namesi
Name:Adal
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1923144. Adal.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Adenosine deaminase-like proteinPRO_0000285091Add
BLAST

Proteomic databases

MaxQBiQ80SY6.
PaxDbiQ80SY6.
PRIDEiQ80SY6.

Expressioni

Gene expression databases

BgeeiQ80SY6.
CleanExiMM_ADAL.
ExpressionAtlasiQ80SY6. baseline and differential.
GenevisibleiQ80SY6. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000067133.

Structurei

3D structure databases

ProteinModelPortaliQ80SY6.
SMRiQ80SY6. Positions 18-315.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1097. Eukaryota.
COG1816. LUCA.
GeneTreeiENSGT00730000111081.
HOGENOMiHOG000205847.
HOVERGENiHBG055638.
InParanoidiQ80SY6.
OMAiIEHSMTA.
OrthoDBiEOG7H4DV1.
PhylomeDBiQ80SY6.
TreeFamiTF314270.

Family and domain databases

InterProiIPR001365. A/AMP_deaminase_dom.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q80SY6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MEAGQQWPGK TDFYLQLPKV ELHAHLNGSI SSSTMKKLIA KKPHLNVHGH
60 70 80 90 100
MTMIDKGKKR TLQECFQMFQ VIHQLTTSAE DILMVTKDVI KEFADDGVKY
110 120 130 140 150
LELRSTPREE NATGMTRKTY VESVLEGIKQ CKQENLDIDV RYLMAIDRRG
160 170 180 190 200
GPTIARETVE LAKEFFLSTE NTVLGLDLSG DPTIGQANDF LEPLLEAKKA
210 220 230 240 250
GLKLALHLAE IPNREKENQM LLSLLPDRIG HGTFLSASEA GALDQVDFVR
260 270 280 290 300
QHQIPLELCL TSNIKSQTVP SYDQHHFGFW YSIAHPSVIC TDDKGVFATY
310 320 330 340 350
LSQEYQLAAE TFNLTPFQVW DLSYESINYI FACDNTRSEL RKRWTHLKQK
360
VLNCNEVNYF
Length:360
Mass (Da):41,001
Last modified:June 1, 2003 - v1
Checksum:i525AEBD0EF7D217D
GO
Isoform 2 (identifier: Q80SY6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: Missing.

Show »
Length:293
Mass (Da):33,375
Checksum:i8C321E1E770FEA9D
GO
Isoform 3 (identifier: Q80SY6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     86-114: TKDVIKEFADDGVKYLELRSTPREENATG → RHRGRLKWRDFPQQCTANLAHVLWLSSTL
     115-360: Missing.

Show »
Length:114
Mass (Da):13,175
Checksum:iADF1223487A426F4
GO
Isoform 4 (identifier: Q80SY6-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-143: Missing.

Show »
Length:217
Mass (Da):24,597
Checksum:iDDB3891B89539BEE
GO

Sequence cautioni

The sequence CAM18206.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Isoform 3 (identifier: Q80SY6-3)
Sequence conflicti39 – 391I → T in BAC31744 (PubMed:16141072).Curated
Sequence conflicti103 – 1031N → H in BAC31744 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 143143Missing in isoform 4. CuratedVSP_024825Add
BLAST
Alternative sequencei1 – 6767Missing in isoform 2. 1 PublicationVSP_024822Add
BLAST
Alternative sequencei86 – 11429TKDVI…ENATG → RHRGRLKWRDFPQQCTANLA HVLWLSSTL in isoform 3. 1 PublicationVSP_024823Add
BLAST
Alternative sequencei115 – 360246Missing in isoform 3. 1 PublicationVSP_024824Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016299 mRNA. Translation: BAB30184.1.
AK044025 mRNA. Translation: BAC31744.1.
AK048809 mRNA. Translation: BAC33464.1.
AK049697 mRNA. Translation: BAC33880.1.
AL845479 Genomic DNA. Translation: CAM18204.1.
AL845479 Genomic DNA. Translation: CAM18205.1.
AL845479 Genomic DNA. Translation: CAM18206.1. Sequence problems.
AL845479 Genomic DNA. Translation: CAM18207.1.
BC050879 mRNA. Translation: AAH50879.1.
BC052048 mRNA. Translation: AAH52048.1.
CCDSiCCDS16633.1. [Q80SY6-1]
CCDS71121.1. [Q80SY6-2]
RefSeqiNP_001277740.1. NM_001290811.1. [Q80SY6-2]
NP_001277741.1. NM_001290812.1.
NP_083751.1. NM_029475.2. [Q80SY6-1]
XP_006500414.1. XM_006500351.2. [Q80SY6-1]
XP_006500415.1. XM_006500352.2. [Q80SY6-1]
XP_006500416.1. XM_006500353.2. [Q80SY6-1]
XP_006500421.1. XM_006500358.2. [Q80SY6-4]
XP_006500422.1. XM_006500359.2. [Q80SY6-4]
XP_006500423.1. XM_006500360.2. [Q80SY6-4]
XP_011238138.1. XM_011239836.1. [Q80SY6-2]
UniGeneiMm.384805.

Genome annotation databases

EnsembliENSMUST00000028702; ENSMUSP00000028702; ENSMUSG00000027259. [Q80SY6-2]
ENSMUST00000066155; ENSMUSP00000067133; ENSMUSG00000027259. [Q80SY6-1]
ENSMUST00000110662; ENSMUSP00000106290; ENSMUSG00000027259. [Q80SY6-4]
ENSMUST00000119031; ENSMUSP00000113052; ENSMUSG00000027259. [Q80SY6-1]
GeneIDi75894.
KEGGimmu:75894.
UCSCiuc008lxo.1. mouse. [Q80SY6-3]
uc008lxp.2. mouse. [Q80SY6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK016299 mRNA. Translation: BAB30184.1.
AK044025 mRNA. Translation: BAC31744.1.
AK048809 mRNA. Translation: BAC33464.1.
AK049697 mRNA. Translation: BAC33880.1.
AL845479 Genomic DNA. Translation: CAM18204.1.
AL845479 Genomic DNA. Translation: CAM18205.1.
AL845479 Genomic DNA. Translation: CAM18206.1. Sequence problems.
AL845479 Genomic DNA. Translation: CAM18207.1.
BC050879 mRNA. Translation: AAH50879.1.
BC052048 mRNA. Translation: AAH52048.1.
CCDSiCCDS16633.1. [Q80SY6-1]
CCDS71121.1. [Q80SY6-2]
RefSeqiNP_001277740.1. NM_001290811.1. [Q80SY6-2]
NP_001277741.1. NM_001290812.1.
NP_083751.1. NM_029475.2. [Q80SY6-1]
XP_006500414.1. XM_006500351.2. [Q80SY6-1]
XP_006500415.1. XM_006500352.2. [Q80SY6-1]
XP_006500416.1. XM_006500353.2. [Q80SY6-1]
XP_006500421.1. XM_006500358.2. [Q80SY6-4]
XP_006500422.1. XM_006500359.2. [Q80SY6-4]
XP_006500423.1. XM_006500360.2. [Q80SY6-4]
XP_011238138.1. XM_011239836.1. [Q80SY6-2]
UniGeneiMm.384805.

3D structure databases

ProteinModelPortaliQ80SY6.
SMRiQ80SY6. Positions 18-315.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000067133.

Proteomic databases

MaxQBiQ80SY6.
PaxDbiQ80SY6.
PRIDEiQ80SY6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028702; ENSMUSP00000028702; ENSMUSG00000027259. [Q80SY6-2]
ENSMUST00000066155; ENSMUSP00000067133; ENSMUSG00000027259. [Q80SY6-1]
ENSMUST00000110662; ENSMUSP00000106290; ENSMUSG00000027259. [Q80SY6-4]
ENSMUST00000119031; ENSMUSP00000113052; ENSMUSG00000027259. [Q80SY6-1]
GeneIDi75894.
KEGGimmu:75894.
UCSCiuc008lxo.1. mouse. [Q80SY6-3]
uc008lxp.2. mouse. [Q80SY6-1]

Organism-specific databases

CTDi161823.
MGIiMGI:1923144. Adal.

Phylogenomic databases

eggNOGiKOG1097. Eukaryota.
COG1816. LUCA.
GeneTreeiENSGT00730000111081.
HOGENOMiHOG000205847.
HOVERGENiHBG055638.
InParanoidiQ80SY6.
OMAiIEHSMTA.
OrthoDBiEOG7H4DV1.
PhylomeDBiQ80SY6.
TreeFamiTF314270.

Enzyme and pathway databases

ReactomeiR-MMU-2161541. Abacavir metabolism.
R-MMU-74217. Purine salvage.

Miscellaneous databases

NextBioi344213.
PROiQ80SY6.
SOURCEiSearch...

Gene expression databases

BgeeiQ80SY6.
CleanExiMM_ADAL.
ExpressionAtlasiQ80SY6. baseline and differential.
GenevisibleiQ80SY6. MM.

Family and domain databases

InterProiIPR001365. A/AMP_deaminase_dom.
IPR032466. Metal_Hydrolase.
[Graphical view]
PfamiPF00962. A_deaminase. 1 hit.
[Graphical view]
SUPFAMiSSF51556. SSF51556. 1 hit.
ProtoNetiSearch...

Publicationsi

  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] (ISOFORMS 2 AND 3).
    Strain: C57BL/6J.
    Tissue: Brain cortex, Cerebellum, Spinal cord and Testis.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 4).
    Strain: C57BL/6J.
  3. "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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Brain.

Entry informationi

Entry nameiADAL_MOUSE
AccessioniPrimary (citable) accession number: Q80SY6
Secondary accession number(s): A2ARU3
, A2ARU4, Q8BLN3, Q8BX67, Q9D4Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: June 1, 2003
Last modified: May 11, 2016
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.