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Protein

Acylphosphatase-2

Gene

Acyp2

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

Functioni

Catalytic activityi

An acylphosphate + H2O = a carboxylate + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei31 – 311PROSITE-ProRule annotation
Active sitei49 – 491PROSITE-ProRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Acylphosphatase-2 (EC:3.6.1.7)
Alternative name(s):
Acylphosphatase, muscle type isozyme
Acylphosphate phosphohydrolase 2
Gene namesi
Name:Acyp2
Synonyms:Acyp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1922822. Acyp2.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 106106Acylphosphatase-2PRO_0000158543Add
BLAST

Proteomic databases

PaxDbiP56375.
PRIDEiP56375.

PTM databases

iPTMnetiP56375.

Expressioni

Gene expression databases

BgeeiP56375.
CleanExiMM_ACYP2.
GenevisibleiP56375. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074195.

Structurei

3D structure databases

ProteinModelPortaliP56375.
SMRiP56375. Positions 14-106.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 10691Acylphosphatase-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the acylphosphatase family.Curated
Contains 1 acylphosphatase-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3360. Eukaryota.
ENOG41126ER. LUCA.
GeneTreeiENSGT00390000011103.
HOGENOMiHOG000292688.
HOVERGENiHBG050454.
InParanoidiP56375.
KOiK01512.
OMAiQIFCCQF.
OrthoDBiEOG7ZGX55.
PhylomeDBiP56375.
TreeFamiTF300288.

Family and domain databases

InterProiIPR020456. Acylphosphatase.
IPR001792. Acylphosphatase-like_dom.
IPR017968. Acylphosphatase_CS.
[Graphical view]
PfamiPF00708. Acylphosphatase. 1 hit.
[Graphical view]
PRINTSiPR00112. ACYLPHPHTASE.
SUPFAMiSSF54975. SSF54975. 1 hit.
PROSITEiPS00150. ACYLPHOSPHATASE_1. 1 hit.
PS00151. ACYLPHOSPHATASE_2. 1 hit.
PS51160. ACYLPHOSPHATASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P56375-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLGRRLAAM TELLKSVDYE VFGTVQGVCF RMYTEGEAKK RGLVGWVKNT
60 70 80 90 100
SKGTVTGQVQ GPEEKVDAMK SWLSKVGSPS SRIDRADFSN EKTISKLEYS

DFSIRY
Length:106
Mass (Da):11,878
Last modified:October 3, 2012 - v2
Checksum:i54866EE08A445B16
GO

Sequence cautioni

The sequence AAH27642.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 41G → W in AAH27642 (PubMed:15489334).Curated
Sequence conflicti22 – 221F → L in BAC32649 (PubMed:16141072).Curated
Sequence conflicti63 – 631E → K in BAC32649 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046238 mRNA. Translation: BAC32649.1.
AK009134 mRNA. Translation: BAB26095.2.
AL844147, AL732595 Genomic DNA. Translation: CAI24140.2.
AL732595, AL844147 Genomic DNA. Translation: CAI26079.2.
BC027642 mRNA. Translation: AAH27642.1. Different initiation.
CCDSiCCDS24507.1.
RefSeqiNP_083620.1. NM_029344.3.
UniGeneiMm.390319.

Genome annotation databases

EnsembliENSMUST00000074613; ENSMUSP00000074195; ENSMUSG00000060923.
GeneIDi75572.
KEGGimmu:75572.
UCSCiuc007ihw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046238 mRNA. Translation: BAC32649.1.
AK009134 mRNA. Translation: BAB26095.2.
AL844147, AL732595 Genomic DNA. Translation: CAI24140.2.
AL732595, AL844147 Genomic DNA. Translation: CAI26079.2.
BC027642 mRNA. Translation: AAH27642.1. Different initiation.
CCDSiCCDS24507.1.
RefSeqiNP_083620.1. NM_029344.3.
UniGeneiMm.390319.

3D structure databases

ProteinModelPortaliP56375.
SMRiP56375. Positions 14-106.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074195.

PTM databases

iPTMnetiP56375.

Proteomic databases

PaxDbiP56375.
PRIDEiP56375.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000074613; ENSMUSP00000074195; ENSMUSG00000060923.
GeneIDi75572.
KEGGimmu:75572.
UCSCiuc007ihw.1. mouse.

Organism-specific databases

CTDi98.
MGIiMGI:1922822. Acyp2.

Phylogenomic databases

eggNOGiKOG3360. Eukaryota.
ENOG41126ER. LUCA.
GeneTreeiENSGT00390000011103.
HOGENOMiHOG000292688.
HOVERGENiHBG050454.
InParanoidiP56375.
KOiK01512.
OMAiQIFCCQF.
OrthoDBiEOG7ZGX55.
PhylomeDBiP56375.
TreeFamiTF300288.

Miscellaneous databases

PROiP56375.
SOURCEiSearch...

Gene expression databases

BgeeiP56375.
CleanExiMM_ACYP2.
GenevisibleiP56375. MM.

Family and domain databases

InterProiIPR020456. Acylphosphatase.
IPR001792. Acylphosphatase-like_dom.
IPR017968. Acylphosphatase_CS.
[Graphical view]
PfamiPF00708. Acylphosphatase. 1 hit.
[Graphical view]
PRINTSiPR00112. ACYLPHPHTASE.
SUPFAMiSSF54975. SSF54975. 1 hit.
PROSITEiPS00150. ACYLPHOSPHATASE_1. 1 hit.
PS00151. ACYLPHOSPHATASE_2. 1 hit.
PS51160. ACYLPHOSPHATASE_3. 1 hit.
[Graphical view]
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].
    Strain: C57BL/6J.
    Tissue: Corpora quadrigemina and Tongue.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiACYP2_MOUSE
AccessioniPrimary (citable) accession number: P56375
Secondary accession number(s): Q5SPV7, Q8BQX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: October 3, 2012
Last modified: June 8, 2016
This is version 116 of the entry and version 2 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.