ACYP1_MOUSE
ID ACYP1_MOUSE Reviewed; 99 AA.
AC P56376; Q0VG40; Q545K8; Q6P8S7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Acylphosphatase-1;
DE EC=3.6.1.7 {ECO:0000250|UniProtKB:P07311};
DE AltName: Full=Acylphosphatase, organ-common type isozyme;
DE AltName: Full=Acylphosphate phosphohydrolase 1;
GN Name=Acyp1; Synonyms=Acype;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000250|UniProtKB:P07311};
CC -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR EMBL; AK004176; BAB23208.1; -; mRNA.
DR EMBL; AK007244; BAB24911.1; -; mRNA.
DR EMBL; AK018832; BAB31454.1; -; mRNA.
DR EMBL; BC061088; AAH61088.2; -; mRNA.
DR EMBL; BC116781; AAI16782.1; -; mRNA.
DR EMBL; BC116783; AAI16784.1; -; mRNA.
DR CCDS; CCDS26055.1; -.
DR RefSeq; NP_079697.1; NM_025421.2.
DR AlphaFoldDB; P56376; -.
DR SMR; P56376; -.
DR STRING; 10090.ENSMUSP00000008966; -.
DR iPTMnet; P56376; -.
DR PhosphoSitePlus; P56376; -.
DR REPRODUCTION-2DPAGE; IPI00420440; -.
DR CPTAC; non-CPTAC-3630; -.
DR EPD; P56376; -.
DR jPOST; P56376; -.
DR MaxQB; P56376; -.
DR PaxDb; P56376; -.
DR PRIDE; P56376; -.
DR ProteomicsDB; 285754; -.
DR Antibodypedia; 25782; 200 antibodies from 31 providers.
DR DNASU; 66204; -.
DR Ensembl; ENSMUST00000008966; ENSMUSP00000008966; ENSMUSG00000008822.
DR Ensembl; ENSMUST00000117138; ENSMUSP00000113161; ENSMUSG00000008822.
DR GeneID; 66204; -.
DR KEGG; mmu:66204; -.
DR UCSC; uc007ogu.2; mouse.
DR CTD; 97; -.
DR MGI; MGI:1913454; Acyp1.
DR VEuPathDB; HostDB:ENSMUSG00000008822; -.
DR eggNOG; KOG3360; Eukaryota.
DR GeneTree; ENSGT00390000011103; -.
DR HOGENOM; CLU_141932_0_1_1; -.
DR InParanoid; P56376; -.
DR OrthoDB; 1502266at2759; -.
DR PhylomeDB; P56376; -.
DR TreeFam; TF300288; -.
DR BioGRID-ORCS; 66204; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Acyp1; mouse.
DR PRO; PR:P56376; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; P56376; protein.
DR Bgee; ENSMUSG00000008822; Expressed in seminiferous tubule of testis and 267 other tissues.
DR ExpressionAtlas; P56376; baseline and differential.
DR Genevisible; P56376; MM.
DR GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR PANTHER; PTHR10029; PTHR10029; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR PRINTS; PR00112; ACYLPHPHTASE.
DR SUPFAM; SSF54975; SSF54975; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07311"
FT CHAIN 2..99
FT /note="Acylphosphatase-1"
FT /id="PRO_0000158536"
FT DOMAIN 9..99
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT ACT_SITE 42
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00520"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P07311"
SQ SEQUENCE 99 AA; 11241 MW; 3291F35B26338081 CRC64;
MAEGDTLVSV DYEIFGKVQG VFFRKYTQAE GKKLGLVGWV QNTDRGTVQG QLQGPVSKVR
FMQQWLETRG SPKSHIDRAN FNNEKVIANL DYSDFQIVK
