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Acylphosphatase-1 (EC 3.6.1.7) (Acylphosphatase, erythrocyte isozyme) (Acylphosphatase, organ-common type isozyme) (Acylphosphate phosphohydrolase 1)

 ACYP1_HUMAN             Reviewed;          99 AA.
P07311; A6NDV8; B2R590;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
05-DEC-2018, entry version 172.
RecName: Full=Acylphosphatase-1;
EC=3.6.1.7;
AltName: Full=Acylphosphatase, erythrocyte isozyme;
AltName: Full=Acylphosphatase, organ-common type isozyme;
AltName: Full=Acylphosphate phosphohydrolase 1;
Name=ACYP1; Synonyms=ACYPE;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
Raugei G.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12508121; DOI=10.1038/nature01348;
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
Quetier F., Waterston R., Hood L., Weissenbach J.;
"The DNA sequence and analysis of human chromosome 14.";
Nature 421:601-607(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Embryonic carcinoma, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-99, CLEAVAGE OF INITIATOR METHIONINE, AND
ACETYLATION AT ALA-2.
PubMed=3026468; DOI=10.1021/bi00372a044;
Liguri G., Camici G., Manao G., Cappugi G., Nassi P., Modesti A.,
Ramponi G.;
"A new acylphosphatase isoenzyme from human erythrocytes:
purification, characterization, and primary structure.";
Biochemistry 25:8089-8094(1986).
[7]
PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 10-86.
TISSUE=Placenta;
PubMed=7796909; DOI=10.1016/0014-5793(95)00553-L;
Fiaschi T., Raugei G., Marzocchini R., Chiarugi P., Cirri P.,
Ramponi G.;
"Cloning and expression of the cDNA coding for the erythrocyte
isoenzyme of human acylphosphatase.";
FEBS Lett. 367:145-148(1995).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
PubMed=16511269; DOI=10.1107/S174430910504145X;
Yeung R.C., Lam S.Y., Wong K.B.;
"Crystallization and preliminary crystallographic analysis of human
common-type acylphosphatase.";
Acta Crystallogr. F 62:80-82(2006).
[10]
STRUCTURE BY NMR OF 2-99.
PubMed=19196981; DOI=10.1073/pnas.0808220106;
Gribenko A.V., Patel M.M., Liu J., McCallum S.A., Wang C.,
Makhatadze G.I.;
"Rational stabilization of enzymes by computational redesign of
surface charge-charge interactions.";
Proc. Natl. Acad. Sci. U.S.A. 106:2601-2606(2009).
-!- FUNCTION: Its physiological role is not yet clear.
-!- CATALYTIC ACTIVITY:
Reaction=an acyl phosphate + H2O = a carboxylate + H(+) +
phosphate; Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:43474,
ChEBI:CHEBI:59918; EC=3.6.1.7;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P07311-1; Sequence=Displayed;
Name=2;
IsoId=P07311-2; Sequence=VSP_045688;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Organ-common type isozyme is found in many
different tissues.
-!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X84194; CAA58987.1; -; mRNA.
EMBL; AK312101; BAG35037.1; -; mRNA.
EMBL; AC007055; AAD31937.1; -; Genomic_DNA.
EMBL; AL049780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471061; EAW81216.1; -; Genomic_DNA.
EMBL; BC035568; AAH35568.1; -; mRNA.
EMBL; BG614847; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS9838.1; -. [P07311-1]
PIR; S66187; QPHUE.
RefSeq; NP_001098.1; NM_001107.4. [P07311-1]
RefSeq; NP_001289545.1; NM_001302616.1. [P07311-1]
UniGene; Hs.18573; -.
PDB; 2K7J; NMR; -; A=2-99.
PDB; 2K7K; NMR; -; A=2-99.
PDB; 2VH7; X-ray; 1.45 A; A=1-99.
PDB; 2W4C; X-ray; 1.52 A; A=1-99.
PDB; 2W4P; X-ray; 1.70 A; A=1-99.
PDB; 3TOQ; X-ray; 2.00 A; A=1-99.
PDBsum; 2K7J; -.
PDBsum; 2K7K; -.
PDBsum; 2VH7; -.
PDBsum; 2W4C; -.
PDBsum; 2W4P; -.
PDBsum; 3TOQ; -.
ProteinModelPortal; P07311; -.
SMR; P07311; -.
BioGrid; 106612; 1.
STRING; 9606.ENSP00000238618; -.
iPTMnet; P07311; -.
PhosphoSitePlus; P07311; -.
BioMuta; ACYP1; -.
EPD; P07311; -.
MaxQB; P07311; -.
PaxDb; P07311; -.
PeptideAtlas; P07311; -.
PRIDE; P07311; -.
ProteomicsDB; 51984; -.
TopDownProteomics; P07311-1; -. [P07311-1]
Ensembl; ENST00000238618; ENSP00000238618; ENSG00000119640. [P07311-1]
Ensembl; ENST00000357971; ENSP00000350655; ENSG00000119640. [P07311-2]
Ensembl; ENST00000555694; ENSP00000451581; ENSG00000119640. [P07311-1]
GeneID; 97; -.
KEGG; hsa:97; -.
UCSC; uc001xrf.4; human. [P07311-1]
CTD; 97; -.
EuPathDB; HostDB:ENSG00000119640.8; -.
GeneCards; ACYP1; -.
HGNC; HGNC:179; ACYP1.
HPA; HPA034944; -.
MIM; 600875; gene.
neXtProt; NX_P07311; -.
OpenTargets; ENSG00000119640; -.
PharmGKB; PA24499; -.
eggNOG; KOG3360; Eukaryota.
eggNOG; ENOG41126ER; LUCA.
GeneTree; ENSGT00390000011103; -.
HOGENOM; HOG000292688; -.
HOVERGEN; HBG050454; -.
InParanoid; P07311; -.
KO; K01512; -.
PhylomeDB; P07311; -.
TreeFam; TF300288; -.
SABIO-RK; P07311; -.
ChiTaRS; ACYP1; human.
EvolutionaryTrace; P07311; -.
GeneWiki; ACYP1; -.
GenomeRNAi; 97; -.
PRO; PR:P07311; -.
Proteomes; UP000005640; Chromosome 14.
Bgee; ENSG00000119640; Expressed in 218 organ(s), highest expression level in tendon.
CleanEx; HS_ACYP1; -.
ExpressionAtlas; P07311; baseline and differential.
Genevisible; P07311; HS.
GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
GO; GO:0006796; P:phosphate-containing compound metabolic process; TAS:ProtInc.
InterPro; IPR020456; Acylphosphatase.
InterPro; IPR001792; Acylphosphatase-like_dom.
InterPro; IPR036046; Acylphosphatase-like_dom_sf.
InterPro; IPR017968; Acylphosphatase_CS.
PANTHER; PTHR10029; PTHR10029; 1.
Pfam; PF00708; Acylphosphatase; 1.
PRINTS; PR00112; ACYLPHPHTASE.
SUPFAM; SSF54975; SSF54975; 1.
PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Hydrolase; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3026468}.
CHAIN 2 99 Acylphosphatase-1.
/FTId=PRO_0000158535.
DOMAIN 9 99 Acylphosphatase-like.
{ECO:0000255|PROSITE-ProRule:PRU00520}.
ACT_SITE 24 24 {ECO:0000255|PROSITE-ProRule:PRU00520}.
ACT_SITE 42 42 {ECO:0000255|PROSITE-ProRule:PRU00520}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000269|PubMed:3026468}.
VAR_SEQ 29 99 AEGKKLGLVGWVQNTDRGTVQGQLQGPISKVRHMQEWLETR
GSPKSHIDKANFNNEKVILKLDYSDFQIVK -> EMTVENR
IAETHSKSCVPVSFATSYAG (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045688.
STRAND 7 17 {ECO:0000244|PDB:2VH7}.
STRAND 19 21 {ECO:0000244|PDB:2VH7}.
HELIX 23 33 {ECO:0000244|PDB:2VH7}.
STRAND 37 42 {ECO:0000244|PDB:2VH7}.
STRAND 44 46 {ECO:0000244|PDB:2K7J}.
STRAND 48 55 {ECO:0000244|PDB:2VH7}.
HELIX 56 68 {ECO:0000244|PDB:2VH7}.
STRAND 72 74 {ECO:0000244|PDB:2K7J}.
STRAND 75 89 {ECO:0000244|PDB:2VH7}.
STRAND 93 97 {ECO:0000244|PDB:2VH7}.
SEQUENCE 99 AA; 11261 MW; F9F787E490BC8296 CRC64;
MAEGNTLISV DYEIFGKVQG VFFRKHTQAE GKKLGLVGWV QNTDRGTVQG QLQGPISKVR
HMQEWLETRG SPKSHIDKAN FNNEKVILKL DYSDFQIVK


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