ACYP1_HUMAN
ID ACYP1_HUMAN Reviewed; 99 AA.
AC P07311; A6NDV8; B2R590;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Acylphosphatase-1;
DE EC=3.6.1.7 {ECO:0000305|PubMed:3026468};
DE AltName: Full=Acylphosphatase, erythrocyte isozyme;
DE AltName: Full=Acylphosphatase, organ-common type isozyme;
DE AltName: Full=Acylphosphate phosphohydrolase 1;
GN Name=ACYP1; Synonyms=ACYPE;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RA Raugei G.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryonic carcinoma, and Mammary gland;
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 [6]
RP PROTEIN SEQUENCE OF 2-99, CATALYTIC ACTIVITY, CLEAVAGE OF INITIATOR
RP METHIONINE, AND ACETYLATION AT ALA-2.
RX PubMed=3026468; DOI=10.1021/bi00372a044;
RA Liguri G., Camici G., Manao G., Cappugi G., Nassi P., Modesti A.,
RA Ramponi G.;
RT "A new acylphosphatase isoenzyme from human erythrocytes: purification,
RT characterization, and primary structure.";
RL Biochemistry 25:8089-8094(1986).
RN [7]
RP PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 10-86.
RC TISSUE=Placenta;
RX PubMed=7796909; DOI=10.1016/0014-5793(95)00553-l;
RA Fiaschi T., Raugei G., Marzocchini R., Chiarugi P., Cirri P., Ramponi G.;
RT "Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of
RT human acylphosphatase.";
RL FEBS Lett. 367:145-148(1995).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
RX PubMed=16511269; DOI=10.1107/s174430910504145x;
RA Yeung R.C., Lam S.Y., Wong K.B.;
RT "Crystallization and preliminary crystallographic analysis of human common-
RT type acylphosphatase.";
RL Acta Crystallogr. F 62:80-82(2006).
RN [10]
RP STRUCTURE BY NMR OF 2-99.
RX PubMed=19196981; DOI=10.1073/pnas.0808220106;
RA Gribenko A.V., Patel M.M., Liu J., McCallum S.A., Wang C., Makhatadze G.I.;
RT "Rational stabilization of enzymes by computational redesign of surface
RT charge-charge interactions.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2601-2606(2009).
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:0000305|PubMed:3026468};
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P07311-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P07311-2; Sequence=VSP_045688;
CC -!- TISSUE SPECIFICITY: Organ-common type isozyme is found in many
CC different tissues.
CC -!- SIMILARITY: Belongs to the acylphosphatase family. {ECO:0000305}.
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DR EMBL; X84194; CAA58987.1; -; mRNA.
DR EMBL; AK312101; BAG35037.1; -; mRNA.
DR EMBL; AC007055; AAD31937.1; -; Genomic_DNA.
DR EMBL; AL049780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81216.1; -; Genomic_DNA.
DR EMBL; BC035568; AAH35568.1; -; mRNA.
DR EMBL; BG614847; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS9838.1; -. [P07311-1]
DR PIR; S66187; QPHUE.
DR RefSeq; NP_001098.1; NM_001107.4. [P07311-1]
DR RefSeq; NP_001289545.1; NM_001302616.1. [P07311-1]
DR PDB; 2K7J; NMR; -; A=2-99.
DR PDB; 2K7K; NMR; -; A=2-99.
DR PDB; 2VH7; X-ray; 1.45 A; A=1-99.
DR PDB; 2W4C; X-ray; 1.52 A; A=1-99.
DR PDB; 2W4P; X-ray; 1.70 A; A=1-99.
DR PDB; 3TOQ; X-ray; 2.00 A; A=1-99.
DR PDB; 6CBU; X-ray; 1.20 A; A=1-98.
DR PDBsum; 2K7J; -.
DR PDBsum; 2K7K; -.
DR PDBsum; 2VH7; -.
DR PDBsum; 2W4C; -.
DR PDBsum; 2W4P; -.
DR PDBsum; 3TOQ; -.
DR PDBsum; 6CBU; -.
DR AlphaFoldDB; P07311; -.
DR SMR; P07311; -.
DR BioGRID; 106612; 4.
DR IntAct; P07311; 1.
DR STRING; 9606.ENSP00000238618; -.
DR iPTMnet; P07311; -.
DR PhosphoSitePlus; P07311; -.
DR BioMuta; ACYP1; -.
DR EPD; P07311; -.
DR jPOST; P07311; -.
DR MassIVE; P07311; -.
DR MaxQB; P07311; -.
DR PaxDb; P07311; -.
DR PeptideAtlas; P07311; -.
DR PRIDE; P07311; -.
DR ProteomicsDB; 51984; -. [P07311-1]
DR ProteomicsDB; 934; -.
DR TopDownProteomics; P07311-1; -. [P07311-1]
DR Antibodypedia; 25782; 200 antibodies from 31 providers.
DR DNASU; 97; -.
DR Ensembl; ENST00000238618.8; ENSP00000238618.3; ENSG00000119640.9. [P07311-1]
DR Ensembl; ENST00000357971.7; ENSP00000350655.3; ENSG00000119640.9. [P07311-2]
DR Ensembl; ENST00000555694.5; ENSP00000451581.1; ENSG00000119640.9. [P07311-1]
DR GeneID; 97; -.
DR KEGG; hsa:97; -.
DR MANE-Select; ENST00000238618.8; ENSP00000238618.3; NM_001107.5; NP_001098.1.
DR UCSC; uc001xrf.4; human. [P07311-1]
DR CTD; 97; -.
DR DisGeNET; 97; -.
DR GeneCards; ACYP1; -.
DR HGNC; HGNC:179; ACYP1.
DR HPA; ENSG00000119640; Low tissue specificity.
DR MIM; 600875; gene.
DR neXtProt; NX_P07311; -.
DR OpenTargets; ENSG00000119640; -.
DR PharmGKB; PA24499; -.
DR VEuPathDB; HostDB:ENSG00000119640; -.
DR eggNOG; KOG3360; Eukaryota.
DR GeneTree; ENSGT00940000166472; -.
DR HOGENOM; CLU_141932_0_1_1; -.
DR InParanoid; P07311; -.
DR OMA; FRKYTQG; -.
DR PhylomeDB; P07311; -.
DR TreeFam; TF300288; -.
DR PathwayCommons; P07311; -.
DR SABIO-RK; P07311; -.
DR SignaLink; P07311; -.
DR BioGRID-ORCS; 97; 8 hits in 1078 CRISPR screens.
DR ChiTaRS; ACYP1; human.
DR EvolutionaryTrace; P07311; -.
DR GeneWiki; ACYP1; -.
DR GenomeRNAi; 97; -.
DR Pharos; P07311; Tbio.
DR PRO; PR:P07311; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P07311; protein.
DR Bgee; ENSG00000119640; Expressed in right uterine tube and 189 other tissues.
DR ExpressionAtlas; P07311; baseline and differential.
DR Genevisible; P07311; HS.
DR GO; GO:0003998; F:acylphosphatase activity; IBA:GO_Central.
DR GO; GO:0006796; P:phosphate-containing compound metabolic process; TAS:ProtInc.
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 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3026468"
FT CHAIN 2..99
FT /note="Acylphosphatase-1"
FT /id="PRO_0000158535"
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:0000269|PubMed:3026468"
FT VAR_SEQ 29..99
FT /note="AEGKKLGLVGWVQNTDRGTVQGQLQGPISKVRHMQEWLETRGSPKSHIDKAN
FT FNNEKVILKLDYSDFQIVK -> EMTVENRIAETHSKSCVPVSFATSYAG (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045688"
FT STRAND 7..17
FT /evidence="ECO:0007829|PDB:6CBU"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:6CBU"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:6CBU"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:6CBU"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:2K7J"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:6CBU"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:6CBU"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2K7J"
FT STRAND 75..89
FT /evidence="ECO:0007829|PDB:6CBU"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:6CBU"
SQ SEQUENCE 99 AA; 11261 MW; F9F787E490BC8296 CRC64;
MAEGNTLISV DYEIFGKVQG VFFRKHTQAE GKKLGLVGWV QNTDRGTVQG QLQGPISKVR
HMQEWLETRG SPKSHIDKAN FNNEKVILKL DYSDFQIVK
