P07311 (ACYP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acylphosphatase-1
EC=3.6.1.7

Alternative name(s):
Acylphosphatase, erythrocyte isozyme
Acylphosphatase, organ-common type isozyme
Acylphosphate phosphohydrolase 1

Gene names

Name:	ACYP1
Synonyms:	ACYPE

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	99 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Its physiological role is not yet clear.
Catalytic activity	An acylphosphate + H2O = a carboxylate + phosphate.
Tissue specificity	Organ-common type isozyme is found in many different tissues.
Sequence similarities	Belongs to the acylphosphatase family. Contains 1 acylphosphatase-like domain.

Ontologies

Keywords
Coding sequence diversity	Alternative splicing
Molecular function	Hydrolase
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	phosphate-containing compound metabolic process Traceable author statement Ref.6. Source: ProtInc
Molecular_function	acylphosphatase activity Traceable author statement Ref.7. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P07311-1)

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.

Isoform 2 (identifier: P07311-2)

The sequence of this isoform differs from the canonical sequence as follows:
     29-99: AEGKKLGLVG...LDYSDFQIVK → EMTVENRIAETHSKSCVPVSFATSYAG

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 99

98

Acylphosphatase-1

PRO_0000158535

Regions

Domain

9 – 99

91

Acylphosphatase-like

Sites

Active site

24

1

Potential

Active site

42

1

Potential

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.6

Natural variations

Alternative sequence

29 – 99

71

AEGKK…FQIVK → EMTVENRIAETHSKSCVPVS FATSYAG in isoform 2.

VSP_045688

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

99

Helix Strand Turn

Details...

Beta strand

7 – 17

11

Beta strand

19 – 21

3

Helix

23 – 33

11

Beta strand

37 – 42

6

Beta strand

44 – 46

3

Beta strand

48 – 55

8

Helix

56 – 68

13

Beta strand

72 – 74

3

Beta strand

75 – 89

15

Beta strand

93 – 97

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: F9F787E490BC8296	FASTA	99	11,261
	10 20 30 40 50 60 MAEGNTLISV DYEIFGKVQG VFFRKHTQAE GKKLGLVGWV QNTDRGTVQG QLQGPISKVR 70 80 90 HMQEWLETRG SPKSHIDKAN FNNEKVILKL DYSDFQIVK
	Isoform 2 [UniParc]. Checksum: 37822D3FA5EF8F81	FASTA	55	6,113
	10 20 30 40 50 MAEGNTLISV DYEIFGKVQG VFFRKHTQEM TVENRIAETH SKSCVPVSFA TSYAG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Raugei G. Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[2]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Testis.
[3]	"The DNA sequence and analysis of human chromosome 14." 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. Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] (ISOFORMS 1 AND 2). Tissue: Embryonic carcinoma and Mammary gland.
[6]	"A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure." Liguri G., Camici G., Manao G., Cappugi G., Nassi P., Modesti A., Ramponi G. Biochemistry 25:8089-8094(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-99.
[7]	"Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase." Fiaschi T., Raugei G., Marzocchini R., Chiarugi P., Cirri P., Ramponi G. FEBS Lett. 367:145-148(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 10-86. Tissue: Placenta.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]	"Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase." Yeung R.C., Lam S.Y., Wong K.B. Acta Crystallogr. F 62:80-82(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS).
[10]	"Rational stabilization of enzymes by computational redesign of surface charge-charge interactions." Gribenko A.V., Patel M.M., Liu J., McCallum S.A., Wang C., Makhatadze G.I. Proc. Natl. Acad. Sci. U.S.A. 106:2601-2606(2009) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 2-99.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X84194 mRNA. Translation: CAA58987.1.
AK312101 mRNA. Translation: BAG35037.1.
AC007055 Genomic DNA. Translation: AAD31937.1.
AL049780 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW81216.1.
BC035568 mRNA. Translation: AAH35568.1.
BG614847 mRNA. No translation available.

IPI

IPI00221117.
IPI00409627.

PIR

QPHUE. S66187.

RefSeq

NP_001098.1. NM_001107.3.
NP_982355.1. NM_203488.1.

UniGene

Hs.18573.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K7J	NMR	-	A	2-99	[»]
2K7K	NMR	-	A	2-99	[»]
2VH7	X-ray	1.45	A	1-99	[»]
2W4C	X-ray	1.52	A	1-98	[»]
2W4P	X-ray	1.70	A	1-98	[»]
3TOQ	X-ray	2.00	A	1-99	[»]

ProteinModelPortal

P07311.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000238618.

PTM databases

PhosphoSite

P07311.

Polymorphism databases

DMDM

2507560.

Proteomic databases

PaxDb

P07311.

PRIDE

P07311.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000238618; ENSP00000238618; ENSG00000119640.
ENST00000357971; ENSP00000350655; ENSG00000119640.
ENST00000555694; ENSP00000451581; ENSG00000119640.

GeneID

97.

KEGG

hsa:97.

UCSC

uc001xrg.3. human.

Organism-specific databases

CTD

97.

GeneCards

GC14M075519.

HGNC

HGNC:179. ACYP1.

HPA

HPA034944.

MIM

600875. gene.

neXtProt

NX_P07311.

PharmGKB

PA24499.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG289322.

HOGENOM

HOG000292688.

HOVERGEN

HBG050454.

InParanoid

P07311.

KO

K01512.

OrthoDB

EOG4XD3SN.

PhylomeDB

P07311.

Enzyme and pathway databases

SABIO-RK

P07311.

Gene expression databases

ArrayExpress

P07311.

Bgee

P07311.

CleanEx

HS_ACYP1.

Genevestigator

P07311.

GermOnline

ENSG00000119640. Homo sapiens.

Family and domain databases

InterPro

IPR020456. Acylphosphatase.
IPR001792. Acylphosphatase-like.
IPR017968. Acylphosphatase_CS.
[Graphical view]

Pfam

PF00708. Acylphosphatase. 1 hit.
[Graphical view]

PRINTS

PR00112. ACYLPHPHTASE.

SUPFAM

SSF54975. Acylphosphatase. 1 hit.

PROSITE

PS00150. ACYLPHOSPHATASE_1. 1 hit.
PS00151. ACYLPHOSPHATASE_2. 1 hit.
PS51160. ACYLPHOSPHATASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07311.

GenomeRNAi

97.

NextBio

367.

SOURCE

Search...

Entry information

Entry name

ACYP1_HUMAN

Accession

Primary (citable) accession number: P07311
Secondary accession number(s): A6NDV8, B2R590

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 130 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.