P28039 (AOAH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acyloxyacyl hydrolase
EC=3.1.1.77

Cleaved into the following 2 chains:

1. Acyloxyacyl hydrolase small subunit
2. Acyloxyacyl hydrolase large subunit

Gene names

Name:

AOAH

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	575 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	Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides.
Catalytic activity	3-(acyloxy)acyl group of bacterial toxin = 3-hydroxyacyl group of bacterial toxin + a fatty acid.
Subunit structure	Heterodimer.
Subcellular location	Secreted.
Post-translational modification	Both subunits contain a number of cysteine residues that may form disulfide bridges.
Sequence similarities	Contains 1 saposin B-type domain.

Ontologies

Keywords
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	inflammatory response Traceable author statement. Source: ProtInc
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	acyloxyacyl hydrolase activity Inferred from electronic annotation. Source: EC lipoprotein lipase activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23	Potential
	Propeptide	24 – 34	11			PRO_0000020739
	Chain	35 – 156	122	Acyloxyacyl hydrolase small subunit		PRO_0000020740
	Chain	157 – 575	419	Acyloxyacyl hydrolase large subunit		PRO_0000020741
Regions
	Domain	37 – 118	82	Saposin B-type
Sites
	Active site	263	1	Potential
Amino acid modifications
	Glycosylation	59	1	N-linked (GlcNAc...) Potential
	Glycosylation	207	1	N-linked (GlcNAc...) Potential
	Glycosylation	336	1	N-linked (GlcNAc...) Potential
	Glycosylation	409	1	N-linked (GlcNAc...) Potential
	Glycosylation	466	1	N-linked (GlcNAc...) Potential
	Disulfide bond	41 ↔ 114		By similarity
	Disulfide bond	44 ↔ 108		By similarity
	Disulfide bond	70 ↔ 83		By similarity
	Disulfide bond	123 ↔ ?
Natural variations
	Natural variant	28	1	D → N. Ref.2 Ref.3 Corresponds to variant rs11976480 [ dbSNP | Ensembl ].		VAR_050663
	Natural variant	166	1	A → T. Corresponds to variant rs3735384 [ dbSNP | Ensembl ].		VAR_020133
	Natural variant	266	1	A → G. Corresponds to variant rs3735386 [ dbSNP | Ensembl ].		VAR_033513
Experimental info
	Sequence conflict	222	1	W → C in BAD97196. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P28039 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: E3B3853DBD308AF7	FASTA	575	65,105
	10 20 30 40 50 60 MQSPWKILTV APLFLLLSLQ SSASPANDDQ SRPSLSNGHT CVGCVLVVSV IEQLAQVHNS 70 80 90 100 110 120 TVQASMERLC SYLPEKLFLK TTCYLVIDKF GSDIIKLLSA DMNADVVCHT LEFCKQNTGQ 130 140 150 160 170 180 PLCHLYPLPK ETWKFTLQKA RQIVKKSPIL KYSRSGSDIC SLPVLAKICQ KIKLAMEQSV 190 200 210 220 230 240 PFKDVDSDKY SVFPTLRGYH WRGRDCNDSD ESVYPGRRPN NWDVHQDSNC NGIWGVDPKD 250 260 270 280 290 300 GVPYEKKFCE GSQPRGIILL GDSAGAHFHI SPEWITASQM SLNSFINLPT ALTNELDWPQ 310 320 330 340 350 360 LSGATGFLDS TVGIKEKSIY LRLWKRNHCN HRDYQNISRN GASSRNLKKF IESLSRNKVL 370 380 390 400 410 420 DYPAIVIYAM IGNDVCSGKS DPVPAMTTPE KLYSNVMQTL KHLNSHLPNG SHVILYGLPD 430 440 450 460 470 480 GTFLWDNLHN RYHPLGQLNK DMTYAQLYSF LNCLQVSPCH GWMSSNKTLR TLTSERAEQL 490 500 510 520 530 540 SNTLKKIAAS EKFTNFNLFY MDFAFHEIIQ EWQKRGGQPW QLIEPVDGFH PNEVALLLLA 550 560 570 DHFWKKVQLQ WPQILGKENP FNPQIKQVFG DQGGH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides." Hagen F.S., Grant F.J., Kuijper J.L., Slaughter C.A., Moomaw C.R., Orth K., O'Hara P.J., Munford R.S. Biochemistry 30:8415-8423(1991) [PubMed: 1883828] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-49 AND 157-185.
[2]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed: 12690205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-28.
[3]	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], VARIANT ASN-28.
[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Synovial cell.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M62840 mRNA. Translation: AAA35506.1. AK223476 mRNA. Translation: BAD97196.1. CH236951 Genomic DNA. Translation: EAL23977.1. CH471073 Genomic DNA. Translation: EAW94073.1. BC025698 mRNA. Translation: AAH25698.1.
IPI	IPI00000731.
PIR	A40292.
RefSeq	NP_001170977.1. NM_001177506.1. NP_001628.1. NM_001637.3.
UniGene	Hs.488007.
3D structure databases
ProteinModelPortal	P28039.
SMR	P28039. Positions 39-117.
ModBase	Search...
Protein-protein interaction databases
IntAct	P28039. 1 interaction.
STRING	P28039.
Polymorphism databases
DMDM	113976.
Proteomic databases
PRIDE	P28039.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000258749; ENSP00000258749; ENSG00000136250.
GeneID	313.
KEGG	hsa:313.
UCSC	uc003tfh.2. human.
Organism-specific databases
CTD	313.
GeneCards	GC07M036519.
H-InvDB	HIX0006604.
HGNC	HGNC:548. AOAH.
MIM	102593. gene.
neXtProt	NX_P28039.
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00390000008427.
HOVERGEN	HBG004254.
InParanoid	P28039.
OrthoDB	EOG444KK0.
PhylomeDB	P28039.
Enzyme and pathway databases
BRENDA	3.1.1.77. 2681.
Gene expression databases
ArrayExpress	P28039.
Bgee	P28039.
CleanEx	HS_AOAH.
Genevestigator	P28039.
GermOnline	ENSG00000136250. Homo sapiens.
Family and domain databases
InterPro	IPR013830. Esterase_SGNH_hydro-type. IPR013831. Esterase_SGNH_hydro-type_subgr. IPR001087. Lipase_GDSL. IPR008138. SapB_2. IPR011001. Saposin-like. IPR008139. SaposinB. [Graphical view]
Gene3D	G3DSA:3.40.50.1110. Esterase_SGNH_hydro-type_subgr. 3 hits. G3DSA:1.10.225.10. Saposin_like. 1 hit.
KO	K01065.
Pfam	PF00657. Lipase_GDSL. 1 hit. PF03489. SapB_2. 1 hit. [Graphical view]
SMART	SM00741. SapB. 1 hit. [Graphical view]
SUPFAM	SSF52266. Esterase_SGNH_hydro-type. 1 hit. SSF47862. Saposin_like. 1 hit.
PROSITE	PS01098. LIPASE_GDSL_SER. False negative. PS50015. SAP_B. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	1273.
SOURCE	Search...

Entry information

Entry name

AOAH_HUMAN

Accession

Primary (citable) accession number: P28039
Secondary accession number(s): A4D1Y5, Q53F13

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	December 14, 2011
This is version 101 of the entry and version 1 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.