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Protein

Acyloxyacyl hydrolase

Gene

AOAH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Removes the secondary (acyloxyacyl-linked) fatty acyl chains from the lipid A region of bacterial lipopolysaccharides.

Catalytic activityi

3-(acyloxy)acyl group of bacterial toxin = 3-hydroxyacyl group of bacterial toxin + a fatty acid.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei263 – 2631Sequence Analysis

GO - Molecular functioni

  1. acyloxyacyl hydrolase activity Source: UniProtKB-EC
  2. catalytic activity Source: ProtInc
  3. lipoprotein lipase activity Source: ProtInc

GO - Biological processi

  1. inflammatory response Source: ProtInc
  2. lipid metabolic process Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.1.1.77. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Acyloxyacyl hydrolase (EC:3.1.1.77)
Cleaved into the following 2 chains:
Gene namesi
Name:AOAH
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:548. AOAH.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24838.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Propeptidei24 – 34111 PublicationPRO_0000020739Add
BLAST
Chaini35 – 156122Acyloxyacyl hydrolase small subunitPRO_0000020740Add
BLAST
Chaini157 – 575419Acyloxyacyl hydrolase large subunitPRO_0000020741Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi41 ↔ 114PROSITE-ProRule annotation
Disulfide bondi44 ↔ 108PROSITE-ProRule annotation
Glycosylationi59 – 591N-linked (GlcNAc...)PROSITE-ProRule annotation
Disulfide bondi70 ↔ 83PROSITE-ProRule annotation
Disulfide bondi123 ↔ ?
Glycosylationi207 – 2071N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi336 – 3361N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi409 – 4091N-linked (GlcNAc...)PROSITE-ProRule annotation
Glycosylationi466 – 4661N-linked (GlcNAc...)PROSITE-ProRule annotation

Post-translational modificationi

Both subunits contain a number of cysteine residues that may form disulfide bridges.

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

PaxDbiP28039.
PRIDEiP28039.

PTM databases

PhosphoSiteiP28039.

Expressioni

Gene expression databases

BgeeiP28039.
CleanExiHS_AOAH.
ExpressionAtlasiP28039. baseline and differential.
GenevestigatoriP28039.

Organism-specific databases

HPAiHPA021666.
HPA026714.
HPA026716.

Interactioni

Subunit structurei

Heterodimer.

Protein-protein interaction databases

IntActiP28039. 1 interaction.
STRINGi9606.ENSP00000258749.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini37 – 11882Saposin B-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 saposin B-type domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG47076.
GeneTreeiENSGT00390000008427.
HOGENOMiHOG000008100.
HOVERGENiHBG004254.
InParanoidiP28039.
KOiK01065.
OrthoDBiEOG75MVVQ.
PhylomeDBiP28039.
TreeFamiTF329246.

Family and domain databases

Gene3Di1.10.225.10. 1 hit.
3.40.50.1110. 2 hits.
InterProiIPR001087. GDSL.
IPR008138. SapB_2.
IPR011001. Saposin-like.
IPR008139. SaposinB.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 1 hit.
PF03489. SapB_2. 1 hit.
[Graphical view]
SMARTiSM00741. SapB. 1 hit.
[Graphical view]
SUPFAMiSSF47862. SSF47862. 1 hit.
SSF52266. SSF52266. 2 hits.
PROSITEiPS50015. SAP_B. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P28039-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MQSPWKILTV APLFLLLSLQ SSASPANDDQ SRPSLSNGHT CVGCVLVVSV
60 70 80 90 100
IEQLAQVHNS TVQASMERLC SYLPEKLFLK TTCYLVIDKF GSDIIKLLSA
110 120 130 140 150
DMNADVVCHT LEFCKQNTGQ PLCHLYPLPK ETWKFTLQKA RQIVKKSPIL
160 170 180 190 200
KYSRSGSDIC SLPVLAKICQ KIKLAMEQSV PFKDVDSDKY SVFPTLRGYH
210 220 230 240 250
WRGRDCNDSD ESVYPGRRPN NWDVHQDSNC NGIWGVDPKD GVPYEKKFCE
260 270 280 290 300
GSQPRGIILL GDSAGAHFHI SPEWITASQM SLNSFINLPT ALTNELDWPQ
310 320 330 340 350
LSGATGFLDS TVGIKEKSIY LRLWKRNHCN HRDYQNISRN GASSRNLKKF
360 370 380 390 400
IESLSRNKVL DYPAIVIYAM IGNDVCSGKS DPVPAMTTPE KLYSNVMQTL
410 420 430 440 450
KHLNSHLPNG SHVILYGLPD GTFLWDNLHN RYHPLGQLNK DMTYAQLYSF
460 470 480 490 500
LNCLQVSPCH GWMSSNKTLR TLTSERAEQL SNTLKKIAAS EKFTNFNLFY
510 520 530 540 550
MDFAFHEIIQ EWQKRGGQPW QLIEPVDGFH PNEVALLLLA DHFWKKVQLQ
560 570
WPQILGKENP FNPQIKQVFG DQGGH
Length:575
Mass (Da):65,105
Last modified:July 31, 1992 - v1
Checksum:iE3B3853DBD308AF7
GO
Isoform 2 (identifier: P28039-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-74: Missing.

Note: No experimental confirmation available.

Show »
Length:543
Mass (Da):61,647
Checksum:iBE14624794189A57
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti222 – 2221W → C in BAD97196 (Ref. 6) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti28 – 281D → N.2 Publications
Corresponds to variant rs11976480 [ dbSNP | Ensembl ].
VAR_050663
Natural varianti166 – 1661A → T.
Corresponds to variant rs3735384 [ dbSNP | Ensembl ].
VAR_020133
Natural varianti266 – 2661A → G.
Corresponds to variant rs3735386 [ dbSNP | Ensembl ].
VAR_033513

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei43 – 7432Missing in isoform 2. 1 PublicationVSP_042571Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62840 mRNA. Translation: AAA35506.1.
AK297016 mRNA. Translation: BAH12476.1.
AK223476 mRNA. Translation: BAD97196.1.
AC083876 Genomic DNA. No translation available.
AC087069 Genomic DNA. No translation available.
CH236951 Genomic DNA. Translation: EAL23977.1.
CH471073 Genomic DNA. Translation: EAW94073.1.
BC025698 mRNA. Translation: AAH25698.1.
CCDSiCCDS5448.1. [P28039-1]
CCDS55102.1. [P28039-2]
PIRiA40292.
RefSeqiNP_001170977.1. NM_001177506.1.
NP_001170978.1. NM_001177507.1. [P28039-2]
NP_001628.1. NM_001637.3. [P28039-1]
UniGeneiHs.488007.

Genome annotation databases

EnsembliENST00000612871; ENSP00000484305; ENSG00000136250. [P28039-2]
ENST00000617537; ENSP00000483783; ENSG00000136250. [P28039-1]
GeneIDi313.
KEGGihsa:313.
UCSCiuc003tfh.4. human. [P28039-1]
uc011kba.2. human. [P28039-2]

Polymorphism databases

DMDMi113976.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M62840 mRNA. Translation: AAA35506.1.
AK297016 mRNA. Translation: BAH12476.1.
AK223476 mRNA. Translation: BAD97196.1.
AC083876 Genomic DNA. No translation available.
AC087069 Genomic DNA. No translation available.
CH236951 Genomic DNA. Translation: EAL23977.1.
CH471073 Genomic DNA. Translation: EAW94073.1.
BC025698 mRNA. Translation: AAH25698.1.
CCDSiCCDS5448.1. [P28039-1]
CCDS55102.1. [P28039-2]
PIRiA40292.
RefSeqiNP_001170977.1. NM_001177506.1.
NP_001170978.1. NM_001177507.1. [P28039-2]
NP_001628.1. NM_001637.3. [P28039-1]
UniGeneiHs.488007.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP28039. 1 interaction.
STRINGi9606.ENSP00000258749.

PTM databases

PhosphoSiteiP28039.

Polymorphism databases

DMDMi113976.

Proteomic databases

PaxDbiP28039.
PRIDEiP28039.

Protocols and materials databases

DNASUi313.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000612871; ENSP00000484305; ENSG00000136250. [P28039-2]
ENST00000617537; ENSP00000483783; ENSG00000136250. [P28039-1]
GeneIDi313.
KEGGihsa:313.
UCSCiuc003tfh.4. human. [P28039-1]
uc011kba.2. human. [P28039-2]

Organism-specific databases

CTDi313.
GeneCardsiGC07M036519.
HGNCiHGNC:548. AOAH.
HPAiHPA021666.
HPA026714.
HPA026716.
MIMi102593. gene.
neXtProtiNX_P28039.
PharmGKBiPA24838.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG47076.
GeneTreeiENSGT00390000008427.
HOGENOMiHOG000008100.
HOVERGENiHBG004254.
InParanoidiP28039.
KOiK01065.
OrthoDBiEOG75MVVQ.
PhylomeDBiP28039.
TreeFamiTF329246.

Enzyme and pathway databases

BRENDAi3.1.1.77. 2681.

Miscellaneous databases

ChiTaRSiAOAH. human.
GeneWikiiAOAH.
GenomeRNAii313.
NextBioi1273.
PROiP28039.
SOURCEiSearch...

Gene expression databases

BgeeiP28039.
CleanExiHS_AOAH.
ExpressionAtlasiP28039. baseline and differential.
GenevestigatoriP28039.

Family and domain databases

Gene3Di1.10.225.10. 1 hit.
3.40.50.1110. 2 hits.
InterProiIPR001087. GDSL.
IPR008138. SapB_2.
IPR011001. Saposin-like.
IPR008139. SaposinB.
IPR013830. SGNH_hydro.
[Graphical view]
PfamiPF00657. Lipase_GDSL. 1 hit.
PF03489. SapB_2. 1 hit.
[Graphical view]
SMARTiSM00741. SapB. 1 hit.
[Graphical view]
SUPFAMiSSF47862. SSF47862. 1 hit.
SSF52266. SSF52266. 2 hits.
PROSITEiPS50015. SAP_B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 35-49 AND 157-185.
  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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Umbilical cord blood.
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Synovial cell.
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-28.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ASN-28.
  7. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Pancreas.

Entry informationi

Entry nameiAOAH_HUMAN
AccessioniPrimary (citable) accession number: P28039
Secondary accession number(s): A4D1Y5, B7Z490, Q53F13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 31, 1992
Last sequence update: July 31, 1992
Last modified: March 31, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.