AOAH_HUMAN
ID AOAH_HUMAN Reviewed; 575 AA.
AC P28039; A4D1Y5; B7Z490; Q53F13;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Acyloxyacyl hydrolase {ECO:0000303|PubMed:1883828};
DE EC=3.1.1.77 {ECO:0000269|PubMed:1883828, ECO:0000269|PubMed:29343645, ECO:0000269|PubMed:8089145};
DE Contains:
DE RecName: Full=Acyloxyacyl hydrolase small subunit {ECO:0000303|PubMed:1883828};
DE Contains:
DE RecName: Full=Acyloxyacyl hydrolase large subunit {ECO:0000303|PubMed:1883828};
DE Flags: Precursor;
GN Name=AOAH {ECO:0000303|PubMed:1883828};
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), PROTEIN SEQUENCE OF 35-49 AND
RP 157-185, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PROTEOLYTIC CLEAVAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=1883828; DOI=10.1021/bi00098a020;
RA Hagen F.S., Grant F.J., Kuijper J.L., Slaughter C.A., Moomaw C.R., Orth K.,
RA O'Hara P.J., Munford R.S.;
RT "Expression and characterization of recombinant human acyloxyacyl
RT hydrolase, a leukocyte enzyme that deacylates bacterial
RT lipopolysaccharides.";
RL Biochemistry 30:8415-8423(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
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 MRNA] (ISOFORM 1).
RC TISSUE=Synovial cell;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-28.
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-28.
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pancreas;
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 [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PROTEOLYTIC CLEAVAGE, SUBCELLULAR
RP LOCATION, SIGNAL SEQUENCE CLEAVAGE SITE, GLYCOSYLATION AT ASN-59, AND
RP MUTAGENESIS OF THR-61; SER-263; GLY-372 AND PRO-419.
RX PubMed=8089145; DOI=10.1016/s0021-9258(17)31577-6;
RA Staab J.F., Ginkel D.L., Rosenberg G.B., Munford R.S.;
RT "A saposin-like domain influences the intracellular localization,
RT stability, and catalytic activity of human acyloxyacyl hydrolase.";
RL J. Biol. Chem. 269:23736-23742(1994).
RN [9] {ECO:0007744|PDB:5W78, ECO:0007744|PDB:5W7C}
RP X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 24-152 AND 153-575 OF MUTANT
RP ALA-263 IN COMPLEXES WITH CALCIUM; BACTERIAL LIPOPOLYSACCHARIDE CLEAVAGE
RP PRODUCTS, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, MUTAGENESIS OF
RP LYS-173; SER-263; ARG-345 AND LYS-379, SUBUNIT, GLYCOSYLATION AT ASN-59;
RP ASN-207; ASN-409 AND ASN-466, DISULFIDE BONDS, PROTEOLYTIC CLEAVAGE, AND
RP ACTIVITY REGULATION.
RX PubMed=29343645; DOI=10.1073/pnas.1719834115;
RA Gorelik A., Illes K., Nagar B.;
RT "Crystal structure of the mammalian lipopolysaccharide detoxifier.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:E896-E905(2018).
CC -!- FUNCTION: Removes the secondary (acyloxyacyl-linked) fatty acyl chains
CC from the lipid A region of bacterial lipopolysaccharides
CC (PubMed:1883828, PubMed:8089145, PubMed:29343645). By breaking down
CC LPS, terminates the host response to bacterial infection and prevents
CC prolonged and damaging inflammatory responses (By similarity). In
CC peritoneal macrophages, seems to be important for recovery from a state
CC of immune tolerance following infection by Gram-negative bacteria (By
CC similarity). {ECO:0000250|UniProtKB:O35298, ECO:0000269|PubMed:1883828,
CC ECO:0000269|PubMed:29343645, ECO:0000269|PubMed:8089145}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3-(acyloxy)acyl derivative of bacterial toxin + H2O = 3-
CC hydroxyacyl derivative of bacterial toxin + a fatty acid + H(+);
CC Xref=Rhea:RHEA:12032, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:136853, ChEBI:CHEBI:140675;
CC EC=3.1.1.77; Evidence={ECO:0000269|PubMed:1883828,
CC ECO:0000269|PubMed:29343645, ECO:0000269|PubMed:8089145};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:29343645};
CC Note=Binds 3 Ca(2+) ions per subunit. The calcium ions probably have a
CC structural role. {ECO:0000269|PubMed:29343645};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:29343645}.
CC -!- SUBUNIT: Heterodimer of the large and small subunits; disulfide-linked.
CC {ECO:0000269|PubMed:1883828, ECO:0000269|PubMed:29343645,
CC ECO:0000269|PubMed:8089145}.
CC -!- INTERACTION:
CC P28039; Q15700: DLG2; NbExp=3; IntAct=EBI-1222067, EBI-80426;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8089145,
CC ECO:0000305|PubMed:1883828}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:8089145}. Note=Detected in urine.
CC {ECO:0000250|UniProtKB:O35298}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P28039-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P28039-2; Sequence=VSP_042571;
CC -!- PTM: Cleaved into a large and a small subunit.
CC {ECO:0000269|PubMed:1883828, ECO:0000269|PubMed:29343645,
CC ECO:0000269|PubMed:8089145}.
CC -!- PTM: The small subunit is N-glycosylated. {ECO:0000269|PubMed:8089145}.
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DR EMBL; M62840; AAA35506.1; -; mRNA.
DR EMBL; AK297016; BAH12476.1; -; mRNA.
DR EMBL; AK223476; BAD97196.1; -; mRNA.
DR EMBL; AC083876; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC087069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236951; EAL23977.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW94073.1; -; Genomic_DNA.
DR EMBL; BC025698; AAH25698.1; -; mRNA.
DR CCDS; CCDS5448.1; -. [P28039-1]
DR CCDS; CCDS55102.1; -. [P28039-2]
DR PIR; A40292; A40292.
DR RefSeq; NP_001170977.1; NM_001177506.1.
DR RefSeq; NP_001170978.1; NM_001177507.1. [P28039-2]
DR RefSeq; NP_001628.1; NM_001637.3. [P28039-1]
DR PDB; 5W78; X-ray; 2.27 A; A=24-152, B=153-575.
DR PDB; 5W7C; X-ray; 2.23 A; A/B=24-152, C/D=153-575.
DR PDBsum; 5W78; -.
DR PDBsum; 5W7C; -.
DR AlphaFoldDB; P28039; -.
DR SMR; P28039; -.
DR BioGRID; 106810; 1.
DR IntAct; P28039; 2.
DR STRING; 9606.ENSP00000479664; -.
DR GuidetoPHARMACOLOGY; 2873; -.
DR GlyGen; P28039; 4 sites.
DR iPTMnet; P28039; -.
DR PhosphoSitePlus; P28039; -.
DR BioMuta; AOAH; -.
DR DMDM; 113976; -.
DR EPD; P28039; -.
DR MassIVE; P28039; -.
DR PaxDb; P28039; -.
DR PeptideAtlas; P28039; -.
DR PRIDE; P28039; -.
DR ProteomicsDB; 54435; -. [P28039-1]
DR ProteomicsDB; 54436; -. [P28039-2]
DR Antibodypedia; 26560; 150 antibodies from 24 providers.
DR DNASU; 313; -.
DR Ensembl; ENST00000612871.4; ENSP00000484305.1; ENSG00000136250.12. [P28039-2]
DR Ensembl; ENST00000617537.5; ENSP00000483783.1; ENSG00000136250.12. [P28039-1]
DR GeneID; 313; -.
DR KEGG; hsa:313; -.
DR MANE-Select; ENST00000617537.5; ENSP00000483783.1; NM_001637.4; NP_001628.1.
DR UCSC; uc032zjw.2; human. [P28039-1]
DR CTD; 313; -.
DR DisGeNET; 313; -.
DR GeneCards; AOAH; -.
DR HGNC; HGNC:548; AOAH.
DR HPA; ENSG00000136250; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 102593; gene.
DR neXtProt; NX_P28039; -.
DR OpenTargets; ENSG00000136250; -.
DR PharmGKB; PA24838; -.
DR VEuPathDB; HostDB:ENSG00000136250; -.
DR eggNOG; ENOG502QVQW; Eukaryota.
DR GeneTree; ENSGT00390000008427; -.
DR HOGENOM; CLU_025769_0_0_1; -.
DR InParanoid; P28039; -.
DR OMA; AGQPFCH; -.
DR OrthoDB; 692811at2759; -.
DR PhylomeDB; P28039; -.
DR TreeFam; TF329246; -.
DR BRENDA; 3.1.1.77; 2681.
DR PathwayCommons; P28039; -.
DR SignaLink; P28039; -.
DR BioGRID-ORCS; 313; 21 hits in 1073 CRISPR screens.
DR ChiTaRS; AOAH; human.
DR GeneWiki; AOAH; -.
DR GenomeRNAi; 313; -.
DR Pharos; P28039; Tchem.
DR PRO; PR:P28039; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; P28039; protein.
DR Bgee; ENSG00000136250; Expressed in granulocyte and 139 other tissues.
DR ExpressionAtlas; P28039; baseline and differential.
DR Genevisible; P28039; HS.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0050528; F:acyloxyacyl hydrolase activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:UniProtKB.
DR GO; GO:0009104; P:lipopolysaccharide catabolic process; IDA:UniProtKB.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IBA:GO_Central.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR039676; AOAH.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR008138; SapB_2.
DR InterPro; IPR011001; Saposin-like.
DR InterPro; IPR008139; SaposinB_dom.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR15010; PTHR15010; 1.
DR Pfam; PF00657; Lipase_GDSL; 1.
DR Pfam; PF03489; SapB_2; 1.
DR SMART; SM00741; SapB; 1.
DR SUPFAM; SSF47862; SSF47862; 1.
DR PROSITE; PS50015; SAP_B; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cytoplasmic vesicle;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW Lipid metabolism; Metal-binding; Reference proteome; Secreted; Signal;
KW Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:8089145"
FT PROPEP 24..34
FT /evidence="ECO:0000305|PubMed:1883828"
FT /id="PRO_0000020739"
FT CHAIN 35..156
FT /note="Acyloxyacyl hydrolase small subunit"
FT /evidence="ECO:0000305|PubMed:1883828"
FT /id="PRO_0000020740"
FT CHAIN 157..575
FT /note="Acyloxyacyl hydrolase large subunit"
FT /evidence="ECO:0000305|PubMed:1883828"
FT /id="PRO_0000020741"
FT DOMAIN 37..118
FT /note="Saposin B-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415"
FT REGION 38..70
FT /note="Important for enzyme activity, localization to
FT cytoplasmic vesicles, and protein stability"
FT /evidence="ECO:0000269|PubMed:8089145"
FT REGION 173..177
FT /note="Lipopolysaccharide binding"
FT /evidence="ECO:0000250|UniProtKB:O18823"
FT ACT_SITE 263
FT /evidence="ECO:0000305|PubMed:29343645,
FT ECO:0000305|PubMed:8089145"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 205
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 207
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 208
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 213
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:29343645"
FT SITE 345
FT /note="Interacts with lipopolysaccharide"
FT /evidence="ECO:0000250|UniProtKB:O18823"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0000305|PubMed:8089145, ECO:0007744|PDB:5W78"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W78"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W78"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W78"
FT DISULFID 41..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W78,
FT ECO:0007744|PDB:5W7C"
FT DISULFID 44..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W78,
FT ECO:0007744|PDB:5W7C"
FT DISULFID 70..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00415,
FT ECO:0000269|PubMed:29343645, ECO:0007744|PDB:5W78,
FT ECO:0007744|PDB:5W7C"
FT DISULFID 123..453
FT /note="Interchain (between small and large subunit)"
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W78, ECO:0007744|PDB:5W7C"
FT DISULFID 160..169
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W78, ECO:0007744|PDB:5W7C"
FT DISULFID 206..230
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W78, ECO:0007744|PDB:5W7C"
FT DISULFID 249..329
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W78, ECO:0007744|PDB:5W7C"
FT DISULFID 376..459
FT /evidence="ECO:0000269|PubMed:29343645,
FT ECO:0007744|PDB:5W78, ECO:0007744|PDB:5W7C"
FT VAR_SEQ 43..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042571"
FT VARIANT 28
FT /note="D -> N (in dbSNP:rs2228410)"
FT /evidence="ECO:0000269|PubMed:12690205, ECO:0000269|Ref.6"
FT /id="VAR_050663"
FT VARIANT 166
FT /note="A -> T (in dbSNP:rs3735384)"
FT /id="VAR_020133"
FT VARIANT 266
FT /note="A -> G (in dbSNP:rs3735386)"
FT /id="VAR_033513"
FT MUTAGEN 61
FT /note="T->A: Loss of glycosylation. No effect on enzyme
FT activity or localization to cytoplasmic vesicles."
FT /evidence="ECO:0000269|PubMed:8089145"
FT MUTAGEN 173
FT /note="K->E: No effect on enzyme activity."
FT /evidence="ECO:0000269|PubMed:29343645"
FT MUTAGEN 263
FT /note="S->A: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:29343645"
FT MUTAGEN 263
FT /note="S->L: Nearly abolishes catalytic activity."
FT /evidence="ECO:0000269|PubMed:8089145"
FT MUTAGEN 345
FT /note="R->E: No effect on enzyme activity; when associated
FT with E-379."
FT /evidence="ECO:0000269|PubMed:29343645"
FT MUTAGEN 372
FT /note="G->M: Loss of enzyme activity with
FT lipopolysaccharide, due to steric hindrance. No effect on
FT activity with small, synthetic substrate."
FT /evidence="ECO:0000269|PubMed:29343645"
FT MUTAGEN 379
FT /note="K->E: No effect on enzyme activity; when associated
FT with E-345."
FT /evidence="ECO:0000269|PubMed:29343645"
FT MUTAGEN 419
FT /note="P->M: Loss of enzyme activity with
FT lipopolysaccharide, due to steric hindrance. No effect on
FT activity with small, synthetic substrate."
FT /evidence="ECO:0000269|PubMed:29343645"
FT CONFLICT 222
FT /note="W -> C (in Ref. 6; BAD97196)"
FT /evidence="ECO:0000305"
FT HELIX 38..57
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 79..99
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:5W78"
FT HELIX 130..143
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 165..178
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 244..249
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 263..267
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 294..296
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 303..305
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 319..326
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 364..369
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 383..385
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 389..404
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 411..416
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 423..428
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 437..440
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 444..454
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 460..462
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 467..490
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 496..501
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 505..514
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 519..522
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 525..527
FT /evidence="ECO:0007829|PDB:5W7C"
FT STRAND 528..531
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 533..550
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 552..555
FT /evidence="ECO:0007829|PDB:5W7C"
FT HELIX 562..569
FT /evidence="ECO:0007829|PDB:5W7C"
FT TURN 570..573
FT /evidence="ECO:0007829|PDB:5W7C"
SQ SEQUENCE 575 AA; 65105 MW; E3B3853DBD308AF7 CRC64;
MQSPWKILTV APLFLLLSLQ SSASPANDDQ SRPSLSNGHT CVGCVLVVSV IEQLAQVHNS
TVQASMERLC SYLPEKLFLK TTCYLVIDKF GSDIIKLLSA DMNADVVCHT LEFCKQNTGQ
PLCHLYPLPK ETWKFTLQKA RQIVKKSPIL KYSRSGSDIC SLPVLAKICQ KIKLAMEQSV
PFKDVDSDKY SVFPTLRGYH WRGRDCNDSD ESVYPGRRPN NWDVHQDSNC NGIWGVDPKD
GVPYEKKFCE GSQPRGIILL GDSAGAHFHI SPEWITASQM SLNSFINLPT ALTNELDWPQ
LSGATGFLDS TVGIKEKSIY LRLWKRNHCN HRDYQNISRN GASSRNLKKF IESLSRNKVL
DYPAIVIYAM IGNDVCSGKS DPVPAMTTPE KLYSNVMQTL KHLNSHLPNG SHVILYGLPD
GTFLWDNLHN RYHPLGQLNK DMTYAQLYSF LNCLQVSPCH GWMSSNKTLR TLTSERAEQL
SNTLKKIAAS EKFTNFNLFY MDFAFHEIIQ EWQKRGGQPW QLIEPVDGFH PNEVALLLLA
DHFWKKVQLQ WPQILGKENP FNPQIKQVFG DQGGH
