PLB1_MONDO
ID PLB1_MONDO Reviewed; 1474 AA.
AC Q06HQ7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Phospholipase B1, membrane-associated;
DE Short=Phospholipase B;
DE AltName: Full=Lysophospholipase;
DE EC=3.1.1.5 {ECO:0000250|UniProtKB:O54728};
DE AltName: Full=Phospholipase A2;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:O54728};
DE AltName: Full=Phospholipase B/lipase;
DE Short=PLB/LIP;
DE AltName: Full=Triacylglycerol lipase;
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:O54728};
DE Flags: Precursor;
GN Name=PLB1; Synonyms=PLB;
OS Monodelphis domestica (Gray short-tailed opossum).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Didelphimorphia; Didelphidae; Monodelphis.
OX NCBI_TaxID=13616;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Chan J., Kushwaha R.S., Gluhak-Heinrich J., Donalson L.M., VandeBerg J.F.,
RA VandeBerg J.L.;
RT "Dietary cholesterol increases intestinal phospholipase B gene expression
RT in laboratory opossums.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Calcium-independent membrane-associated phospholipase that
CC catalyzes complete diacylation of phospholipids by hydrolyzing both sn-
CC 1 and sn-2 fatty acyl chains attached to the glycerol backbone
CC (phospholipase B activity) (By similarity). Has dual phospholipase and
CC lysophospholipase activities toward diacylphospholipids. Preferentially
CC cleaves sn-2 ester bonds over sn-1 bonds. Acts as a lipase toward
CC glycerolipid substrates (By similarity). Hydrolyzes fatty acyl chains
CC of diacylglycerols with preference for the sn-2 position and of
CC triacylglycerols with not positional selectivity (By similarity). May
CC also hydrolyze long chain retinyl esters such as retinyl palmitate (By
CC similarity). May contribute to digestion of dietary phospholipids,
CC glycerolipids and retinoids, facilitating lipid absorption at the brush
CC border (By similarity). {ECO:0000250|UniProtKB:O54728,
CC ECO:0000250|UniProtKB:Q05017}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H(+); Xref=Rhea:RHEA:40923, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28610, ChEBI:CHEBI:30823, ChEBI:CHEBI:74669;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40924;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = 2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:40971,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:73002, ChEBI:CHEBI:76084;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40911,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73004, ChEBI:CHEBI:73007;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40912;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1'-
CC sn-glycerol) + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-
CC 3-phospho-(1'-sn-glycerol) + H(+); Xref=Rhea:RHEA:40919,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:72841, ChEBI:CHEBI:75158;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40920;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + 2 H2O = 2
CC H(+) + 2 hexadecanoate + sn-glycerol 3-phosphocholine;
CC Xref=Rhea:RHEA:40975, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(9Z)-octadecenoyl-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-O-hexadecyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:40915, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:34112,
CC ChEBI:CHEBI:64496; Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40916;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + di-(9Z)-octadecenoylglycerol + H(+);
CC Xref=Rhea:RHEA:38575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC + H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + H(+) +
CC octadecanoate; Xref=Rhea:RHEA:41111, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75466,
CC ChEBI:CHEBI:77623; Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41112;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = (9Z)-
CC octadecenoate + 1,3-dihexadecanoylglycerol + H(+);
CC Xref=Rhea:RHEA:40983, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75688, ChEBI:CHEBI:77619;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40984;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-dihexadecanoyl-2-(9Z-octadecenoyl)glycerol + H2O = 1-
CC hexadecanoyl-2-(9Z-octadecenoyl)glycerol + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:40979, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:75585, ChEBI:CHEBI:75688;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40980;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-3-octadecanoyl-sn-
CC glycerol + H(+); Xref=Rhea:RHEA:41103, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77623,
CC ChEBI:CHEBI:77624; Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41104;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z)-octadecenoyl-3-octadecanoyl-sn-glycerol
CC + H2O = 2-(9Z-octadecenoyl)-3-octadecanoyl-sn-glycerol + H(+) +
CC hexadecanoate; Xref=Rhea:RHEA:41107, ChEBI:CHEBI:7896,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75558,
CC ChEBI:CHEBI:77623; Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41108;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-glycerol + H2O =
CC (9Z,12Z)-octadecadienoate + 1-octadecanoyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:40927, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75550, ChEBI:CHEBI:77097;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40928;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 1-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:41219, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:75757;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41220;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 3-(9Z-octadecenoyl)-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:42604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75824, ChEBI:CHEBI:75938;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42605;
CC Evidence={ECO:0000250|UniProtKB:O54728};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC (9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:39939,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75735, ChEBI:CHEBI:75937;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38487, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75342; Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC glycerol + H(+); Xref=Rhea:RHEA:38491, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:73990; Evidence={ECO:0000250|UniProtKB:Q05017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC Evidence={ECO:0000250|UniProtKB:Q05017};
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:O54728}; Single-pass type I membrane protein
CC {ECO:0000255}. Note=Present in the intestinal brush border membranes.
CC {ECO:0000250|UniProtKB:O54728}.
CC -!- DOMAIN: Repeat 2 contains the catalytic domain.
CC {ECO:0000250|UniProtKB:O54728}.
CC -!- PTM: Undergoes proteolytic cleavage in the ileum.
CC {ECO:0000250|UniProtKB:O54728}.
CC -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC Phospholipase B1 subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ875604; ABI74623.1; -; mRNA.
DR RefSeq; NP_001070653.1; NM_001077185.1.
DR AlphaFoldDB; Q06HQ7; -.
DR STRING; 13616.ENSMODP00000019434; -.
DR PRIDE; Q06HQ7; -.
DR GeneID; 768082; -.
DR KEGG; mdo:768082; -.
DR CTD; 151056; -.
DR eggNOG; KOG3670; Eukaryota.
DR InParanoid; Q06HQ7; -.
DR OrthoDB; 1232962at2759; -.
DR Proteomes; UP000002280; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031526; C:brush border membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004622; F:lysophospholipase activity; IBA:GO_Central.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0004623; F:phospholipase A2 activity; IBA:GO_Central.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0050253; F:retinyl-palmitate esterase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central.
DR CDD; cd01824; Phospholipase_B_like; 3.
DR Gene3D; 3.40.50.1110; -; 3.
DR InterPro; IPR001087; GDSL.
DR InterPro; IPR008265; Lipase_GDSL_AS.
DR InterPro; IPR035547; Phospholipase_B.
DR InterPro; IPR038885; PLB1.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR21325; PTHR21325; 3.
DR Pfam; PF00657; Lipase_GDSL; 3.
DR PROSITE; PS01098; LIPASE_GDSL_SER; 2.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Hydrolase; Lipid metabolism; Membrane;
KW Phospholipid metabolism; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..1474
FT /note="Phospholipase B1, membrane-associated"
FT /id="PRO_0000324384"
FT TOPO_DOM 23..1432
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1433..1453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1454..1474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 36..350
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 365..710
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 711..1069
FT /note="3"
FT /evidence="ECO:0000255"
FT REPEAT 1079..1417
FT /note="4"
FT /evidence="ECO:0000255"
FT REGION 36..1417
FT /note="4 X 308-326 AA approximate repeats"
FT /evidence="ECO:0000255"
FT REGION 1418..1461
FT /note="Necessary for membrane localization"
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT ACT_SITE 403
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT ACT_SITE 517
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT ACT_SITE 658
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 532
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 593
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 711
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 813
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1070
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1474 AA; 165157 MW; B22844CD69B35A60 CRC64;
MRLQPSLLLL ALLLLKVTTI QATLGNNSWE EQTWPEGLKN FPFPCRPEEI PFSPPSESVH
SLRISDIRVV GAIGNLETTP DAKMVLKRQK WIERNQMQTC MQVMTVLSDF IKKFSPSVLP
LLCPSREKVL PRMRNEDLGP QARELVQHMK KNQKLNFRND WKLINVFFNA QSQCHPCSSS
QKEGNMTSSM QELIRLLDYL QKEVPKAFVN LVDISELGNS IQSNNQENGP RDINEVCECP
QEPSRLTTAV QRWYYQNSWE KLLTSGRYDT KDTFTVIYQS FLHEMEPSVF PIKQTSGSSL
KKLSTALAVS LWNGMIDPTG KKEEFFTTGQ RIPVKCPTQK HPYLFTYRNN NKLSSTPEIK
RISETREGTE IRCPDMDPSN AVPTSVHHLR PADIKVIGAL GDSLTAGNGA GSTPGNILDV
LTQYRGLSWS IGGNENISTV TTLANILREF NPSLIGFSTG TGNQNSAAAF LNQAVAGATS
ETLPSQARRL VDLMKENKRI NFQDDWKIVT LFIGGNDLCD SCSDPPRYSS QNFTAHIGKA
LDILHAEVPR VFVNLVTVLS IVSLRELYQE ESINCPRVIL RSLCPCVLKF KDNSTELTTL
IELNKQYQEE THRLVDSGRY DTRDDFTVVL QPFLEQVPMP KTPEGLPDSS FFAPDCFHFH
SKAHARVARS LWNNMLEPVG EKKKEENLEN IVDLICPSES QPYLRTYKNS NYTYPTATPT
SSPKPDYGSQ LWCEDRAPSA SFPTSVHALK PADIQVVAAV GDSLTAGNGI GSKPDDLPDV
ITQYRGLSYS AGGDASLESV TTLPNILREF NMNLTGFAVG VGSADDANAF LNQAVPGAKA
EGLKKQVQTL VQKMKSDPRI NFQRDWKVIT LLIGTTDLCD YCTDSNLYSA TNFSAYLRDA
LDFLHREVPR ALVNLVDFMN PIIFRQVFLG NQDKCPMTQA CSLCNCLLTV REDSPELARM
KEVVKVYQTK IRELVESGRY DTREDFTIVL QPFLEEVKLA FQDGIPDVSF FAPDCIHPNQ
KFHSQLSRAL WNNMLQPLGK KMDFLDLTAD TTLSCPSLEE PFLRTYRNSN YTYPANPAIE
NWGSDFLCPE QGSSNSAPSS VHQLRPADIK VVAALGDSLT TAVGAGAKNN SNWSTAWRGL
SWSIGGDGTL ETHTTLPNIL KKFNPHLHGF STGTQEEAAG LNVAVEGAIA QDMPSQARIL
VDRMKNSSEI NLDQDWKLIT IFVGSNDLCQ YCENPEAHSV KNYVQSLQQA LDIFYKELPR
AFINVVEIME LVGLRQIQGE KCAVTTQSIC PCFGRSLDNS PELQEMKNIN RHFQSGSSLI
TYHHQYMERE DFAVVVQPFF QSTVVPLDDK GKPDLSFFSV DCFHFSERGH AEMAIALWNN
MLEPVGQKQT YNNFTHSRTK VKCPTSENPY FFTMRNSGLL RKEASHKTPS VPFWAVLVAA
AASFIVGVVL VMLWRTKKCS RREERPISLV ATVF
