PLB1_RABIT
ID PLB1_RABIT Reviewed; 1458 AA.
AC Q05017;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 108.
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:0000269|PubMed:8509424};
DE AltName: Full=Phospholipase AdRab-B;
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;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Intestine;
RX PubMed=8509424; DOI=10.1016/s0021-9258(18)31471-6;
RA Boll W., Schmid-Chanda T., Semenza G., Mantei N.;
RT "Messenger RNAs expressed in intestine of adult but not baby rabbits.
RT Isolation of cognate cDNAs and characterization of a novel brush border
RT protein with esterase and phospholipase activity.";
RL J. Biol. Chem. 268:12901-12911(1993).
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) (PubMed:8509424). 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 (PubMed:8509424). Hydrolyzes fatty acyl chains
CC of diacylglycerols with preference for the sn-2 position and of
CC triacylglycerols with not positional selectivity (PubMed:8509424). May
CC also hydrolyze long chain retinyl esters such as retinyl palmitate
CC (Probable). May contribute to digestion of dietary phospholipids,
CC glycerolipids and retinoids, facilitating lipid absorption at the brush
CC border (Probable). {ECO:0000269|PubMed:8509424,
CC ECO:0000305|PubMed:8509424}.
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:0000269|PubMed:8509424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:8509424};
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:0000269|PubMed:8509424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:8509424};
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:0000269|PubMed:8509424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40972;
CC Evidence={ECO:0000305|PubMed:8509424};
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:0000269|PubMed:8509424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40976;
CC Evidence={ECO:0000305|PubMed:8509424};
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)-glycerol + H2O = (9Z)-octadecenoate +
CC 1-(9Z-octadecenoyl)-glycerol + H(+); Xref=Rhea:RHEA:40967,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:75342;
CC Evidence={ECO:0000269|PubMed:8509424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40968;
CC Evidence={ECO:0000305|PubMed:8509424};
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:0000269|PubMed:8509424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39940;
CC Evidence={ECO:0000305|PubMed:8509424};
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:0000269|PubMed:8509424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38488;
CC Evidence={ECO:0000305|PubMed:8509424};
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:0000269|PubMed:8509424};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38492;
CC Evidence={ECO:0000305|PubMed:8509424};
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 -!- TISSUE SPECIFICITY: Intestine. {ECO:0000269|PubMed:8509424}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the intestine of adult but not baby
CC rabbits. {ECO:0000269|PubMed:8509424}.
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}.
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DR EMBL; Z12841; CAA78303.1; -; mRNA.
DR PIR; A45665; A45665.
DR RefSeq; NP_001095178.1; NM_001101708.1.
DR AlphaFoldDB; Q05017; -.
DR STRING; 9986.ENSOCUP00000013064; -.
DR SwissLipids; SLP:000000630; -.
DR PRIDE; Q05017; -.
DR GeneID; 100009309; -.
DR KEGG; ocu:100009309; -.
DR CTD; 151056; -.
DR eggNOG; KOG3670; Eukaryota.
DR InParanoid; Q05017; -.
DR OrthoDB; 1232962at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:UniProtKB.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IDA:UniProtKB.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IEA:UniProtKB-EC.
DR GO; GO:0046340; P:diacylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0052651; P:monoacylglycerol catabolic process; IDA:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Hydrolase; Lipid metabolism; Membrane;
KW Phospholipid metabolism; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1458
FT /note="Phospholipase B1, membrane-associated"
FT /id="PRO_0000017854"
FT TOPO_DOM 20..1415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1416..1436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1437..1458
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REPEAT 39..347
FT /note="1"
FT /evidence="ECO:0000255"
FT REPEAT 362..707
FT /note="2"
FT /evidence="ECO:0000255"
FT REPEAT 708..1054
FT /note="3"
FT /evidence="ECO:0000255"
FT REPEAT 1064..1403
FT /note="4"
FT /evidence="ECO:0000255"
FT REGION 39..1403
FT /note="4 X 308-326 AA approximate repeats"
FT /evidence="ECO:0000255"
FT REGION 1404..1446
FT /note="Necessary for membrane localization"
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT ACT_SITE 400
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT ACT_SITE 514
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT ACT_SITE 655
FT /evidence="ECO:0000250|UniProtKB:O54728"
FT CARBOHYD 173
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 529
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 590
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 783
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1077
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 1458 AA; 161344 MW; 9D1608F47B1062E6 CRC64;
MALWPSVFLL GLLPLLGRGA DQIQTSSGKN TLEGQLWPES LKTFPFPCDP KTLAESVPSE
SVHSLRPSDI KFVAAIGNVE TAPDSGADDL EEQDGTEKRP EQACMGVVTV LSDIIGRFSP
SALMPLCPET RLVPRGGAED LWMQATELVR SMRENPQLDF EHDWKLINVF FSNTSQCFPC
PSAQQKGLVL GGMDKLTRTL DYLQQEVPKA FVNLVDLSEL AAFSRWRQGA QLSPAAEPCR
CLRETSQLTK VLTQWSYLEA WDSLLASSKY NTQESFAVVF QPFFYESSLS ALLAEPPLQD
PTTLALSLWN RMMEPIGRKE EPFSEKERKP LRCPTQESPY LFTYRNSGQL TRVSQPQGKL
EVREGTEIRC PDKDPSDSVP TSVHRLKPAD IKVIGAMGDS LTAGNGAGSQ PGNILDVLTQ
YRGLSWSVGG DQNISTVTTL ANILREFNPS LQGFSVGTGR ETTSQAFFNQ AVAGARADGL
IPQAQRLVAL MKNDTRINFQ EDWKIITVFI GGNDLCDFCN DPVRYSPQNF TDNIGTALDI
LHAEIPRAFV NLVKVLEISK LRELYQETKV SCPRMILRSL CPCVLKFDDN STEIASLIET
IKEYQERTQQ LIDSGRYDTR DDFTVVLQPF FEKVNMPKTQ DGLPDNSFFA PDCFHFSSKA
HAHAASALWN NMLEPVGQKT THNDFEGAVN ITCPNQVWPF LSTYKNSVQG FGTWLPCRDR
SPSASPPTSV HALRPADIQV VAALGDSLTA GIGIGSKPND LSDGTTQYRG LSYSSGGDGS
LDNVTTLPNI LRQFNSNLMG FAVGTGDASG TNAFFNQAVP GAKARDLMSQ VQTLVQRMKD
DHRVNFQEDW KVITVQIGAS DLCDYCTDSN LYSAANFYDH LRDALDALHR EVPRALVNLV
DFMNPSVTRQ VFLGNPDKCP VQQASALCNC VLSPRENSYE LARLEALAQA YQSSLRELVE
SGRYDTREDF SVVLQPFFHS IQLPVLQDGR LDTSFFAPDC VHPNQKFHSQ LSRALWRNML
EPLGGKTDAL DLTAAITLTC PTQNEPFLRT FRNSDYTYPS RPAVENWGSD FLCTAWNASR
GVPNSVHELQ PGDIKVVAAL GDSLTLAMGA RPSNSSDPPM FWRGLSWSIG GDGALETHTT
LPNILKKFNP SILGFSTGTL EGTMGLNVAV QGARAQDMPA QARDLVERMR NSPEIDLEKD
WKLVTLFVGG NDLCHFCENP EGSSEGEYVQ HIQQALDVLY EELPRTFVNV VEVMELAGLH
QDQGGRCATL LAAQSHCTCF KYSQSSVEMQ ELKKVNWNLQ SGLSRLSYSH QYVQREDFAV
VVQPFFQNTL VPLNGRGDTD LTFFSDDCFH FSERGHAEMA IALWNNMLEP VGHKTTSNNF
TYSRTKLKCP SPDSPYLYTL RNSRLLPDQA EADPTVLYWA VPVAAGAGLL IGILAMVAGR
GMRCRPREDP PLSLSTGL
