LIPC_RAT
ID LIPC_RAT Reviewed; 494 AA.
AC P07867;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 25-MAY-2022, entry version 156.
DE RecName: Full=Hepatic triacylglycerol lipase;
DE Short=HL;
DE Short=Hepatic lipase;
DE EC=3.1.1.3 {ECO:0000269|PubMed:1531641, ECO:0000269|PubMed:1770315, ECO:0000269|PubMed:1865764, ECO:0000269|PubMed:7074125};
DE AltName: Full=Lipase member C;
DE AltName: Full=Lysophospholipase;
DE EC=3.1.1.5 {ECO:0000269|PubMed:1531641};
DE AltName: Full=Phospholipase A1;
DE EC=3.1.1.32 {ECO:0000269|PubMed:1531641, ECO:0000269|PubMed:1865764, ECO:0000269|PubMed:6747460, ECO:0000269|PubMed:7074125};
DE Flags: Precursor;
GN Name=Lipc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=2322583; DOI=10.1016/0167-4781(90)90071-9;
RA Sensel M.G., Legrand-Lorans A., Wang M.E., Bensadoun A.;
RT "Isolation and characterization of clones for the rat hepatic lipase gene
RT upstream regulatory region.";
RL Biochim. Biophys. Acta 1048:297-302(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=3470738; DOI=10.1073/pnas.84.6.1526;
RA Komaromy M.C., Schotz M.C.;
RT "Cloning of rat hepatic lipase cDNA: evidence for a lipase gene family.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:1526-1530(1987).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=7074125; DOI=10.1016/0005-2760(82)90130-8;
RA Jensen G.L., Daggy B., Bensadoun A.;
RT "Triacylglycerol lipase, monoacylglycerol lipase and phospholipase
RT activities of highly purified rat hepatic lipase.";
RL Biochim. Biophys. Acta 710:464-470(1982).
RN [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6747460;
RA Landin B., Nilsson A., Twu J.S., Schotz M.C.;
RT "A role for hepatic lipase in chylomicron and high density lipoprotein
RT phospholipid metabolism.";
RL J. Lipid Res. 25:559-563(1984).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=1770315;
RA Warren R.J., Ebert D.L., Mitchell A., Barter P.J.;
RT "Rabbit hepatic lipase cDNA sequence: low activity is associated with low
RT messenger RNA levels.";
RL J. Lipid Res. 32:1333-1339(1991).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1865764; DOI=10.1007/bf02537138;
RA Wilcox R.W., Thuren T., Sisson P., Kucera G.L., Waite M.;
RT "Hydrolysis of neutral lipid substrates by rat hepatic lipase.";
RL Lipids 26:283-288(1991).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RX PubMed=1531641; DOI=10.1016/0014-5793(92)80294-q;
RA Bohn E., Gerke V., Kresse H., Loeffler B.M., Kunze H.;
RT "Annexin II inhibits calcium-dependent phospholipase A1 and
RT lysophospholipase but not triacyl glycerol lipase activities of rat liver
RT hepatic lipase.";
RL FEBS Lett. 296:237-240(1992).
CC -!- FUNCTION: Catalyzes the hydrolysis of triglycerides and phospholipids
CC present in circulating plasma lipoproteins, including chylomicrons,
CC intermediate density lipoproteins (IDL), low density lipoproteins (LDL)
CC of large size and high density lipoproteins (HDL), releasing free fatty
CC acids (FFA) and smaller lipoprotein particles (PubMed:7074125,
CC PubMed:6747460, PubMed:1770315, PubMed:1865764, PubMed:1531641). Also
CC exhibits lysophospholipase activity (PubMed:1531641). Can hydrolyze
CC both neutral lipid and phospholipid substrates but shows a greater
CC binding affinity for neutral lipid substrates than phospholipid
CC substrates (PubMed:1865764). In native LDL, preferentially hydrolyzes
CC the phosphatidylcholine species containing polyunsaturated fatty acids
CC at sn-2 position (By similarity). {ECO:0000250|UniProtKB:P11150,
CC ECO:0000269|PubMed:1531641, ECO:0000269|PubMed:1770315,
CC ECO:0000269|PubMed:1865764, ECO:0000269|PubMed:6747460,
CC ECO:0000269|PubMed:7074125}.
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:0000269|PubMed:1531641, ECO:0000269|PubMed:1770315,
CC ECO:0000269|PubMed:1865764, ECO:0000269|PubMed:7074125};
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:0000269|PubMed:1531641};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:57875; EC=3.1.1.32;
CC Evidence={ECO:0000269|PubMed:1531641, ECO:0000269|PubMed:1865764,
CC ECO:0000269|PubMed:6747460, ECO:0000269|PubMed:7074125};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycerol + H2O = (9Z)-
CC octadecenoate + 2-(9Z-octadecenoyl)-glycerol + H(+);
CC Xref=Rhea:RHEA:38511, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:52333, ChEBI:CHEBI:73990;
CC Evidence={ECO:0000269|PubMed:1865764};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38512;
CC Evidence={ECO:0000305|PubMed:1865764};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:38391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75824;
CC Evidence={ECO:0000269|PubMed:1531641, ECO:0000269|PubMed:7074125};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392;
CC Evidence={ECO:0000305|PubMed:1531641};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O =
CC (9Z)-octadecenoate + H(+) + sn-glycero-3-phospho-L-serine;
CC Xref=Rhea:RHEA:40499, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:64765, ChEBI:CHEBI:74617;
CC Evidence={ECO:0000269|PubMed:1531641};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40500;
CC Evidence={ECO:0000305|PubMed:1531641};
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:0000269|PubMed:1531641};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:1531641};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-octadecenoate +
CC 3-(9Z-octadecenoyl)-sn-glycerol + H(+); Xref=Rhea:RHEA:38651,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:75735, ChEBI:CHEBI:75938;
CC Evidence={ECO:0000269|PubMed:1531641};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38652;
CC Evidence={ECO:0000305|PubMed:1531641};
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:P11150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000250|UniProtKB:P11150};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O =
CC (9Z)-octadecenoate + (9Z-octadecenoyl)-sn-glycero-3-phosphocholine +
CC H(+); Xref=Rhea:RHEA:38699, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:74669, ChEBI:CHEBI:76083;
CC Evidence={ECO:0000250|UniProtKB:P11150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38700;
CC Evidence={ECO:0000250|UniProtKB:P11150};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tributanoylglycerol + H2O = butanoate +
CC dibutanoylglycerol + H(+); Xref=Rhea:RHEA:40475, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:35020,
CC ChEBI:CHEBI:76478; Evidence={ECO:0000250|UniProtKB:P11150};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40476;
CC Evidence={ECO:0000250|UniProtKB:P11150};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + hexadecanoyl-sn-glycero-3-phosphocholine;
CC Xref=Rhea:RHEA:41384, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64563, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:7074125};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41385;
CC Evidence={ECO:0000269|PubMed:7074125};
CC -!- ACTIVITY REGULATION: Phospholipase A1 and lysophospholipase activities
CC are inhibited by annexin II. {ECO:0000269|PubMed:1531641}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.82 mM for 1,2,3-tri-(9Z-octadecenoyl)-glycerol
CC {ECO:0000269|PubMed:7074125};
CC KM=0.16 mM for 1,2-di-O-palmitoyl-sn-glycero-3-phosphocholine
CC {ECO:0000269|PubMed:7074125};
CC Vmax=144 umol/min/mg enzyme with 1-oleoyl-sn-glycerol as substrate
CC {ECO:0000269|PubMed:1865764};
CC Vmax=163 umol/min/mg enzyme with 1,2-dioleoyl-sn-glycerol as
CC substrate {ECO:0000269|PubMed:1865764};
CC Vmax=145 umol/min/mg enzyme with 1,3-dioleoyl-sn-glycerol as
CC substrate {ECO:0000269|PubMed:1865764};
CC Vmax=67 umol/min/mg enzyme with phosphatidic acid as substrate
CC {ECO:0000269|PubMed:1865764};
CC Vmax=50 umol/min/mg enzyme with phosphatidylethanolamine as substrate
CC {ECO:0000269|PubMed:1865764};
CC Vmax=4 umol/min/mg enzyme with phosphatidylcholine as substrate
CC {ECO:0000269|PubMed:1865764};
CC pH dependence:
CC Optimum pH is 8-9. {ECO:0000269|PubMed:7074125};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P11150}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P11150}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family.
CC {ECO:0000305}.
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DR EMBL; X17366; CAA35241.1; -; mRNA.
DR EMBL; X17367; CAA35242.1; -; Genomic_DNA.
DR EMBL; M16235; AAA41335.1; -; mRNA.
DR PIR; A27442; A27442.
DR AlphaFoldDB; P07867; -.
DR SMR; P07867; -.
DR IntAct; P07867; 1.
DR STRING; 10116.ENSRNOP00000047403; -.
DR SwissLipids; SLP:000000571; -.
DR ESTHER; ratno-1hlip; Hepatic_Lipase.
DR GlyGen; P07867; 2 sites.
DR PaxDb; P07867; -.
DR PeptideAtlas; P07867; -.
DR UCSC; RGD:3009; rat.
DR RGD; 3009; Lipc.
DR eggNOG; ENOG502QVTG; Eukaryota.
DR InParanoid; P07867; -.
DR PhylomeDB; P07867; -.
DR Reactome; R-RNO-8963889; Assembly of active LPL and LIPC lipase complexes.
DR Reactome; R-RNO-8964026; Chylomicron clearance.
DR PRO; PR:P07867; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005769; C:early endosome; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0034364; C:high-density lipoprotein particle; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IDA:RGD.
DR GO; GO:0005902; C:microvillus; IDA:RGD.
DR GO; GO:0052740; F:1-acyl-2-lysophosphatidylserine acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0047372; F:acylglycerol lipase activity; IDA:RGD.
DR GO; GO:0016746; F:acyltransferase activity; IDA:RGD.
DR GO; GO:0034185; F:apolipoprotein binding; IDA:RGD.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:RGD.
DR GO; GO:0035478; F:chylomicron binding; IDA:BHF-UCL.
DR GO; GO:0043395; F:heparan sulfate proteoglycan binding; IMP:RGD.
DR GO; GO:0008201; F:heparin binding; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0016298; F:lipase activity; ISO:RGD.
DR GO; GO:0008289; F:lipid binding; IDA:RGD.
DR GO; GO:0004465; F:lipoprotein lipase activity; IBA:GO_Central.
DR GO; GO:0030169; F:low-density lipoprotein particle binding; IDA:BHF-UCL.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:RGD.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0052739; F:phosphatidylserine 1-acylhydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008970; F:phospholipase A1 activity; IDA:UniProtKB.
DR GO; GO:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0032870; P:cellular response to hormone stimulus; IEP:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR GO; GO:0030301; P:cholesterol transport; ISO:RGD.
DR GO; GO:0034382; P:chylomicron remnant clearance; IDA:RGD.
DR GO; GO:0034371; P:chylomicron remodeling; IDA:RGD.
DR GO; GO:0007623; P:circadian rhythm; IEP:RGD.
DR GO; GO:0048589; P:developmental growth; IEP:RGD.
DR GO; GO:0006633; P:fatty acid biosynthetic process; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; IDA:RGD.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IDA:RGD.
DR GO; GO:0015012; P:heparan sulfate proteoglycan biosynthetic process; IDA:RGD.
DR GO; GO:0034375; P:high-density lipoprotein particle remodeling; IDA:RGD.
DR GO; GO:0016042; P:lipid catabolic process; IBA:GO_Central.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; IDA:RGD.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; IDA:BHF-UCL.
DR GO; GO:0046461; P:neutral lipid catabolic process; IDA:RGD.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; IDA:RGD.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IDA:RGD.
DR GO; GO:0046337; P:phosphatidylethanolamine metabolic process; IDA:RGD.
DR GO; GO:0006658; P:phosphatidylserine metabolic process; IDA:RGD.
DR GO; GO:0097006; P:regulation of plasma lipoprotein particle levels; IMP:RGD.
DR GO; GO:0010034; P:response to acetate; IEP:RGD.
DR GO; GO:0043200; P:response to amino acid; IEP:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0009743; P:response to carbohydrate; IEP:RGD.
DR GO; GO:0046688; P:response to copper ion; IEP:RGD.
DR GO; GO:0070542; P:response to fatty acid; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR GO; GO:0010035; P:response to inorganic substance; IEP:RGD.
DR GO; GO:0033993; P:response to lipid; IEP:RGD.
DR GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
DR GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0019433; P:triglyceride catabolic process; ISO:RGD.
DR GO; GO:0070328; P:triglyceride homeostasis; ISO:RGD.
DR GO; GO:0006641; P:triglyceride metabolic process; IDA:RGD.
DR GO; GO:0034372; P:very-low-density lipoprotein particle remodeling; IDA:RGD.
DR CDD; cd00707; Pancreat_lipase_like; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013818; Lipase.
DR InterPro; IPR002333; Lipase_hep.
DR InterPro; IPR016272; Lipase_LIPH.
DR InterPro; IPR033906; Lipase_N.
DR InterPro; IPR001024; PLAT/LH2_dom.
DR InterPro; IPR036392; PLAT/LH2_dom_sf.
DR InterPro; IPR000734; TAG_lipase.
DR PANTHER; PTHR11610; PTHR11610; 1.
DR PANTHER; PTHR11610:SF2; PTHR11610:SF2; 1.
DR Pfam; PF00151; Lipase; 1.
DR Pfam; PF01477; PLAT; 1.
DR PIRSF; PIRSF000865; Lipoprotein_lipase_LIPH; 1.
DR PRINTS; PR00824; HEPLIPASE.
DR PRINTS; PR00821; TAGLIPASE.
DR SMART; SM00308; LH2; 1.
DR SUPFAM; SSF49723; SSF49723; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
DR PROSITE; PS50095; PLAT; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; HDL; Heparin-binding; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000250|UniProtKB:P11150"
FT CHAIN 22..494
FT /note="Hepatic triacylglycerol lipase"
FT /id="PRO_0000017771"
FT DOMAIN 353..487
FT /note="PLAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00152"
FT REGION 255..278
FT /note="Essential for determining substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:P11150"
FT ACT_SITE 169
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT ACT_SITE 280
FT /note="Charge relay system"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10037"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 277
FT /note="N -> K (in Ref. 2; AAA41335)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="Q -> H (in Ref. 2; AAA41335)"
FT /evidence="ECO:0000305"
FT CONFLICT 308
FT /note="S -> T (in Ref. 2; AAA41335)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="V -> A (in Ref. 2; AAA41335)"
FT /evidence="ECO:0000305"
FT CONFLICT 369
FT /note="M -> I (in Ref. 2; AAA41335)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="N -> D (in Ref. 2; AAA41335)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="V -> L (in Ref. 2; AAA41335)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 55623 MW; 2A9461B1F80845EA CRC64;
MGNHLQISVS LVLCIFIQSS ACGQGVGTEP FGRNLGATEE RKPLQKPEIR FLLFKDESDR
LGCQLRPQHP ETLQECGFNS SHPLVMIIHG WSVDGLLETW IWKIVGALKS RQSQPVNVGL
VDWISLAYQH YAIAVRNTRV VGQEVAALLL WLEESMKFSR SKVHLIGYSL GAHVSGFAGS
SMGGKRKIGR ITGLDPAGPM FEGTSPNERL SPDDANFVDA IHTFTREHMG LSVGIKQPIA
HYDFYPNGGS FQPGCHFLEL YKHIAEHGLN AITQTINCAH ERSVHLFIDS LQHSNLQNTG
FQCSNMDSFS QGLCLNCKKG RCNSLGYDIR RIGHVKSKTL FLITRAQSPF KVYHYQFKIQ
FINQMEKPME PTFTMTLLGT KEEIKKIPIT LGEGITSNKT YSLLITLNKD IGELIMLKFK
WENSAVWANV WNTVQTIMLW DTEPHYAGLI VKTIWVKAGE TQQRMTFCPD NVDDLQLHPT
QEKVFVKCDL KSKD
