CEL_RAT
ID CEL_RAT Reviewed; 612 AA.
AC P07882; P14722;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Bile salt-activated lipase;
DE Short=BAL;
DE EC=3.1.1.13 {ECO:0000250|UniProtKB:P19835};
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:P19835};
DE EC=3.1.1.6 {ECO:0000250|UniProtKB:P19835};
DE AltName: Full=Bile salt-stimulated lipase;
DE Short=BSSL;
DE AltName: Full=Carboxyl ester lipase;
DE AltName: Full=Cholesterol esterase;
DE AltName: Full=Pancreatic lysophospholipase;
DE AltName: Full=Sterol esterase;
DE Flags: Precursor;
GN Name=Cel;
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 [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Pancreas;
RX PubMed=2688744; DOI=10.1016/0005-2760(89)90201-4;
RA Kissel J.A., Fontaine R.N., Turck C.W., Brockman H.L., Hui D.Y.;
RT "Molecular cloning and expression of cDNA for rat pancreatic cholesterol
RT esterase.";
RL Biochim. Biophys. Acta 1006:227-237(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3593682; DOI=10.1021/bi00380a020;
RA Han J.H., Stratowa C., Rutter W.J.;
RT "Isolation of full-length putative rat lysophospholipase cDNA using
RT improved methods for mRNA isolation and cDNA cloning.";
RL Biochemistry 26:1617-1625(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2069957; DOI=10.1021/bi00242a028;
RA Fontaine R.N., Carter C.P., Hui D.Y.;
RT "Structure of the rat pancreatic cholesterol esterase gene.";
RL Biochemistry 30:7008-7014(1991).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE SER-214, AND MUTAGENESIS OF
RP SER-214.
RX PubMed=2211595; DOI=10.1016/s0021-9258(17)44832-0;
RA Dipersio L.P., Fontaine R.N., Hui D.Y.;
RT "Identification of the active site serine in pancreatic cholesterol
RT esterase by chemical modification and site-specific mutagenesis.";
RL J. Biol. Chem. 265:16801-16806(1990).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE HIS-455, AND MUTAGENESIS OF
RP HIS-440 AND HIS-455.
RX PubMed=1999399; DOI=10.1016/s0021-9258(20)64279-x;
RA Dipersio L.P., Fontaine R.N., Hui D.Y.;
RT "Site-specific mutagenesis of an essential histidine residue in pancreatic
RT cholesterol esterase.";
RL J. Biol. Chem. 266:4033-4036(1991).
CC -!- FUNCTION: Catalyzes the hydrolysis of a wide range of substrates
CC including cholesteryl esters, phospholipids, lysophospholipids, di- and
CC tri-acylglycerols, and fatty acid esters of hydroxy fatty acids (FAHFA)
CC (PubMed:2211595, PubMed:1999399). Preferentially hydrolyzes FAHFAs with
CC the ester bond further away from the carboxylate. Unsaturated FAHFAs
CC are hydrolyzed more quickly than saturated FAHFAs (By similarity). Has
CC an essential role in the complete digestion of dietary lipids and their
CC intestinal absorption, along with the absorption of fat-soluble
CC vitamins (By similarity). {ECO:0000250|UniProtKB:P19835,
CC ECO:0000250|UniProtKB:Q64285, ECO:0000269|PubMed:1999399,
CC ECO:0000269|PubMed:2211595}.
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:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:P19835};
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:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38576;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-trioctanoylglycerol + H2O = dioctanoylglycerol + H(+) +
CC octanoate; Xref=Rhea:RHEA:47864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:76978,
CC ChEBI:CHEBI:88066; Evidence={ECO:0000250|UniProtKB:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47865;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a sterol ester + H2O = a fatty acid + a sterol + H(+);
CC Xref=Rhea:RHEA:10100, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15889, ChEBI:CHEBI:28868, ChEBI:CHEBI:35915; EC=3.1.1.13;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10101;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cholesteryl (9Z-octadecenoate) + H2O = (9Z)-octadecenoate +
CC cholesterol + H(+); Xref=Rhea:RHEA:33875, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:46898; Evidence={ECO:0000269|PubMed:1999399,
CC ECO:0000269|PubMed:2211595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33876;
CC Evidence={ECO:0000305|PubMed:1999399};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+);
CC Xref=Rhea:RHEA:12957, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:47622; EC=3.1.1.6;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12958;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate +
CC H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477;
CC Evidence={ECO:0000269|PubMed:1999399, ECO:0000269|PubMed:2211595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47349;
CC Evidence={ECO:0000305|PubMed:1999399};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-hexadecanoyloxy-octadecanoate + H2O = 9-hydroxy-
CC octadecanoate + H(+) + hexadecanoate; Xref=Rhea:RHEA:52052,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:83670, ChEBI:CHEBI:136286;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52053;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC octadecenoate + 9-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52048,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:136282, ChEBI:CHEBI:136286;
CC Evidence={ECO:0000250|UniProtKB:P19835};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52049;
CC Evidence={ECO:0000250|UniProtKB:P19835};
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:2211595};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:2211595};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-hexadecanoyloxy-octadecanoate + H2O = 12-
CC hydroxyoctadecanoate + H(+) + hexadecanoate; Xref=Rhea:RHEA:52056,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:83677, ChEBI:CHEBI:84201;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52057;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC octadecenoate + 12-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:52060,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:84201, ChEBI:CHEBI:136302;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52061;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-(9Z-octadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC octadecenoate + 13-hydroxy-octadecanoate + H(+);
CC Xref=Rhea:RHEA:52064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:136303, ChEBI:CHEBI:136304;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52065;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 9-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52068,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:136286, ChEBI:CHEBI:136309;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52069;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 12-hydroxyoctadecanoate + H(+); Xref=Rhea:RHEA:52072,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:84201, ChEBI:CHEBI:136312;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52073;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 13-hydroxy-octadecanoate + H(+);
CC Xref=Rhea:RHEA:52076, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32372, ChEBI:CHEBI:136304, ChEBI:CHEBI:136315;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52077;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=12-octadecanoyloxy-octadecanoate + H2O = 12-
CC hydroxyoctadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52080,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:84201, ChEBI:CHEBI:136330;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52081;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=13-octadecanoyloxy-octadecanoate + H2O = 13-hydroxy-
CC octadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52084,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:136304, ChEBI:CHEBI:136335;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52085;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-(9Z-hexadecenoyloxy)-octadecanoate + H2O = (9Z)-
CC hexadecenoate + 5-hydroxy-octadecanoate + H(+); Xref=Rhea:RHEA:52092,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:136369, ChEBI:CHEBI:136370;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52093;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=9-octadecanoyloxy-octadecanoate + H2O = 9-hydroxy-
CC octadecanoate + H(+) + octadecanoate; Xref=Rhea:RHEA:52096,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629,
CC ChEBI:CHEBI:136286, ChEBI:CHEBI:136373;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52097;
CC Evidence={ECO:0000250|UniProtKB:Q64285};
CC -!- ACTIVITY REGULATION: Activated by bile salts such as sodium
CC taurocholate. {ECO:0000250|UniProtKB:P19835}.
CC -!- SUBUNIT: Interacts with CLC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P19835}.
CC -!- TISSUE SPECIFICITY: Synthesized primarily in the pancreas and then
CC transported to the intestine.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; X16054; CAA34189.1; -; mRNA.
DR EMBL; M15893; AAA41540.1; -; mRNA.
DR EMBL; M69157; AAB46376.1; -; Genomic_DNA.
DR PIR; A34967; A34967.
DR AlphaFoldDB; P07882; -.
DR SMR; P07882; -.
DR STRING; 10116.ENSRNOP00000014572; -.
DR ESTHER; ratno-balip; Cholesterol_esterase.
DR MEROPS; S09.985; -.
DR GlyGen; P07882; 1 site.
DR PaxDb; P07882; -.
DR UCSC; RGD:2331; rat.
DR RGD; 2331; Cel.
DR eggNOG; KOG1516; Eukaryota.
DR InParanoid; P07882; -.
DR PhylomeDB; P07882; -.
DR Reactome; R-RNO-192456; Digestion of dietary lipid.
DR PRO; PR:P07882; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005794; C:Golgi apparatus; IDA:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IDA:RGD.
DR GO; GO:0042588; C:zymogen granule; IDA:RGD.
DR GO; GO:0008126; F:acetylesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IDA:RGD.
DR GO; GO:0043208; F:glycosphingolipid binding; IDA:RGD.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0050253; F:retinyl-palmitate esterase activity; IDA:RGD.
DR GO; GO:0004771; F:sterol esterase activity; IDA:RGD.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:RGD.
DR GO; GO:0046514; P:ceramide catabolic process; ISO:RGD.
DR GO; GO:0006707; P:cholesterol catabolic process; ISO:RGD.
DR GO; GO:0030157; P:pancreatic juice secretion; ISO:RGD.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR033560; BAL.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019826; Carboxylesterase_B_AS.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR PANTHER; PTHR43903:SF1; PTHR43903:SF1; 1.
DR Pfam; PF00135; COesterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid metabolism; Reference proteome; Repeat; Secreted; Serine esterase;
KW Signal.
FT SIGNAL 1..20
FT CHAIN 21..612
FT /note="Bile salt-activated lipase"
FT /id="PRO_0000008633"
FT REPEAT 556..566
FT /note="1"
FT REPEAT 567..577
FT /note="2"
FT REPEAT 578..588
FT /note="3"
FT REPEAT 589..599
FT /note="4"
FT REGION 553..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..599
FT /note="4 X 11 AA tandem repeats, O-glycosylated region"
FT COMPBIAS 578..602
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 214
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT ACT_SITE 340
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 455
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 84..100
FT /evidence="ECO:0000250"
FT DISULFID 266..277
FT /evidence="ECO:0000250"
FT MUTAGEN 214
FT /note="S->T,A: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:2211595"
FT MUTAGEN 440
FT /note="H->Q: No effect on activity."
FT /evidence="ECO:0000269|PubMed:1999399"
FT MUTAGEN 455
FT /note="H->Q,R,A,S,D: Abolishes activity."
FT /evidence="ECO:0000269|PubMed:1999399"
FT CONFLICT 26
FT /note="V -> L (in Ref. 2; AAA41540)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="G -> A (in Ref. 2; AAA41540)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="A -> G (in Ref. 2; AAA41540)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="S -> I (in Ref. 2; AAA41540)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="M -> T (in Ref. 3; AAB46376)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="T -> M (in Ref. 2; AAA41540 and 3; AAB46376)"
FT /evidence="ECO:0000305"
FT CONFLICT 576..577
FT /note="GG -> VV (in Ref. 3; AAB46376)"
FT /evidence="ECO:0000305"
FT CONFLICT 608..609
FT /note="GP -> VA (in Ref. 3; AAB46376)"
FT /evidence="ECO:0000305"
FT CONFLICT 611
FT /note="G -> A (in Ref. 3; AAB46376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 67040 MW; 1569CE4EA71ED02A CRC64;
MGRLEVLFLG LTCCLAAACA AKLGAVYTEG GFVEGVNKKL SLLGGDSVDI FKGIPFATAK
TLENPQRHPG WQGTLKATDF KKRCLQATIT QDDTYGQEDC LYLNIWVPQG RKQVSHDLPV
MVWIYGGAFL MGSGQGANFL KNYLYDGEEI ATRGNVIVVT FNYRVGPLGF LSTGDANLPG
NFGLRDQHMA IAWVKRNIAA FGGDPDNITI FGESAGAASV SLQTLSPYNK GLIRRAISQS
GVALSPWAIQ ENPLFWAKTI AKKVGCPTED TAKMAGCLKI TDPRALTLAY RLPLKSQEYP
IVHYLAFIPV VDGDFIPDDP INLYDNAADI DYLAGINDMD GHLFATVDVP AIDKAKQDVT
EEDFYRLVSG HTVAKGLKGT QATFDIYTES WAQDPSQENM KKTVVAFETD ILFLIPTEMA
LAQHRAHAKS AKTYSYLFSH PSRMPIYPKW MGADHADDLQ YVFGKPFATP LGYRAQDRTV
SKAMIAYWTN FAKSGDPNMG NSPVPTHWYP YTTENGNYLD INKKITSTSM KEHLREKFLK
FWAVTFEMLP TVVGDHTPPE DDSEAAPVPP TDDSQGGPVP PTDDSQTTPV PPTDNSQAGD
SVEAQMPGPI GF
