MRP3_RAT
ID MRP3_RAT Reviewed; 1522 AA.
AC O88563; O88270;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=ATP-binding cassette sub-family C member 3;
DE EC=7.6.2.- {ECO:0000269|PubMed:10644759};
DE EC=7.6.2.2 {ECO:0000250|UniProtKB:O15438};
DE EC=7.6.2.3 {ECO:0000250|UniProtKB:O15438};
DE AltName: Full=Canalicular multispecific organic anion transporter 2;
DE AltName: Full=MRP-like protein 2 {ECO:0000303|PubMed:9614210};
DE Short=MLP-2 {ECO:0000303|PubMed:9614210};
DE AltName: Full=Multidrug resistance-associated protein 3;
GN Name=Abcc3; Synonyms=Cmoat2, Mlp2, Mrp3;
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], TISSUE SPECIFICITY, AND INDUCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Colon;
RX PubMed=9614210;
RA Hirohashi T., Suzuki H., Ito K., Ogawa K., Kume K., Shimizu T.,
RA Sugiyama Y.;
RT "Hepatic expression of multidrug resistance-associated protein-like
RT proteins maintained in eisai hyperbilirubinemic rats.";
RL Mol. Pharmacol. 53:1068-1075(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=10362653; DOI=10.1152/ajpgi.1999.276.6.g1493;
RA Ortiz D.F., Li S., Iyer R., Zhang X., Novikoff P., Arias I.M.;
RT "MRP3, a new ATP-binding cassette protein localized to the canalicular
RT domain of the hepatocyte.";
RL Am. J. Physiol. 276:G1493-G1500(1999).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=10644759; DOI=10.1074/jbc.275.4.2905;
RA Hirohashi T., Suzuki H., Takikawa H., Sugiyama Y.;
RT "ATP-dependent transport of bile salts by rat multidrug resistance-
RT associated protein 3 (Mrp3).";
RL J. Biol. Chem. 275:2905-2910(2000).
RN [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=11897632; DOI=10.1152/ajpgi.00318.2001;
RA Rost D., Mahner S., Sugiyama Y., Stremmel W.;
RT "Expression and localization of the multidrug resistance-associated protein
RT 3 in rat small and large intestine.";
RL Am. J. Physiol. 282:G720-G726(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-902 AND SER-905, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: ATP-dependent transporter of the ATP-binding cassette (ABC)
CC family that bind and hydrolyze ATP to enable active transport of
CC various substrates including many drugs, toxicants and endogenous
CC compound across cell membranes. Transports glucuronide conjugates such
CC as bilirubin diglucuronide, estradiol-17-beta-o-glucuronide and GSH
CC conjugates such as leukotriene C4 (LTC4) (By similarity). Transports
CC also various bile salts (taurocholate, glycocholate,
CC taurochenodeoxycholate-3-sulfate, taurolithocholate- 3-sulfate). Does
CC not contribute substantially to bile salt physiology but provides an
CC alternative route for the export of bile acids and glucuronides from
CC cholestatic hepatocytes (By similarity). {ECO:0000250|UniProtKB:B2RX12,
CC ECO:0000250|UniProtKB:O15438}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-
CC substituted glutathione(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779,
CC ChEBI:CHEBI:456216; EC=7.6.2.3;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate +
CC taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:10644759};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053;
CC Evidence={ECO:0000305|PubMed:10644759};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+)
CC + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:10644759};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057;
CC Evidence={ECO:0000305|PubMed:10644759};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H(+) +
CC phosphate + taurolithocholate 3-sulfate(out); Xref=Rhea:RHEA:50084,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58301, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:10644759};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=17beta-estradiol 17-O-(beta-D-glucuronate)(in) + ATP + H2O =
CC 17beta-estradiol 17-O-(beta-D-glucuronate)(out) + ADP + H(+) +
CC phosphate; Xref=Rhea:RHEA:60128, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82961, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:10644759};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000305|PubMed:10644759};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + dehydroepiandrosterone 3-sulfate(in) + H2O = ADP +
CC dehydroepiandrosterone 3-sulfate(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:61364, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57905,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61365;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene
CC C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57973, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + bilirubin-glucuronoside(in) + H2O = ADP + bilirubin-
CC glucuronoside(out) + H(+) + phosphate; Xref=Rhea:RHEA:66180,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57767, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66181;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + bilirubin-bisglucuronoside(in) + H2O = ADP + bilirubin-
CC bisglucuronoside(out) + H(+) + phosphate; Xref=Rhea:RHEA:66192,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58471, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66193;
CC Evidence={ECO:0000250|UniProtKB:O15438};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + taurochenodeoxycholate 3-sulfate(in) = ADP + H(+)
CC + phosphate + taurochenodeoxycholate 3-sulfate(out);
CC Xref=Rhea:RHEA:66176, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:166912,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:10644759};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66177;
CC Evidence={ECO:0000305|PubMed:10644759};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.36 uM for ATP (determined by measuring estradiol-17-beta-o-
CC glucuronide transport) {ECO:0000269|PubMed:10644759};
CC KM=3.06 uM for taurolithocholate sulfate
CC {ECO:0000269|PubMed:10644759};
CC KM=15.9 uM for taurocholate {ECO:0000269|PubMed:10644759};
CC Vmax=161.9 pmol/min/mg enzyme for taurolithocholate-3-sulfate
CC {ECO:0000269|PubMed:10644759};
CC Vmax=50.1 pmol/min/mg enzyme for taurocholate transport
CC {ECO:0000269|PubMed:10644759};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:11897632}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, ileum, colon and liver. Higher
CC in liver of Eisai hyperbilirubinemic rats.
CC {ECO:0000269|PubMed:9614210}.
CC -!- INDUCTION: Strongly up-regulated under conditions of cholestasis.
CC {ECO:0000269|PubMed:9614210}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA28955.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF072816; AAC25416.1; -; mRNA.
DR EMBL; AB010467; BAA28955.1; ALT_FRAME; mRNA.
DR RefSeq; NP_542148.1; NM_080581.1.
DR AlphaFoldDB; O88563; -.
DR SMR; O88563; -.
DR BioGRID; 250828; 1.
DR STRING; 10116.ENSRNOP00000003977; -.
DR BindingDB; O88563; -.
DR ChEMBL; CHEMBL2073682; -.
DR GlyGen; O88563; 3 sites.
DR iPTMnet; O88563; -.
DR PhosphoSitePlus; O88563; -.
DR PRIDE; O88563; -.
DR GeneID; 140668; -.
DR KEGG; rno:140668; -.
DR CTD; 8714; -.
DR RGD; 71101; Abcc3.
DR eggNOG; KOG0054; Eukaryota.
DR InParanoid; O88563; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; O88563; -.
DR Reactome; R-RNO-159418; Recycling of bile acids and salts.
DR Reactome; R-RNO-382556; ABC-family proteins mediated transport.
DR Reactome; R-RNO-9749641; Aspirin ADME.
DR Reactome; R-RNO-9753281; Paracetamol ADME.
DR PRO; PR:O88563; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015432; F:ABC-type bile acid transporter activity; IDA:UniProtKB.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; ISS:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015164; F:glucuronoside transmembrane transporter activity; ISO:RGD.
DR GO; GO:0071714; F:icosanoid transmembrane transporter activity; ISO:RGD.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:RGD.
DR GO; GO:0098656; P:anion transmembrane transport; IDA:RGD.
DR GO; GO:0015721; P:bile acid and bile salt transport; IMP:UniProtKB.
DR GO; GO:0015722; P:canalicular bile acid transport; IDA:MGI.
DR GO; GO:0071716; P:leukotriene transport; ISS:UniProtKB.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IEP:RGD.
DR GO; GO:0055085; P:transmembrane transport; IMP:RGD.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; ISO:RGD.
DR GO; GO:0042908; P:xenobiotic transport; ISO:RGD.
DR Gene3D; 1.20.1560.10; -; 2.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR005292; Multidrug-R_assoc.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR TIGRFAMs; TIGR00957; MRP_assoc_pro; 1.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cell membrane; Glycoprotein; Lipid transport; Membrane;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1522
FT /note="ATP-binding cassette sub-family C member 3"
FT /id="PRO_0000093361"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 33..53
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 54..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 74..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 95..99
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 100..120
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 121..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 133..153
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 154..171
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 172..192
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 193..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 302..322
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 323..347
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 348..368
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 369..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 425..445
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 446..448
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 449..469
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 470..531
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 532..552
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 553..574
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 575..595
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 596..958
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 959..979
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 980..1016
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1017..1037
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1038..1080
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1081..1101
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1102
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1103..1123
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1124..1194
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1195..1215
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1216..1217
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1218..1238
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1239..1522
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 310..592
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 625..849
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 966..1247
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1286..1518
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 659..666
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1318..1325
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 902
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 905
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1001
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1002
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 645
FT /note="I -> L (in Ref. 1; BAA28955)"
FT /evidence="ECO:0000305"
FT CONFLICT 1075
FT /note="H -> D (in Ref. 1; BAA28955)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1522 AA; 168978 MW; 740E31E0C4C64297 CRC64;
MDRLCGSGEL GSKFWDSNLT VYTNTPDLTP CFQNSLLAWV PCIYLWAALP CYLFYLRHHR
LGYIVLSCLS RLKTALGVLL WCISWVDLFY SFHGLVHGSS PAPVFFITPL LVGITMLLAT
LLIQYERLRG VRSSGVLIIF WLLCVICAII PFRSKILLAL AEGKILDPFR FTTFYIYFAL
VLCAFILSCF QEKPPLFSPE NLDTNPCPEA SAGFFSRLSF WWFTKLAILG YRRPLEDSDL
WSLSEEDCSH KVVQRLLEAW QKQQTQASGP QTAALEPKIA GEDEVLLKAR PKTKKPSFLR
ALVRTFTSSL LMGACFKLIQ DLSPSSTHSC SASSSGLFRP HGPYWWGFLL AGLMFVSSTM
QTLILHQHYH CIFVMALRIR TAIIGVIYRK ALTITNSVKR EYTVGEMVNL MSVDAQRFMD
VSPFINLLWS APLQVILAIY FLWQILGPSA LAGVAVIVLL IPLNGAVSMK MKTYQVQQMK
FKDSRIKLMS EILNGIKVLK LYAWEPTFLE QVEGIRQGEL QLLRKGAYLQ AISTFIWVCT
PFMVTLITLG VYVCVDKNNV LDAEKAFVSL SLFNILKIPL NLLPQLISGM TQTSVSLKRI
QDFLNQDELD PQCVERKTIS PGRAITIHNG TFSWSKDLPP TLHSINIQIP KGALVAVVGP
VGCGKSSLVS ALLGEMEKLE GAVSVKGSVA YVPQQAWIQN CTLQENVLFG QPMNPKRYQQ
ALETCALLAD LDVLPGGDQT EIGEKGINLS GGQRQRVSLA RAVYSDANIF LLDDPLSAVD
SHVAKHIFDQ VIGPEGVLAG KTRVLVTHGI SFLPQTDFII VLADGQITEM GHYSELLQHD
GSFANFLRNY APDENQEANE GVLQHANEEV LLLEDTLSTH TDLTDTEPAI YEVRKQFMRE
MSSLSSEGEG QNRPVLKRYT SSLEKEVPAT QTKETGALIK EEIAETGNVK LSVYWDYAKS
VGLCTTLFIC LLYAGQNAVA IGANVWLSAW TNDVEEHGQQ NNTSVRLGVY ATLGILQGLL
VMLSAFTMVV GAIQAARLLH TALLHNQIRA PQSFFDTTPS GRILNRFSKD IYVIHEVLAP
TILMLFNSFY TSISTIVVIV ASTPLFCVVV LPLAVFYGFV QRFYVATSRQ LKRLESVSRS
PIFSHFSETV TGTSVIRAYG RVQDFKVLSD AKVDSNQKTT YPYIASNRWL GVHVEFVGNC
VVLFSALFAV IGRNSLNPGL VGLSVSYALQ VTLSLNWMIR TLSDLESNII AVERVKEYSK
TETEAPWVLE SNRAPEGWPR SGVVEFRNYS VRYRPGLELV LKNLTLHVQG GEKVGIVGRT
GAGKSSMTLC LFRILEAAEG EIFIDGLNVA HIGLHDLRSQ LTIIPQDPIL FSGTLRMNLD
PFGRYSDEDI WRTLELSHLS AFVSSQPTGL DFQCSEGGDN LSVGQRQLVC LARALLRKSR
VLVLDEATAA IDLETDDLIQ GTIRTQFEDC TVLTIAHRLN TIMDYNRVLV LDKGVVAEFD
SPVNLIAAGG IFYGMAKDAG LA
