MRP1_BOVIN
ID MRP1_BOVIN Reviewed; 1530 AA.
AC Q8HXQ5;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Multidrug resistance-associated protein 1 {ECO:0000250|UniProtKB:P33527};
DE EC=7.6.2.2 {ECO:0000269|PubMed:12067707};
DE AltName: Full=ATP-binding cassette sub-family C member 1;
DE AltName: Full=Glutathione-S-conjugate-translocating ATPase ABCC1 {ECO:0000250|UniProtKB:O35379};
DE EC=7.6.2.3 {ECO:0000250|UniProtKB:O35379};
DE AltName: Full=Leukotriene C(4) transporter;
DE Short=LTC4 transporter;
GN Name=ABCC1 {ECO:0000250|UniProtKB:P33527}; Synonyms=MRP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
RC TISSUE=Mammary gland;
RX PubMed=12067707; DOI=10.1016/s0014-5793(02)02816-8;
RA Taguchi Y., Saeki K., Komano T.;
RT "Functional analysis of MRP1 cloned from bovine.";
RL FEBS Lett. 521:211-213(2002).
CC -!- FUNCTION: Mediates export of organic anions and drugs from the
CC cytoplasm. Mediates ATP-dependent transport of glutathione and
CC glutathione conjugates, leukotriene C4, estradiol-17-beta-o-
CC glucuronide, methotrexate, antiviral drugs and other xenobiotics.
CC Confers resistance to anticancer drugs by decreasing accumulation of
CC drug in cells, and by mediating ATP- and GSH-dependent drug export
CC (PubMed:12067707). Hydrolyzes ATP with low efficiency. Catalyzes the
CC export of sphingosine 1-phosphate from mast cells independently of
CC their degranulation (By similarity). Participates in inflammatory
CC response by allowing export of leukotriene C4 from leukotriene C4-
CC synthezing cells (By similarity). {ECO:0000250|UniProtKB:O35379,
CC ECO:0000250|UniProtKB:P33527, ECO:0000269|PubMed:12067707}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC Evidence={ECO:0000269|PubMed:12067707};
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:O35379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122;
CC Evidence={ECO:0000250|UniProtKB:O35379};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + sphing-4-enine 1-phosphate(in) = ADP + H(+) +
CC phosphate + sphing-4-enine 1-phosphate(out); Xref=Rhea:RHEA:38951,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:60119, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38952;
CC Evidence={ECO:0000250|UniProtKB:P33527};
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:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964;
CC Evidence={ECO:0000250|UniProtKB:P33527};
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:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60129;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + daunorubicin(in) + H2O = ADP + daunorubicin(out) + H(+)
CC + phosphate; Xref=Rhea:RHEA:33147, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64677, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33148;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + vincristine(in) = ADP + H(+) + phosphate +
CC vincristine(out); Xref=Rhea:RHEA:60160, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:143658, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60161;
CC Evidence={ECO:0000250|UniProtKB:P33527};
CC -!- ACTIVITY REGULATION: MK 571 inhibits sphingosine 1-phosphate and
CC leukotriene C4 export. {ECO:0000250|UniProtKB:P33527}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, spleen, lung, kidney, skeletal
CC muscle, mammary gland and weaker in brain and liver.
CC {ECO:0000269|PubMed:12067707}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
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DR EMBL; AB082124; BAC15550.1; -; mRNA.
DR RefSeq; NP_776648.1; NM_174223.1.
DR PDB; 5UJ9; EM; 3.49 A; A=205-1530.
DR PDB; 5UJA; EM; 3.34 A; A=205-1530.
DR PDB; 6BHU; EM; 3.14 A; A=1-1530.
DR PDB; 6UY0; EM; 3.23 A; A=1-1530.
DR PDBsum; 5UJ9; -.
DR PDBsum; 5UJA; -.
DR PDBsum; 6BHU; -.
DR PDBsum; 6UY0; -.
DR AlphaFoldDB; Q8HXQ5; -.
DR SMR; Q8HXQ5; -.
DR STRING; 9913.ENSBTAP00000028094; -.
DR PaxDb; Q8HXQ5; -.
DR PRIDE; Q8HXQ5; -.
DR Ensembl; ENSBTAT00000028094; ENSBTAP00000028094; ENSBTAG00000021090.
DR GeneID; 281588; -.
DR KEGG; bta:281588; -.
DR CTD; 4363; -.
DR VEuPathDB; HostDB:ENSBTAG00000021090; -.
DR VGNC; VGNC:25468; ABCC1.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000160271; -.
DR InParanoid; Q8HXQ5; -.
DR OMA; IRYDFTP; -.
DR OrthoDB; 138195at2759; -.
DR BRENDA; 7.6.2.2; 908.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000021090; Expressed in corpus epididymis and 109 other tissues.
DR ExpressionAtlas; Q8HXQ5; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0015431; F:ABC-type glutathione S-conjugate transporter activity; ISS:UniProtKB.
DR GO; GO:0140359; F:ABC-type transporter activity; ISS:UniProtKB.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034040; F:ATPase-coupled lipid transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046943; F:carboxylic acid transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0034634; F:glutathione transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0140115; P:export across plasma membrane; IEA:Ensembl.
DR GO; GO:0034775; P:glutathione transmembrane transport; IBA:GO_Central.
DR GO; GO:0071716; P:leukotriene transport; ISS:UniProtKB.
DR GO; GO:0045332; P:phospholipid translocation; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0099039; P:sphingolipid translocation; IEA:Ensembl.
DR GO; GO:0070633; P:transepithelial transport; IEA:Ensembl.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0042908; P:xenobiotic transport; IBA:GO_Central.
DR GO; GO:1990962; P:xenobiotic transport across blood-brain barrier; IEA:Ensembl.
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 3D-structure; ATP-binding; Cell membrane; Glycoprotein; Hydrolase;
KW Lipid transport; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1530
FT /note="Multidrug resistance-associated protein 1"
FT /id="PRO_0000093349"
FT TOPO_DOM 1..33
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 34..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 55..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 75..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 96..100
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 101..121
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 122..133
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 134..154
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 155..172
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 173..193
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 194..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 317..337
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 338..363
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 364..384
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 385..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 441..461
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 462..464
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 465..485
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 486..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 548..568
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 569..590
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 591..611
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 612..966
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 967..987
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 988..1024
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1025..1045
FT /note="Helical; Name=13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1046..1088
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1089..1109
FT /note="Helical; Name=14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1110
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1111..1131
FT /note="Helical; Name=15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1132..1202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 1203..1223
FT /note="Helical; Name=16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1224..1225
FT /note="Extracellular"
FT /evidence="ECO:0000250"
FT TRANSMEM 1226..1246
FT /note="Helical; Name=17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1247..1530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT DOMAIN 325..608
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 644..868
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 974..1255
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1292..1526
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 912..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..927
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 678..685
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1326..1333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MOD_RES 277
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O35379"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35379"
FT MOD_RES 503
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:O35379"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33527"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P33527"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1005
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6UY0"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:6UY0"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 246..249
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 316..319
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 328..354
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 361..407
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 412..417
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 420..440
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 443..461
FT /evidence="ECO:0007829|PDB:6BHU"
FT TURN 464..466
FT /evidence="ECO:0007829|PDB:6UY0"
FT HELIX 467..509
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 512..518
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 521..554
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 556..570
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 580..589
FT /evidence="ECO:0007829|PDB:6BHU"
FT TURN 590..592
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 593..597
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 599..620
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 627..629
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 642..657
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 663..671
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 673..679
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 684..690
FT /evidence="ECO:0007829|PDB:6BHU"
FT TURN 691..693
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 695..706
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 722..727
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 734..743
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 747..752
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 753..755
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 763..768
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 770..784
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 787..792
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 795..798
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 800..809
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 812..816
FT /evidence="ECO:0007829|PDB:5UJA"
FT STRAND 818..825
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 829..831
FT /evidence="ECO:0007829|PDB:6UY0"
FT HELIX 832..834
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 835..842
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 845..848
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 852..858
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 861..865
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 959..969
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 971..999
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1005..1007
FT /evidence="ECO:0007829|PDB:5UJA"
FT HELIX 1008..1057
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1060..1065
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1068..1109
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1112..1114
FT /evidence="ECO:0007829|PDB:6UY0"
FT TURN 1115..1117
FT /evidence="ECO:0007829|PDB:6UY0"
FT HELIX 1118..1146
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1148..1159
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1161..1167
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1170..1219
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1221..1224
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1226..1256
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1258..1263
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1264..1266
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1267..1269
FT /evidence="ECO:0007829|PDB:6UY0"
FT STRAND 1278..1280
FT /evidence="ECO:0007829|PDB:6UY0"
FT TURN 1286..1288
FT /evidence="ECO:0007829|PDB:5UJA"
FT STRAND 1292..1298
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1301..1305
FT /evidence="ECO:0007829|PDB:6UY0"
FT STRAND 1308..1316
FT /evidence="ECO:0007829|PDB:6UY0"
FT STRAND 1322..1326
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1330..1332
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1333..1339
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1346..1354
FT /evidence="ECO:0007829|PDB:6BHU"
FT TURN 1357..1359
FT /evidence="ECO:0007829|PDB:5UJA"
FT HELIX 1362..1366
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1368..1372
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1380..1382
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1383..1387
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1395..1404
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1408..1413
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1414..1418
FT /evidence="ECO:0007829|PDB:6BHU"
FT TURN 1424..1427
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1431..1445
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1448..1454
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1457..1459
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1461..1474
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1475..1483
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1487..1490
FT /evidence="ECO:0007829|PDB:6BHU"
FT STRAND 1493..1504
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1510..1516
FT /evidence="ECO:0007829|PDB:6BHU"
FT HELIX 1519..1527
FT /evidence="ECO:0007829|PDB:6BHU"
SQ SEQUENCE 1530 AA; 171666 MW; AAE4F92ED7832703 CRC64;
MALRDFCSVD GSDLFWEWNV TWNTSNPDFT KCFQNTVLVW VPCSYLWVCF PFYFLYLSHH
DRGYIQMTHL NKAKTALGFL LWIVCWADLF YSFWERSMGK LLAPVFLVSP TLLGITMLLA
TFLIQIERRR GVQSSGIMLT FWLIALLCAL AILRSKIMTA LKEDARVDVF RDVTFYIYFS
LVLIQLVLSC FSDRSPLFSE TINDPNPCPE SSASFLSRIT FWWITGMMVQ GYRQPLESTD
LWSLNKEDTS EQVVPVLVKN WKKECAKSRK QPVKIVYSSK DPAKPKGSSK VDVNEEAEAL
IVKCPQKERD PSLFKVLYKT FGPYFLMSFL FKAVHDLMMF AGPEILKLLI NFVNDKKAPE
WQGYFYTALL FISACLQTLV LHQYFHICFV SGMRIKTAVI GAVYRKALVI TNAARKSSTV
GEIVNLMSVD AQRFMDLATY INMIWSAPLQ VILALYLLWL NLGPSVLAGV AVMVLMVPLN
AVMAMKTKTY QVAHMKSKDN RIKLMNEILN GIKVLKLYAW ELAFKDKVLA IRQEELKVLK
KSAYLAAVGT FTWVCTPFLV ALSTFAVYVT VDENNILDAQ KAFVSLALFN ILRFPLNILP
MVISSIVQAS VSLKRLRVFL SHEDLDPDSI QRRPIKDAGA TNSITVKNAT FTWARNDPPT
LHGITFSVPE GSLVAVVGQV GCGKSSLLSA LLAEMDKVEG HVTVKGSVAY VPQQAWIQNI
SLRENILFGR QLQERYYKAV VEACALLPDL EILPSGDRTE IGEKGVNLSG GQKQRVSLAR
AVYCDSDVYL LDDPLSAVDA HVGKHIFENV IGPKGLLKNK TRLLVTHAIS YLPQMDVIIV
MSGGKISEMG SYQELLARDG AFAEFLRTYA SAEQEQGQPE DGLAGVGGPG KEVKQMENGM
LVTDTAGKQM QRQLSSSSSY SRDVSQHHTS TAELRKPGPT EETWKLVEAD KAQTGQVKLS
VYWDYMKAIG LFISFLSIFL FLCNHVASLV SNYWLSLWTD DPIVNGTQEH TQVRLSVYGA
LGISQGITVF GYSMAVSIGG IFASRRLHLD LLHNVLRSPI SFFERTPSGN LVNRFSKELD
TVDSMIPQVI KMFMGSLFNV IGACIIILLA TPMAAVIIPP LGLIYFFVQR FYVASSRQLK
RLESVSRSPV YSHFNETLLG VSVIRAFEEQ ERFIRQSDLK VDENQKAYYP SIVANRWLAV
RLECVGNCIV LFASLFAVIS RHSLSAGLVG LSVSYSLQVT TYLNWLVRMS SEMETNIVAV
ERLKEYSETE KEAPWQIQDM APPKDWPQVG RVEFRDYGLR YREDLDLVLK HINVTIDGGE
KVGIVGRTGA GKSSLTLGLF RIKESAEGEI IIDDINIAKI GLHDLRFKIT IIPQDPVLFS
GSLRMNLDPF SQYSDEEVWT SLELAHLKGF VSALPDKLNH ECAEGGENLS VGQRQLVCLA
RALLRKTKIL VLDEATAAVD LETDDLIQST IRTQFDDCTV LTIAHRLNTI MDYTRVIVLD
KGEIQEWGSP SDLLQQRGLF YSMAKDSGLV
