CERU_RAT
ID CERU_RAT Reviewed; 1059 AA.
AC P13635; Q64719;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ceruloplasmin;
DE EC=1.16.3.1;
DE AltName: Full=Ferroxidase;
DE Flags: Precursor;
GN Name=Cp;
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, and Lung;
RX PubMed=2332446; DOI=10.1016/s0021-9258(19)39171-9;
RA Fleming R.E., Gitlin J.D.;
RT "Primary structure of rat ceruloplasmin and analysis of tissue-specific
RT gene expression during development.";
RL J. Biol. Chem. 265:7701-7707(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 257-294; 571-612 AND 823-892.
RC TISSUE=Liver;
RX PubMed=3818625; DOI=10.1016/s0021-9258(18)61588-1;
RA Aldred A.R., Grimes A., Schreiber G., Mercer J.F.B.;
RT "Rat ceruloplasmin. Molecular cloning and gene expression in liver, choroid
RT plexus, yolk sac, placenta, and testis.";
RL J. Biol. Chem. 262:2875-2878(1987).
RN [3]
RP COPPER-BINDING, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14707133; DOI=10.1074/jbc.m313678200;
RA Mani K., Cheng F., Havsmark B., David S., Fransson L.A.;
RT "Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in the
RT copper/zinc-nitric oxide-dependent degradation of glypican-1 heparan
RT sulfate in rat C6 glioma cells.";
RL J. Biol. Chem. 279:12918-12923(2004).
CC -!- FUNCTION: Ceruloplasmin is a blue, copper-binding (6-7 atoms per
CC molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to
CC Fe(3+) without releasing radical oxygen species. It is involved in iron
CC transport across the cell membrane. May also play a role in fetal lung
CC development or pulmonary antioxidant defense. involved in iron
CC transport across the cell membrane (By similarity). Provides Cu(2+)
CC ions for the ascorbate-mediated deaminase degradation of the heparan
CC sulfate chains of GPC1. {ECO:0000250, ECO:0000269|PubMed:14707133}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Note=Binds 6 Cu cations per monomer.;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14707133}.
CC Note=Colocalizes with GCP1 in secretory intracellular compartments.
CC -!- TISSUE SPECIFICITY: Synthesized in liver and secreted into the plasma.
CC Also choroid plexus, yolk sac, placenta, and testis; not in stomach and
CC small intestine. Fetal lung and liver.
CC -!- INDUCTION: By inflammation.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA40914.1; Type=Miscellaneous discrepancy; Note=Wrong order of assembly of the mRNA fragments.; Evidence={ECO:0000305};
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DR EMBL; L33869; AAA40917.1; -; mRNA.
DR EMBL; M80529; AAB65820.1; -; Genomic_DNA.
DR EMBL; J02670; AAA40914.1; ALT_SEQ; mRNA.
DR EMBL; M14102; AAA40915.1; -; mRNA.
DR PIR; A35210; A35210.
DR PDB; 5N0K; X-ray; 2.30 A; A=1-1059.
DR PDB; 5N4L; X-ray; 3.20 A; A/B=20-1053.
DR PDBsum; 5N0K; -.
DR PDBsum; 5N4L; -.
DR AlphaFoldDB; P13635; -.
DR SMR; P13635; -.
DR IntAct; P13635; 1.
DR STRING; 10116.ENSRNOP00000016083; -.
DR GlyGen; P13635; 6 sites.
DR iPTMnet; P13635; -.
DR PhosphoSitePlus; P13635; -.
DR jPOST; P13635; -.
DR PaxDb; P13635; -.
DR PRIDE; P13635; -.
DR UCSC; RGD:2387; rat.
DR RGD; 2387; Cp.
DR eggNOG; KOG1263; Eukaryota.
DR InParanoid; P13635; -.
DR OrthoDB; 1209165at2759; -.
DR BRENDA; 1.16.3.1; 5301.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-425410; Metal ion SLC transporters.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Reactome; R-RNO-917937; Iron uptake and transport.
DR PRO; PR:P13635; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0046658; C:anchored component of plasma membrane; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0051087; F:chaperone binding; ISO:RGD.
DR GO; GO:0005507; F:copper ion binding; IDA:RGD.
DR GO; GO:0004322; F:ferroxidase activity; ISO:RGD.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006879; P:cellular iron ion homeostasis; TAS:RGD.
DR GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR GO; GO:0055072; P:iron ion homeostasis; IBA:GO_Central.
DR GO; GO:0006826; P:iron ion transport; IBA:GO_Central.
DR GO; GO:0007595; P:lactation; IEP:RGD.
DR GO; GO:0001889; P:liver development; IEP:RGD.
DR GO; GO:0030324; P:lung development; IEP:RGD.
DR GO; GO:0060056; P:mammary gland involution; IEP:RGD.
DR GO; GO:0015679; P:plasma membrane copper ion transport; TAS:RGD.
DR GO; GO:0046688; P:response to copper ion; IDA:RGD.
DR GO; GO:0007584; P:response to nutrient; IEP:RGD.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR024715; Factor_5/8-like.
DR PANTHER; PTHR11709; PTHR11709; 3.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 3.
DR PIRSF; PIRSF000354; Factors_V_VIII; 1.
DR SUPFAM; SSF49503; SSF49503; 6.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Copper transport; Disulfide bond; Glycoprotein;
KW Ion transport; Metal-binding; Oxidoreductase; Reference proteome; Repeat;
KW Secreted; Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000305"
FT CHAIN 20..1059
FT /note="Ceruloplasmin"
FT /id="PRO_0000002914"
FT DOMAIN 20..356
FT /note="F5/8 type A 1"
FT DOMAIN 20..199
FT /note="Plastocyanin-like 1"
FT DOMAIN 208..354
FT /note="Plastocyanin-like 2"
FT DOMAIN 369..712
FT /note="F5/8 type A 2"
FT DOMAIN 369..554
FT /note="Plastocyanin-like 3"
FT DOMAIN 564..710
FT /note="Plastocyanin-like 4"
FT DOMAIN 724..1055
FT /note="F5/8 type A 3"
FT DOMAIN 724..894
FT /note="Plastocyanin-like 5"
FT DOMAIN 902..1051
FT /note="Plastocyanin-like 6"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 337
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 342
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 650
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 693
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 698
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 988
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 991
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 993
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1033
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1034
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1035
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1039
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1044
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 396
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 173..199
FT /evidence="ECO:0000250"
FT DISULFID 275..356
FT /evidence="ECO:0000250"
FT DISULFID 528..554
FT /evidence="ECO:0000250"
FT DISULFID 631..712
FT /evidence="ECO:0000250"
FT DISULFID 868..894
FT /evidence="ECO:0000250"
FT CONFLICT 271
FT /note="G -> A (in Ref. 2; AAA40914)"
FT /evidence="ECO:0000305"
FT CONFLICT 604..605
FT /note="ED -> DN (in Ref. 2; AAA40914)"
FT /evidence="ECO:0000305"
FT CONFLICT 823
FT /note="T -> S (in Ref. 2; AAA40915)"
FT /evidence="ECO:0000305"
FT CONFLICT 833
FT /note="V -> L (in Ref. 2; AAA40915)"
FT /evidence="ECO:0000305"
FT CONFLICT 868
FT /note="C -> V (in Ref. 2; AAA40915)"
FT /evidence="ECO:0000305"
FT CONFLICT 891
FT /note="L -> R (in Ref. 2; AAA40915)"
FT /evidence="ECO:0000305"
FT STRAND 21..34
FT /evidence="ECO:0007829|PDB:5N0K"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 65..77
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 88..90
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 104..115
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:5N4L"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:5N4L"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:5N4L"
FT STRAND 172..179
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5N4L"
FT HELIX 184..190
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 193..199
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 213..224
FT /evidence="ECO:0007829|PDB:5N0K"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 231..238
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:5N0K"
FT TURN 265..268
FT /evidence="ECO:0007829|PDB:5N4L"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 279..289
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 329..337
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:5N0K"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 370..384
FT /evidence="ECO:0007829|PDB:5N0K"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 405..408
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 417..429
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 452..455
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 491..494
FT /evidence="ECO:0007829|PDB:5N0K"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 508..514
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 517..519
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 527..534
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 539..545
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 548..554
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:5N4L"
FT STRAND 569..580
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 581..583
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 587..594
FT /evidence="ECO:0007829|PDB:5N0K"
FT TURN 598..600
FT /evidence="ECO:0007829|PDB:5N4L"
FT HELIX 606..611
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 613..617
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 629..631
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 636..642
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 650..654
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 659..661
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 664..671
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 676..681
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 687..693
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 696..700
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 704..710
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 724..739
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 744..753
FT /evidence="ECO:0007829|PDB:5N0K"
FT TURN 760..762
FT /evidence="ECO:0007829|PDB:5N0K"
FT TURN 765..767
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 771..783
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 787..789
FT /evidence="ECO:0007829|PDB:5N4L"
FT TURN 794..796
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 797..799
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 806..809
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 813..824
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 829..832
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 836..838
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 848..854
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 857..859
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 867..874
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 879..885
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 888..894
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 907..918
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 919..921
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 925..932
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 936..938
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 944..949
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 951..955
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 967..969
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 973..980
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 982..985
FT /evidence="ECO:0007829|PDB:5N4L"
FT STRAND 988..992
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 997..1000
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 1001..1003
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 1005..1012
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 1017..1022
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 1028..1034
FT /evidence="ECO:0007829|PDB:5N0K"
FT HELIX 1037..1041
FT /evidence="ECO:0007829|PDB:5N0K"
FT STRAND 1045..1051
FT /evidence="ECO:0007829|PDB:5N0K"
SQ SEQUENCE 1059 AA; 120841 MW; 12BA3B990A0B95E3 CRC64;
MKFLLLSALL FLHSSLAWTR EKHYYIGITE AVWDYASGSE EKELISVDTE QSNFYLRNGP
DRIGRKYKKA LYSEYTDGTF TKTIDKPAWL GFLGPVIKAE VGDKVSVHVK NFASRPYTFH
AHGVTYTKAN EGAIYPDNTT DFQRADDKLF PGQQYLYVLR ANEPSPGEGD SNCVTRIYHS
HVDAPKDIAS GLIGPLILCK KGSLHKEKEE NIDQEFVLMF SVVDENLSWY LEDNIKTFCS
EPEKVDKDNE DFQESNRMYS INGYTFGSLP GLSMCAEDRV KWYLFGMGNE VDVHSELFHG
QALTSKNYHT DIINLFPATL IDVSMVAQNP GVWMLSCQNL NHLKAGLQAF FQVRDCNKPS
PDDDIQDRHV RHYYIAAEET IWDYAPSGTD TFTGENFTSL GSDSRVFFEQ GATRIGGSYK
KLVYREYTDD SFTNRKERGP DEEHLGILGP VIWAEVGDII RVTFHNKGQF PLSIQPMGVR
FTKENEGTYY GPDGRSSKQA SHVAPKETFT YEWTVPKEMG PTYADPVCLS KMYYSGVDLT
KDIFTGLIGP MKICKKGSLL ADGRQKDVDK EFYLFATVFD ENESLLLDDN IRMFTTAPEN
VDKEDEDFQE SNKMHSMNGF MYGNLPGLNM CLGESIVWYL FSAGNEADVH GIYFSGNTYL
SKGERRDTAN LFPHKSLTLL MTPDTEGSFD VECLTTDHYT GGMKQKYTVN QCKGQFEDVT
LYQGERTYYI AAVEVEWDYS PSRDWEMELH HLQEQNVSNA FLDKEEFFIG SKYKKVVYRE
FTDSTFREQV KRRAEEEHLG MLGPLIHADV GAKVKVVFKN MATRPYSIHA HGVKTKSSTV
APTLPGEVRT YIWQIPERSG AGTEDSPCIP WAYYSTVDRV KDLYSGLIGP LIVCRKSYVK
VFNPKKKMEF SLLFLVFDEN ESWYLDDNIN TYPDHPEKDN KDNEEFIESN KMHAINGKMF
GNLQGLTMHV GDEVNWYVMA MGNEIDLHTV HFHGHSFQYK HRGIHSSDVF DFFPGTYQTL
EMFPQTPGTW LLHCHVTDHI HAGMVTTYTV LPNQETKSG
