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Complement C3 (HSE-MSF) [Cleaved into: Complement C3 beta chain; C3-beta-c (C3bc); Complement C3 alpha chain; C3a anaphylatoxin; Acylation stimulating protein (ASP) (C3adesArg); Complement C3b alpha' chain; Complement C3c alpha' chain fragment 1; Complement C3dg fragment; Complement C3g fragment; Complement C3d fragment; Complement C3f fragment; Complement C3c alpha' chain fragment 2]

 CO3_MOUSE               Reviewed;        1663 AA.
P01027; Q61370; Q80XP1;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
05-DEC-2018, entry version 190.
RecName: Full=Complement C3;
AltName: Full=HSE-MSF;
Contains:
RecName: Full=Complement C3 beta chain;
Contains:
RecName: Full=C3-beta-c;
Short=C3bc;
Contains:
RecName: Full=Complement C3 alpha chain;
Contains:
RecName: Full=C3a anaphylatoxin;
Contains:
RecName: Full=Acylation stimulating protein;
Short=ASP;
AltName: Full=C3adesArg;
Contains:
RecName: Full=Complement C3b alpha' chain;
Contains:
RecName: Full=Complement C3c alpha' chain fragment 1;
Contains:
RecName: Full=Complement C3dg fragment;
Contains:
RecName: Full=Complement C3g fragment;
Contains:
RecName: Full=Complement C3d fragment;
Contains:
RecName: Full=Complement C3f fragment;
Contains:
RecName: Full=Complement C3c alpha' chain fragment 2;
Flags: Precursor;
Name=C3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
PubMed=6208565; DOI=10.1098/rstb.1984.0094;
Fey G.H., Lundwall A., Wetsel R.A., Tack B.F., de Bruijn M.H.L.,
Domdey H.;
"Nucleotide sequence of complementary DNA and derived amino acid
sequence of murine complement protein C3.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 306:333-344(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-724 (ISOFORM LONG).
PubMed=6548745;
Lundwall A., Wetsel R.A., Domdey H., Tack B.F., Fey G.H.;
"Structure of murine complement component C3. I. Nucleotide sequence
of cloned complementary and genomic DNA coding for the beta chain.";
J. Biol. Chem. 259:13851-13856(1984).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
PubMed=6985486; DOI=10.1073/pnas.79.23.7077;
Wiebauer K., Domdey H., Diggelmann H., Fey G.;
"Isolation and analysis of genomic DNA clones encoding the third
component of mouse complement.";
Proc. Natl. Acad. Sci. U.S.A. 79:7077-7081(1982).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-1663 (ISOFORM LONG).
PubMed=2578664; DOI=10.1073/pnas.82.1.9;
Sottrup-Jensen L., Stepanik T.M., Kristensen T., Lonblad P.B.,
Jones C.M., Wierzbicki D.M., Magnusson S., Domdey H., Wetsel R.A.,
Lundwall A., Tack B.F., Fey G.H.;
"Common evolutionary origin of alpha 2-macroglobulin and complement
components C3 and C4.";
Proc. Natl. Acad. Sci. U.S.A. 82:9-13(1985).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-240 (ISOFORM LONG).
PubMed=6356427; DOI=10.1007/BF00205869;
Fey G., Domdey H., Wiebauer K., Whitehead A.S., Odink K.;
"Structure and expression of the C3 gene.";
Springer Semin. Immunopathol. 6:119-147(1983).
[7]
PROTEIN SEQUENCE OF 25-41 AND 749-760.
PubMed=8364938;
Hamada J., Cavanaugh P.G., Miki K., Nicolson G.L.;
"A paracrine migration-stimulating factor for metastatic tumor cells
secreted by mouse hepatic sinusoidal endothelial cells: identification
as complement component C3b.";
Cancer Res. 53:4418-4423(1993).
[8]
PROTEIN SEQUENCE OF 25-31 AND 671-680.
PubMed=2065778; DOI=10.1016/0014-5793(91)80715-F;
Sato T., Hong M.H., Jin C.H., Ishimi Y., Udagawa N., Shinki T.,
Abe E., Suda T.;
"The specific production of the third component of complement by
osteoblastic cells treated with 1 alpha,25-dihydroxyvitamin D3.";
FEBS Lett. 285:21-24(1991).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 658-761.
PubMed=6609661; DOI=10.1111/j.1749-6632.1983.tb18118.x;
Fey G.H., Wiebauer K., Domdey H.;
"Amino acid sequences of mouse complement C3 derived from nucleotide
sequences of cloned cDNA.";
Ann. N. Y. Acad. Sci. 421:307-312(1983).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 671-1663 (ISOFORM LONG).
PubMed=6094532;
Wetsel R.A., Lundwall A., Davidson F., Gibson T., Tack B.F., Fey G.H.;
"Structure of murine complement component C3. II. Nucleotide sequence
of cloned complementary DNA coding for the alpha chain.";
J. Biol. Chem. 259:13857-13862(1984).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 671-748.
PubMed=6961437; DOI=10.1073/pnas.79.24.7619;
Domdey H., Wiebauer K., Kazmaier M., Mueller V., Odink K., Fey G.H.;
"Characterization of the mRNA and cloned cDNA specifying the third
component of mouse complement.";
Proc. Natl. Acad. Sci. U.S.A. 79:7619-7623(1982).
[12]
ALTERNATIVE INITIATION (ISOFORM SHORT).
PubMed=7964485; DOI=10.1084/jem.180.6.2079;
Cahen-Kramer Y., Martensson I.L., Melchers F.;
"The structure of an alternate form of complement C3 that displays
costimulatory growth factor activity for B lymphocytes.";
J. Exp. Med. 180:2079-2088(1994).
[13]
FUNCTION.
PubMed=12244109; DOI=10.1074/jbc.M207281200;
Xia Z., Sniderman A.D., Cianflone K.;
"Acylation-stimulating protein (ASP) deficiency induces obesity
resistance and increased energy expenditure in ob/ob mice.";
J. Biol. Chem. 277:45874-45879(2002).
[14]
DISRUPTION PHENOTYPE, AND FUNCTION.
PubMed=18160458; DOI=10.1152/ajpendo.00590.2007;
Paglialunga S., Fisette A., Yan Y., Deshaies Y., Brouillette J.F.,
Pekna M., Cianflone K.;
"Acylation-stimulating protein deficiency and altered adipose tissue
in alternative complement pathway knockout mice.";
Am. J. Physiol. 294:E521-E529(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: C3 plays a central role in the activation of the
complement system. Its processing by C3 convertase is the central
reaction in both classical and alternative complement pathways.
After activation C3b can bind covalently, via its reactive
thioester, to cell surface carbohydrates or immune aggregates.
-!- FUNCTION: Derived from proteolytic degradation of complement C3,
C3a anaphylatoxin is a mediator of local inflammatory process. In
chronic inflammation, acts as a chemoattractant for neutrophils
(By similarity). It induces the contraction of smooth muscle,
increases vascular permeability and causes histamine release from
mast cells and basophilic leukocytes. The short isoform has B-cell
stimulatory activity. {ECO:0000250}.
-!- FUNCTION: C3-beta-c: Acts as a chemoattractant for neutrophils in
chronic inflammation. {ECO:0000250}.
-!- FUNCTION: Acylation stimulating protein: adipogenic hormone that
stimulates triglyceride (TG) synthesis and glucose transport in
adipocytes, regulating fat storage and playing a role in
postprandial TG clearance. Appears to stimulate TG synthesis via
activation of the PLC, MAPK and AKT signaling pathways. Ligand for
C5AR2. Promotes the phosphorylation, ARRB2-mediated
internalization and recycling of C5AR2.
-!- SUBUNIT: C3 precursor is first processed by the removal of 4 Arg
residues, forming two chains, beta and alpha, linked by a
disulfide bond. C3 convertase activates C3 by cleaving the alpha
chain, releasing C3a anaphylatoxin and generating C3b (beta chain
+ alpha' chain). C3dg interacts with CR2 (via the N-terminal Sushi
domains 1 and 2). Interacts with VSIG4. Interacts (both C3a and
ASP) with C5AR2; the interaction occurs with higher affinity for
ASP, enhancing the phosphorylation and activation of C5AR2,
recruitment of ARRB2 to the cell surface and endocytosis of GRP77
(By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative initiation; Named isoforms=2;
Name=Long;
IsoId=P01027-1; Sequence=Displayed;
Name=Short;
IsoId=P01027-2; Sequence=VSP_018708;
-!- PTM: C3b is rapidly split in two positions by factor I and a
cofactor to form iC3b (inactivated C3b) and C3f which is released.
Then iC3b is slowly cleaved (possibly by factor I) to form C3c
(beta chain + alpha' chain fragment 1 + alpha' chain fragment 2),
C3dg and C3f. Other proteases produce other fragments such as C3d
or C3g. C3a is further processed by carboxypeptidases to release
the C-terminal arginine residue generating the acylation
stimulating protein (ASP). Levels of ASP are increased in
adipocytes in the postprandial period and by dietary chylomicrons.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P01024}.
-!- DISRUPTION PHENOTYPE: Null mice displayed altered lipid metabolism
and morphological changes in adipocyte distribution. There is
reduced adipsin/CFD expression, increased number of smaller fat
cells, decreased DGAT1 expression and activity, and less
triglyceride storage capacity associated with delayed postprandial
clearance. Mice on a high-fat diet exihibited no diet-induced up-
regulation of adipsin/CFD expression nor adipocyte
differentiation. {ECO:0000269|PubMed:18160458}.
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EMBL; K02782; AAC42013.1; -; mRNA.
EMBL; BC043338; AAH43338.1; -; mRNA.
EMBL; M35659; AAA37339.1; -; mRNA.
EMBL; M33032; AAA37378.1; -; mRNA.
EMBL; J00369; AAA37336.1; -; Genomic_DNA.
EMBL; J00367; AAA37336.1; JOINED; Genomic_DNA.
EMBL; Z37998; CAA86099.2; -; Genomic_DNA.
CCDS; CCDS37670.1; -. [P01027-1]
PIR; A92459; C3MS.
PIR; I48284; I48284.
RefSeq; NP_033908.2; NM_009778.3. [P01027-1]
UniGene; Mm.19131; -.
ProteinModelPortal; P01027; -.
SMR; P01027; -.
BioGrid; 198418; 2.
ComplexPortal; CPX-988; Complement C3b complex.
IntAct; P01027; 7.
MINT; P01027; -.
STRING; 10090.ENSMUSP00000024988; -.
MEROPS; I39.950; -.
iPTMnet; P01027; -.
PhosphoSitePlus; P01027; -.
SwissPalm; P01027; -.
MaxQB; P01027; -.
PaxDb; P01027; -.
PeptideAtlas; P01027; -.
PRIDE; P01027; -.
Ensembl; ENSMUST00000024988; ENSMUSP00000024988; ENSMUSG00000024164. [P01027-1]
GeneID; 12266; -.
KEGG; mmu:12266; -.
UCSC; uc008deg.2; mouse. [P01027-1]
CTD; 718; -.
MGI; MGI:88227; C3.
eggNOG; KOG1366; Eukaryota.
eggNOG; ENOG410XRED; LUCA.
GeneTree; ENSGT00940000154063; -.
HOGENOM; HOG000286028; -.
HOVERGEN; HBG005110; -.
InParanoid; P01027; -.
KO; K03990; -.
OMA; QDGEQRI; -.
OrthoDB; EOG091G00FJ; -.
TreeFam; TF313285; -.
Reactome; R-MMU-173736; Alternative complement activation.
Reactome; R-MMU-174577; Activation of C3 and C5.
Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-MMU-375276; Peptide ligand-binding receptors.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-418594; G alpha (i) signalling events.
Reactome; R-MMU-6798695; Neutrophil degranulation.
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
Reactome; R-MMU-977606; Regulation of Complement cascade.
ChiTaRS; C3; mouse.
PMAP-CutDB; P01027; -.
PRO; PR:P01027; -.
Proteomes; UP000000589; Chromosome 17.
Bgee; ENSMUSG00000024164; Expressed in 182 organ(s), highest expression level in uterine cervix.
CleanEx; MM_C3; -.
ExpressionAtlas; P01027; baseline and differential.
Genevisible; P01027; MM.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0031715; F:C5L2 anaphylatoxin chemotactic receptor binding; ISS:UniProtKB.
GO; GO:0048037; F:cofactor binding; ISO:MGI.
GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0008289; F:lipid binding; ISO:MGI.
GO; GO:0097242; P:amyloid-beta clearance; IMP:ARUK-UCL.
GO; GO:0007596; P:blood coagulation; ISO:MGI.
GO; GO:1905114; P:cell surface receptor signaling pathway involved in cell-cell signaling; IMP:ARUK-UCL.
GO; GO:0006956; P:complement activation; IDA:MGI.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0006911; P:phagocytosis, engulfment; IMP:ARUK-UCL.
GO; GO:0001970; P:positive regulation of activation of membrane attack complex; IMP:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
GO; GO:2000427; P:positive regulation of apoptotic cell clearance; ISO:MGI.
GO; GO:0048639; P:positive regulation of developmental growth; ISO:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
GO; GO:0010828; P:positive regulation of glucose transmembrane transport; ISS:UniProtKB.
GO; GO:0010884; P:positive regulation of lipid storage; ISS:UniProtKB.
GO; GO:0050766; P:positive regulation of phagocytosis; IMP:MGI.
GO; GO:0060100; P:positive regulation of phagocytosis, engulfment; IMP:ARUK-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0001798; P:positive regulation of type IIa hypersensitivity; IMP:MGI.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; ISO:MGI.
GO; GO:0010866; P:regulation of triglyceride biosynthetic process; ISS:UniProtKB.
GO; GO:0009617; P:response to bacterium; IEP:MGI.
CDD; cd00017; ANATO; 1.
CDD; cd03583; NTR_complement_C3; 1.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 2.60.40.690; -; 1.
InterPro; IPR009048; A-macroglobulin_rcpt-bd.
InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
InterPro; IPR011625; A2M_N_BRD.
InterPro; IPR011626; Alpha-macroglobulin_TED.
InterPro; IPR000020; Anaphylatoxin/fibulin.
InterPro; IPR018081; Anaphylatoxin_comp_syst.
InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
InterPro; IPR035711; Complement_C3-like.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001599; Macroglobln_a2.
InterPro; IPR019742; MacrogloblnA2_CS.
InterPro; IPR002890; MG2.
InterPro; IPR001134; Netrin_domain.
InterPro; IPR018933; Netrin_module_non-TIMP.
InterPro; IPR035815; NTR_complement_C3.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
InterPro; IPR008993; TIMP-like_OB-fold.
PANTHER; PTHR11412:SF81; PTHR11412:SF81; 1.
Pfam; PF00207; A2M; 1.
Pfam; PF07703; A2M_BRD; 1.
Pfam; PF07677; A2M_recep; 1.
Pfam; PF01821; ANATO; 1.
Pfam; PF01835; MG2; 1.
Pfam; PF01759; NTR; 1.
Pfam; PF07678; TED_complement; 1.
PRINTS; PR00004; ANAPHYLATOXN.
SMART; SM01360; A2M; 1.
SMART; SM01359; A2M_N_2; 1.
SMART; SM01361; A2M_recep; 1.
SMART; SM00104; ANATO; 1.
SMART; SM00643; C345C; 1.
SUPFAM; SSF47686; SSF47686; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF49410; SSF49410; 1.
SUPFAM; SSF50242; SSF50242; 1.
PROSITE; PS00477; ALPHA_2_MACROGLOBULIN; 1.
PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
PROSITE; PS50189; NTR; 1.
1: Evidence at protein level;
Alternative initiation; Cleavage on pair of basic residues;
Complement alternate pathway; Complement pathway; Complete proteome;
Direct protein sequencing; Disulfide bond; Fatty acid metabolism;
Glycoprotein; Immunity; Inflammatory response; Innate immunity;
Lipid metabolism; Phosphoprotein; Reference proteome; Secreted;
Signal; Thioester bond.
SIGNAL 1 24 {ECO:0000269|PubMed:2065778,
ECO:0000269|PubMed:8364938}.
CHAIN 25 1663 Complement C3.
/FTId=PRO_0000005917.
CHAIN 25 666 Complement C3 beta chain.
/FTId=PRO_0000005918.
CHAIN 569 666 C3-beta-c. {ECO:0000250}.
/FTId=PRO_0000430431.
CHAIN 671 1663 Complement C3 alpha chain.
/FTId=PRO_0000005919.
CHAIN 671 748 C3a anaphylatoxin.
/FTId=PRO_0000005920.
CHAIN 671 747 Acylation stimulating protein.
/FTId=PRO_0000419936.
CHAIN 749 1663 Complement C3b alpha' chain.
/FTId=PRO_0000005921.
CHAIN 749 954 Complement C3c alpha' chain fragment 1.
/FTId=PRO_0000005922.
CHAIN 955 1303 Complement C3dg fragment.
/FTId=PRO_0000005923.
CHAIN 955 1001 Complement C3g fragment.
/FTId=PRO_0000005924.
CHAIN 1002 1303 Complement C3d fragment.
/FTId=PRO_0000005925.
PEPTIDE 1304 1320 Complement C3f fragment.
/FTId=PRO_0000005927.
CHAIN 1321 1663 Complement C3c alpha' chain fragment 2.
/FTId=PRO_0000273949.
DOMAIN 693 728 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1518 1661 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 1424 1456 Properdin-binding. {ECO:0000250}.
SITE 747 748 Cleavage; by carboxypeptidases.
{ECO:0000250}.
SITE 748 749 Cleavage; by C3 convertase.
SITE 954 955 Cleavage; by factor I. {ECO:0000255}.
SITE 1303 1304 Cleavage; by factor I.
SITE 1320 1321 Cleavage; by factor I.
MOD_RES 40 40 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 968 968 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 1321 1321 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
MOD_RES 1573 1573 Phosphoserine.
{ECO:0000250|UniProtKB:P01024}.
CARBOHYD 939 939 N-linked (GlcNAc...) asparagine.
CARBOHYD 1617 1617 N-linked (GlcNAc...) asparagine.
DISULFID 559 816 Interchain (between beta and alpha
chains). {ECO:0000255|PROSITE-
ProRule:PRU00022, ECO:0000255|PROSITE-
ProRule:PRU00295}.
DISULFID 626 661 {ECO:0000250}.
DISULFID 693 720 {ECO:0000250}.
DISULFID 694 727 {ECO:0000250}.
DISULFID 707 728 {ECO:0000250}.
DISULFID 873 1513 {ECO:0000250}.
DISULFID 1101 1158 {ECO:0000250}.
DISULFID 1358 1489 {ECO:0000250}.
DISULFID 1389 1458 {ECO:0000250}.
DISULFID 1506 1511 {ECO:0000250}.
DISULFID 1518 1590 {ECO:0000250}.
DISULFID 1537 1661 {ECO:0000250}.
DISULFID 1637 1646 {ECO:0000250}.
CROSSLNK 1010 1013 Isoglutamyl cysteine thioester (Cys-Gln).
{ECO:0000250}.
VAR_SEQ 1 1128 Missing (in isoform Short).
{ECO:0000305}.
/FTId=VSP_018708.
CONFLICT 137 137 K -> Q (in Ref. 6; AAA37339).
{ECO:0000305}.
CONFLICT 858 858 E -> Q (in Ref. 1; AAC42013).
{ECO:0000305}.
CONFLICT 1553 1553 E -> K (in Ref. 1; AAC42013 and 10;
AAA37336). {ECO:0000305}.
SEQUENCE 1663 AA; 186484 MW; 7E5546CC7C314779 CRC64;
MGPASGSQLL VLLLLLASSP LALGIPMYSI ITPNVLRLES EETIVLEAHD AQGDIPVTVT
VQDFLKRQVL TSEKTVLTGA SGHLRSVSIK IPASKEFNSD KEGHKYVTVV ANFGETVVEK
AVMVSFQSGY LFIQTDKTIY TPGSTVLYRI FTVDNNLLPV GKTVVILIET PDGIPVKRDI
LSSNNQHGIL PLSWNIPELV NMGQWKIRAF YEHAPKQIFS AEFEVKEYVL PSFEVRVEPT
ETFYYIDDPN GLEVSIIAKF LYGKNVDGTA FVIFGVQDGD KKISLAHSLT RVVIEDGVGD
AVLTRKVLME GVRPSNADAL VGKSLYVSVT VILHSGSDMV EAERSGIPIV TSPYQIHFTK
TPKFFKPAMP FDLMVFVTNP DGSPASKVLV VTQGSNAKAL TQDDGVAKLS INTPNSRQPL
TITVRTKKDT LPESRQATKT MEAHPYSTMH NSNNYLHLSV SRMELKPGDN LNVNFHLRTD
PGHEAKIRYY TYLVMNKGKL LKAGRQVREP GQDLVVLSLP ITPEFIPSFR LVAYYTLIGA
SGQREVVADS VWVDVKDSCI GTLVVKGDPR DNHLAPGQQT TLRIEGNQGA RVGLVAVDKG
VFVLNKKNKL TQSKIWDVVE KADIGCTPGS GKNYAGVFMD AGLAFKTSQG LQTEQRADLE
CTKPAARRRR SVQLMERRMD KAGQYTDKGL RKCCEDGMRD IPMRYSCQRR ARLITQGENC
IKAFIDCCNH ITKLREQHRR DHVLGLARSE LEEDIIPEED IISRSHFPQS WLWTIEELKE
PEKNGISTKV MNIFLKDSIT TWEILAVSLS DKKGICVADP YEIRVMQDFF IDLRLPYSVV
RNEQVEIRAV LFNYREQEEL KVRVELLHNP AFCSMATAKN RYFQTIKIPP KSSVAVPYVI
VPLKIGQQEV EVKAAVFNHF ISDGVKKTLK VVPEGMRINK TVAIHTLDPE KLGQGGVQKV
DVPAADLSDQ VPDTDSETRI ILQGSPVVQM AEDAVDGERL KHLIVTPAGC GEQNMIGMTP
TVIAVHYLDQ TEQWEKFGIE KRQEALELIK KGYTQQLAFK QPSSAYAAFN NRPPSTWLTA
YVVKVFSLAA NLIAIDSHVL CGAVKWLILE KQKPDGVFQE DGPVIHQEMI GGFRNAKEAD
VSLTAFVLIA LQEARDICEG QVNSLPGSIN KAGEYIEASY MNLQRPYTVA IAGYALALMN
KLEEPYLGKF LNTAKDRNRW EEPDQQLYNV EATSYALLAL LLLKDFDSVP PVVRWLNEQR
YYGGGYGSTQ ATFMVFQALA QYQTDVPDHK DLNMDVSFHL PSRSSATTFR LLWENGNLLR
SEETKQNEAF SLTAKGKGRG TLSVVAVYHA KLKSKVTCKK FDLRVSIRPA PETAKKPEEA
KNTMFLEICT KYLGDVDATM SILDISMMTG FAPDTKDLEL LASGVDRYIS KYEMNKAFSN
KNTLIIYLEK ISHTEEDCLT FKVHQYFNVG LIQPGSVKVY SYYNLEESCT RFYHPEKDDG
MLSKLCHSEM CRCAEENCFM QQSQEKINLN VRLDKACEPG VDYVYKTELT NIELLDDFDE
YTMTIQQVIK SGSDEVQAGQ QRKFISHIKC RNALKLQKGK KYLMWGLSSD LWGEKPNTSY
IIGKDTWVEH WPEAEECQDQ KYQKQCEELG AFTESMVVYG CPN


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