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Apolipoprotein B-100 (Apo B-100) [Cleaved into: Apolipoprotein B-48 (Apo B-48)]

 APOB_RAT                Reviewed;        4743 AA.
Q7TMA5;
10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
12-SEP-2018, entry version 116.
RecName: Full=Apolipoprotein B-100;
Short=Apo B-100;
Contains:
RecName: Full=Apolipoprotein B-48;
Short=Apo B-48;
Flags: Precursor;
Name=Apob; ORFNames=Aa1064, Ac1-060;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
Xu C.S., Li W.Q., Li Y.C., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J.,
Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., Han H.P.,
Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
"Liver regeneration after PH.";
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=632283;
Wu A.L., Windmueller H.G.;
"Identification of circulating apolipoproteins synthesized by rat
small intestine in vivo.";
J. Biol. Chem. 253:2525-2528(1978).
[3]
CHARACTERIZATION.
PubMed=6948299; DOI=10.1073/pnas.79.1.179;
Van't Hooft F.M., Hardman D.A., Kane J.P., Havel R.J.;
"Apolipoprotein B (B-48) of rat chylomicrons is not a precursor of the
apolipoprotein of low density lipoproteins.";
Proc. Natl. Acad. Sci. U.S.A. 79:179-182(1982).
[4]
RNA EDITING.
PubMed=2911593; DOI=10.1073/pnas.86.2.500;
Tennyson G.E., Sabatos C.A., Higuchi K., Meglin N., Brewer H.B. Jr.;
"Expression of apolipoprotein B mRNAs encoding higher- and lower-
molecular weight isoproteins in rat liver and intestine.";
Proc. Natl. Acad. Sci. U.S.A. 86:500-504(1989).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2006, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Apolipoprotein B is a major protein constituent of
chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo
B-100 functions as a recognition signal for the cellular binding
and internalization of LDL particles by the apoB/E receptor.
{ECO:0000269|PubMed:632283}.
-!- SUBUNIT: Interacts with PCSK9. Interacts with MTTP.
{ECO:0000250|UniProtKB:P04114}.
-!- INTERACTION:
P04639:Apoa1; NbExp=2; IntAct=EBI-15185298, EBI-2925493;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04114}.
Secreted {ECO:0000269|PubMed:632283}.
-!- TISSUE SPECIFICITY: Detected in intestine and liver (at protein
level). {ECO:0000269|PubMed:632283}.
-!- PTM: Palmitoylated; structural requirement for proper assembly of
the hydrophobic core of the lipoprotein particle. {ECO:0000250}.
-!- RNA EDITING: Modified_positions=2147 {ECO:0000269|PubMed:2911593};
Note=The stop codon (UAA) at position 2147 is created by RNA
editing. Apo B-48, derived from the fully edited RNA, is produced
only in the intestine and is found in chylomicrons. Apo B-48 is a
shortened form of apo B-100 which lacks the LDL-receptor region.
The unedited version (apo B-100) is produced by the liver and is
found in the VLDL and LDL.;
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EMBL; AY318958; AAP85369.1; -; mRNA.
EMBL; AY321317; AAP86249.1; -; mRNA.
RefSeq; NP_062160.2; NM_019287.2.
UniGene; Rn.33815; -.
ProteinModelPortal; Q7TMA5; -.
SMR; Q7TMA5; -.
BioGrid; 248449; 1.
DIP; DIP-29910N; -.
IntAct; Q7TMA5; 1.
STRING; 10116.ENSRNOP00000039779; -.
CarbonylDB; Q7TMA5; -.
iPTMnet; Q7TMA5; -.
PhosphoSitePlus; Q7TMA5; -.
PaxDb; Q7TMA5; -.
PRIDE; Q7TMA5; -.
Ensembl; ENSRNOT00000046811; ENSRNOP00000039779; ENSRNOG00000005542.
GeneID; 54225; -.
KEGG; rno:54225; -.
CTD; 338; -.
RGD; 2129; Apob.
eggNOG; KOG0654; Eukaryota.
eggNOG; KOG4338; Eukaryota.
eggNOG; ENOG411104F; LUCA.
GeneTree; ENSGT00590000083139; -.
HOGENOM; HOG000034000; -.
HOVERGEN; HBG050546; -.
InParanoid; Q7TMA5; -.
KO; K14462; -.
OMA; FIVPLTD; -.
OrthoDB; EOG091G000G; -.
PhylomeDB; Q7TMA5; -.
TreeFam; TF331316; -.
Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
Reactome; R-RNO-3000471; Scavenging by Class B Receptors.
Reactome; R-RNO-3000480; Scavenging by Class A Receptors.
Reactome; R-RNO-3000497; Scavenging by Class H Receptors.
Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-RNO-432142; Platelet sensitization by LDL.
Reactome; R-RNO-5686938; Regulation of TLR by endogenous ligand.
Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
Reactome; R-RNO-8866423; VLDL assembly.
Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
Reactome; R-RNO-8963888; Chylomicron assembly.
Reactome; R-RNO-8963901; Chylomicron remodeling.
Reactome; R-RNO-8964026; Chylomicron clearance.
Reactome; R-RNO-8964038; LDL clearance.
Reactome; R-RNO-8964041; LDL remodeling.
Reactome; R-RNO-8964046; VLDL clearance.
Reactome; R-RNO-975634; Retinoid metabolism and transport.
PRO; PR:Q7TMA5; -.
Proteomes; UP000002494; Chromosome 6.
Bgee; ENSRNOG00000005542; Expressed in 4 organ(s), highest expression level in liver.
ExpressionAtlas; Q7TMA5; baseline and differential.
Genevisible; Q7TMA5; RN.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070971; C:endoplasmic reticulum exit site; IEA:Ensembl.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0034363; C:intermediate-density lipoprotein particle; IEA:Ensembl.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0034362; C:low-density lipoprotein particle; IDA:RGD.
GO; GO:0034359; C:mature chylomicron; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:RGD.
GO; GO:0031983; C:vesicle lumen; IDA:RGD.
GO; GO:0012506; C:vesicle membrane; IDA:RGD.
GO; GO:0017127; F:cholesterol transporter activity; IEA:Ensembl.
GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
GO; GO:0035473; F:lipase binding; IEA:Ensembl.
GO; GO:0008289; F:lipid binding; IMP:RGD.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IEA:Ensembl.
GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
GO; GO:0071379; P:cellular response to prostaglandin stimulus; IEP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0033344; P:cholesterol efflux; IEA:Ensembl.
GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
GO; GO:0008203; P:cholesterol metabolic process; IEA:UniProtKB-KW.
GO; GO:0009566; P:fertilization; IEA:Ensembl.
GO; GO:0030317; P:flagellated sperm motility; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0006629; P:lipid metabolic process; IDA:RGD.
GO; GO:0042158; P:lipoprotein biosynthetic process; IEA:Ensembl.
GO; GO:0042159; P:lipoprotein catabolic process; IEA:Ensembl.
GO; GO:0042953; P:lipoprotein transport; IEA:Ensembl.
GO; GO:0034383; P:low-density lipoprotein particle clearance; IEA:Ensembl.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; IEA:Ensembl.
GO; GO:0007399; P:nervous system development; IEA:Ensembl.
GO; GO:0010886; P:positive regulation of cholesterol storage; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0045540; P:regulation of cholesterol biosynthetic process; IEA:Ensembl.
GO; GO:0009743; P:response to carbohydrate; IDA:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0010033; P:response to organic substance; IEP:RGD.
GO; GO:0010269; P:response to selenium ion; IEP:RGD.
GO; GO:0009615; P:response to virus; IEA:Ensembl.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
GO; GO:0019433; P:triglyceride catabolic process; IMP:RGD.
GO; GO:0006642; P:triglyceride mobilization; IEA:Ensembl.
CDD; cd00043; CYCLIN; 1.
Gene3D; 1.25.10.20; -; 1.
Gene3D; 2.30.230.10; -; 1.
InterPro; IPR022176; ApoB100_C.
InterPro; IPR013763; Cyclin-like.
InterPro; IPR036915; Cyclin-like_sf.
InterPro; IPR006671; Cyclin_N.
InterPro; IPR015819; Lipid_transp_b-sht_shell.
InterPro; IPR001747; Lipid_transpt_N.
InterPro; IPR009454; Lipid_transpt_open_b-sht.
InterPro; IPR011030; Lipovitellin_superhlx_dom.
InterPro; IPR015816; Vitellinogen_b-sht_N.
InterPro; IPR015255; Vitellinogen_open_b-sht.
Pfam; PF12491; ApoB100_C; 1.
Pfam; PF00134; Cyclin_N; 1.
Pfam; PF06448; DUF1081; 1.
Pfam; PF09172; DUF1943; 1.
Pfam; PF01347; Vitellogenin_N; 1.
SMART; SM00385; CYCLIN; 1.
SMART; SM01169; DUF1943; 1.
SMART; SM00638; LPD_N; 1.
SUPFAM; SSF47954; SSF47954; 2.
SUPFAM; SSF48431; SSF48431; 1.
SUPFAM; SSF56968; SSF56968; 2.
PROSITE; PS51211; VITELLOGENIN; 1.
1: Evidence at protein level;
Acetylation; Atherosclerosis; Cholesterol metabolism; Chylomicron;
Complete proteome; Cytoplasm; Disulfide bond; Glycoprotein;
Heparin-binding; LDL; Lipid metabolism; Lipid transport; Lipoprotein;
Palmitate; Phosphoprotein; Reference proteome; RNA editing; Secreted;
Signal; Steroid metabolism; Sterol metabolism; Transport; VLDL.
SIGNAL 1 27 {ECO:0000250}.
CHAIN 28 4743 Apolipoprotein B-100.
/FTId=PRO_0000293536.
CHAIN 28 2146 Apolipoprotein B-48.
/FTId=PRO_0000293537.
DOMAIN 33 660 Vitellogenin. {ECO:0000255|PROSITE-
ProRule:PRU00557}.
REGION 29 113 Heparin-binding. {ECO:0000250}.
REGION 219 293 Heparin-binding. {ECO:0000250}.
REGION 890 947 Heparin-binding. {ECO:0000250}.
REGION 2010 2145 Heparin-binding. {ECO:0000250}.
REGION 3123 3198 Heparin-binding. {ECO:0000250}.
REGION 3136 3146 Basic (possible receptor binding region).
{ECO:0000250}.
REGION 3336 3356 LDL receptor binding. {ECO:0000250}.
REGION 3346 3479 Heparin-binding. {ECO:0000250}.
REGION 3349 3357 Basic (possible receptor binding region).
{ECO:0000250}.
MOD_RES 1973 1973 N6-acetyllysine.
{ECO:0000250|UniProtKB:P04114}.
MOD_RES 2006 2006 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 3981 3981 Phosphoserine.
{ECO:0000250|UniProtKB:P04114}.
MOD_RES 3985 3985 Phosphothreonine.
{ECO:0000250|UniProtKB:P04114}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 971 971 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1336 1336 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1345 1345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1491 1491 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2094 2094 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2522 2522 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2662 2662 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2741 2741 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2791 2791 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2897 2897 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2944 2944 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3063 3063 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3186 3186 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3299 3299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3321 3321 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3428 3428 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3715 3715 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3828 3828 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4203 4203 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4232 4232 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 65 84 {ECO:0000255|PROSITE-ProRule:PRU00557}.
DISULFID 173 199 {ECO:0000255|PROSITE-ProRule:PRU00557}.
DISULFID 232 248 {ECO:0000255|PROSITE-ProRule:PRU00557}.
DISULFID 372 377 {ECO:0000255|PROSITE-ProRule:PRU00557}.
DISULFID 466 501 {ECO:0000255|PROSITE-ProRule:PRU00557}.
DISULFID 954 964 {ECO:0000255|PROSITE-ProRule:PRU00557}.
SEQUENCE 4743 AA; 536024 MW; B01AD103F8EC5320 CRC64;
MGPQRPALRA PLLLLFLLLF LDTSVWAQDA TRFKHLRKYV YSYEAESSSG VRGTADSRSA
TKINCKVELE VPQVCTLIMR TSQCTLKEVY GFNPEGKALM KKTKNSEEFA SAMSRYELKL
AFPEGKRVAL YPDLGEPNYI LNIKRGIISA LLVPPETEED KQVLFQDTVY GNCSTQVTVN
SRKGTVATEM STERNLQHCD GFQPISTSVS PLALIKGLVR PLSTLISSSQ SCQYTLEPKR
KHVSEAICNE QHLFLPFSYK NKYGIMTHVT QKLSLEDTPK INSRFFRGGI NQVGLAFEST
KSTSPPKQAD AVLKTLQELK KLSISEQNAQ RANLFHKLVT ELRGLSGEAI TSLLPQLIEV
SSPITLQALI QCGQPECYTH ILQWLKTEKA HPLLIDIVTY LMALIPNPSV QRLQEIFNTA
KELQSRATLY ALSHAVNSYY AIMDHSRSPV LEDIAGYLMK QIDNECMGDE DRTFLILRVI
GNMGRTMERV MPALKSSVLN CVRSTKPSLQ IQKAALQALR KMEMGDEVRT ILFDTFVNDV
APVEKRLAAY LLLMRSPSSS DINKIAKLLQ WEQSEQVKNF VASHIANILN SEELYVQDLK
NLIKNALVNS RLPTIMDFRK FSRNYQISKS VSIPLFDPVS AKIEGNLVFD PSSYLPKESM
LKTTLTVFGI ASLDLFEIGL EGKGFEPTLE ALFGKQGFFP DSVNKALYWV NGQVPDRVSK
VLVDHFGYTK DDKHEQDMVN GIMPIVDKLI KELKSKEIPE ARAYLRILGK ELGFVRLQDL
QVLGKLLLNG AQTFRGVPQM IVQAIREGSK DDLFLHYIFM ENAFELPTGV GLQLQVSSSG
VFTPGIKAGV RLELANIQAE LVAKPSVSLE FVTNMGIIIP DFAKSGVQMN TNFFHESGLE
ARVALKAGQL KVIIPSPKRP VKLFSGSNTL HLVSTTKTEV IPPLIENRKS WSTCKPFFTG
MNYCTTGAYS NASSTESASY YPLTGDTRYE LELKPTGEVE QYSASATYEL LKEDKSLVDT
LKFLVQAEGV QQSEATAMFK YNRRSRTLSS EVLIPGFDVN FGTILRVNDE SSKDKNTYKL
ILDIQNKKIT EVSVVGHVSY DKKGDGKVKG VVSIPRLQAE ARSEVHTHWS PTKLLFQMDS
SATAYGSTIS KRVAWRYDNE KIEFDWNTGT NVDTKKVASN FPVDLSRYPR MVHEYANGLL
DHRVPQTDMT FRHMGSKLIV DHLNGLSELN LPKVGLPDFH IPDNLFLKTD GRVKYTLNKN
RIEIDIPLPL GGKSSKDLKV PESVRTPALN FKSVGFHLPS QEVQIPTFTI PKTHQLQVPL
LGILDLSTNV YSNLYNWSVS YTGGNTSRDH FSLQAQYRMK ADSVVDLFSY SVQGSGETTY
DSKSTFTLSC DGSLHHKFLD SKFKVSHVEK FGNNPVSKGL LTFETSSALG PQMSATVQLD
SKKKQHLYVK DIKVDGQFRV FSLYAQGEYG LSYERDSMTG QMSGESNMKF NSTYFQGTNQ
IVGMYQDGML SVTSTSDLQD GIFKNTASLK YENYELTLKS DSSGQYENFA ASNKLDMTFS
KQSALLRSEH QANYKSLRLV TLLSGSLTSQ GVELNADILG TDKINTGAHK STLKIAQDGV
STSATTNLKY SPLLLENELN AELGLSGASM KLSTSGRFKE HHAKFSLDGR AALTEVSLGS
IYQAMILGAD SKNVFNFKLS REGLKLSNDM MGSYAEMKLD HTHSLRISGL SLDFFSKMDN
IYSGDKFYKQ NFNLQLQPYS FGITLSNDLK YDALVLTNNG RLRLEPLKLN VGGNFKGTYQ
NNELKHIYTI SYTDLVVASY RADTVATVQG VEFSHRLNAD IEGLASSVDV TTSYSSDPLH
FNNVFRFVLA PFTLGVDTHT SGDGKMSLWG EHTGQMYSKF LLKAEPLALT FSHDYKGSTS
HNLLYKNSVS TALEHTLSAL LTPAEQTSSW KFKTSLNDKV YSQEFEAYNT KDKIGIELSG
RADLSGLYSP IKVPFFYSEP VNVLNSLEIN DAFDEPREFT IDAVVKYDKN QDVHTISLPF
FQSLPDYLER NRRGIISLLE AMKGELQRLS VDQFVRKYRV ALSRLPQQIH DYLNASDWER
QVAGAKEKLT SFMENYRITD NDVLIALDSA KINLNEKLSQ LETYAIQFDQ YIRDNYDAQD
LKRTIAQIID RIIEKLKMLD EQYHIRVNLA KSIHNLYLFV ENVDLNQISS SGASWIQNVD
TKYQIRIQIQ EKLQHLRTQI HNIDIQQLAA ELKQQIEALD VPMHLDQLRT AILFQRISVI
IERVKYFVMN LIEDFKVTEK INTFRVIVRE LIEKYEVDRQ IQVLMDKSIE LAHRYSLSEP
LQKLSNVLQQ IEIKDYYDKL VGFIDDTVEW IKAVSFKNII EELNRLIDMS VKKLKAFDYH
QFVDKTNSKI REMTQRINAE IQALELPQKT EALKLWVEDF KTTVSNSLEK LKDTKVTVVV
DWLQDGLAQI KAQFQDALED VRDRIYQMDI QGELERCLSL VSQVYSTVVT YISDWWTLTA
KNITDFAEQY STQKWAESVK ALVEQGFIVP EIQTFLGTMP AFEVSLHALQ EANFQTPDFI
VPLTDLRIPS IWINFKMLKN VKIPLRFSTP EFTLLNTFRV RSFTIDLLEI KAKIIRTIDQ
MLSSELQWPL PEVYLRDLEM VNISLARLSL PDFHVPEITI PEFTIPNVNL KDLQVPDLHI
PEFQLPHLSC TTEIPAFGKL HSVLKIQSPL FILDASANIQ NITTSENKAE IVASVTARGE
SKFEALNFDF QAQAQFLELN ANPLVLKESV NFSSKHVRME HEGKILVSGK ALEGKSDTVA
RLHTEKNTVE FNNGIVVKIN NQFTLDSQTK YFHKLSVPRL DFSSKASLNN EIKTLLEAGH
MAWTSSGTGS WNWACPNFSD EGIHSSKISF IVDGPIASFG LSNNINGKHL RVVQKLTSES
GFLNYSRFEV ESKVESQHVG SSILTAEGRA LLGDAKAEMT GEHNANLNGK VIGTLKNSLF
FSAQPFEITA STNNEGNLKV SFPLKLTGKI DFLNNYALFL SPHAQQASWQ LSTRFNQYKY
NQNFSAINNE HNMEASIVMN GDANLDFLNI PLTIPEINLP YTRFTTPLLK DFSIWEETGL
KEFLKTTKQS FDLSIKAQYK KNRDKHSVVI PLKMFYEFML NNVNSWDRKF EKVRDNALHF
LTASYNETKI KFDKYKTENS LNQPSRTFQN RGHTIPVLNI EVSPFAVETL ASSHVIPKAI
RTPSVTIPGP NIIVPSYRLV LPSLQLPVFH IPRTLFKFSL PDFKKLSTID NIYIPAMGNF
TYDFSFKSSV ITLNTNAGLY NQSDLVARFL SSSSFVTDAL QYKLEGTSRL MRKKVLKLAT
AVSLTNKFLK GSHDSTISLT KKNMEASVKT TANLHAPIFT MNFKQELNGN TKSKPTVSSS
IELNYDFNSS KLHSAAKGGV DHKFSLESLT SYLSIESFTK GNIKGSFLSQ EYSGSVANEA
NVYLNSKGTR SSVRLQGASN FAGIWNFEVG ENFAGEATLR RIYGTWEHNM INHLQVFSYF
DTKGKQTCRA TLELSPWTMS TLLQVHVSQP SPLFDLHHFD QEVILKASTK NQKVSWKSEV
QVESQVLQHN AHFSNDQEEV RLDIAGSLEG QLWDLENFFL PAFGKSLREL LQIDGKRQYL
QASTSLHYTK NPNGYLLSLP VQELTDRFII PGLKLNDFSG IKIYKKLSTS PFALNLTMLP
KVKFPGVDLL TQYSKPEGSS VPTFETTIPE IQLTVSQFTL PKSFPVGNTV FDLNKLTNLI
ADVDLPSITL PEQTIEIPSL EFSVPAGIFI PFFGELTAHV GMASPLYNVT WSTGWKNKAD
HVETFLDSTC SSTLQFLEYA LKVVGTHRIE NDKFIYKIKG TLQHCDFNVK YNEDGIFEGL
WDLEGEAHLD ITSPALTDFH LHYKEDKTSV SASAASPAIG TVSLDASTDD QSVRLNVYFR
PQSPPDNKLS IFKMEWRDKE SDGETYIKIN WEEEAAFRLL DSLKSNVPKA SEAVYDYVKK
YHLGHASSEL RKSLQNDAEH AIRMVDEMNV NAQRVTRDTY QSLYKKMLAQ ESQSIPEKLK
KMVLGSLVRI TQKYHMAVTW LMDSVIHFLK FNRVQFPGNA GTYTVDELYT IAMRETKKLL
SQLFNGLGHL FSYVQDQVEK SRVINDITFK CPFSPTPCKL KDVLLIFRED LNILSNLGQQ
DINFTTILSD FQSFLERLLD IIEEKIECLK NNESTCVPDH INMFFKTHIP FAFKSLRENI
YSVFSEFNDF VQSILQEGSY KLQQVHQYMK AFREEYFDPS VVGWTVKYYE IEEKMVDLIK
TLLAPLRDFY SEYSVTAADF ASKMSTQVEQ FVSRDIREYL SMLADINGKG REKVAELSIV
VKERIKSWST AVAEITSDYL RQLHSKLQDF SDQLSGYYEK FVAESTRLID LSIQNYHMFL
RYIAELLKKL QVATANNGLL KRGDFEAAVK LGIACLYNEG LSVSDEAYAE VNGLKASRFF
SMDERLNMGS DPFIWLSICP PCFRKLRDFA GKGCWEAQPA LAKDCAGGSQ LGLEGKAFSE
SVCQLFQASQ AVNKQQIFSV QKGLSDTVRY ILIGWLVEVA PMKDFTSLCL HLTVECVGRY
LQRKLVPRYK LQLLGIACMV ICTWFISKEI LTIREAVRLT DNTYKYKDLV RVKREIISAL
EGKIRIPTVV DYKEVLLTLV PVTPRTQYLC SFLCELTLSV YTPAHLASAA LLLARLMHGQ
TQP


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