APOB_RAT
ID APOB_RAT Reviewed; 4743 AA.
AC Q7TMA5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Apolipoprotein B-100;
DE Short=Apo B-100;
DE Contains:
DE RecName: Full=Apolipoprotein B-48;
DE Short=Apo B-48;
DE Flags: Precursor;
GN Name=Apob; ORFNames=Aa1064, Ac1-060;
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 [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Xu C.S., Li W.Q., Li Y.C., Wang G.P., Chai L.Q., Yuan J.Y., Yang K.J.,
RA Yan H.M., Chang C.F., Zhao L.F., Ma H., Wang L., Wang S.F., Han H.P.,
RA Shi J.B., Rahman S., Wang Q.N., Zhang J.B.;
RT "Liver regeneration after PH.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=632283; DOI=10.1016/s0021-9258(17)40852-0;
RA Wu A.L., Windmueller H.G.;
RT "Identification of circulating apolipoproteins synthesized by rat small
RT intestine in vivo.";
RL J. Biol. Chem. 253:2525-2528(1978).
RN [3]
RP CHARACTERIZATION.
RX PubMed=6948299; DOI=10.1073/pnas.79.1.179;
RA Van't Hooft F.M., Hardman D.A., Kane J.P., Havel R.J.;
RT "Apolipoprotein B (B-48) of rat chylomicrons is not a precursor of the
RT apolipoprotein of low density lipoproteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 79:179-182(1982).
RN [4]
RP RNA EDITING.
RX PubMed=2911593; DOI=10.1073/pnas.86.2.500;
RA Tennyson G.E., Sabatos C.A., Higuchi K., Meglin N., Brewer H.B. Jr.;
RT "Expression of apolipoprotein B mRNAs encoding higher- and lower-molecular
RT weight isoproteins in rat liver and intestine.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:500-504(1989).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2006, AND IDENTIFICATION BY
RP 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: Apolipoprotein B is a major protein constituent of
CC chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-
CC 100 functions as a recognition signal for the cellular binding and
CC internalization of LDL particles by the apoB/E receptor.
CC {ECO:0000269|PubMed:632283}.
CC -!- SUBUNIT: Interacts with PCSK9. Interacts with MTTP. Interacts with
CC AUP1. {ECO:0000250|UniProtKB:P04114}.
CC -!- INTERACTION:
CC Q7TMA5; P04639: Apoa1; NbExp=2; IntAct=EBI-15185298, EBI-2925493;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P04114}.
CC Secreted {ECO:0000269|PubMed:632283}. Lipid droplet
CC {ECO:0000250|UniProtKB:P04114}.
CC -!- TISSUE SPECIFICITY: Detected in intestine and liver (at protein level).
CC {ECO:0000269|PubMed:632283}.
CC -!- PTM: Palmitoylated; structural requirement for proper assembly of the
CC hydrophobic core of the lipoprotein particle. {ECO:0000250}.
CC -!- RNA EDITING: Modified_positions=2147 {ECO:0000269|PubMed:2911593};
CC Note=The stop codon (UAA) at position 2147 is created by RNA editing.
CC Apo B-48, derived from the fully edited RNA, is produced only in the
CC intestine and is found in chylomicrons. Apo B-48 is a shortened form of
CC apo B-100 which lacks the LDL-receptor region. The unedited version
CC (apo B-100) is produced by the liver and is found in the VLDL and LDL.;
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DR EMBL; AY318958; AAP85369.1; -; mRNA.
DR EMBL; AY321317; AAP86249.1; -; mRNA.
DR RefSeq; NP_062160.2; NM_019287.2.
DR SMR; Q7TMA5; -.
DR BioGRID; 248449; 1.
DR DIP; DIP-29910N; -.
DR IntAct; Q7TMA5; 20.
DR STRING; 10116.ENSRNOP00000039779; -.
DR CarbonylDB; Q7TMA5; -.
DR GlyGen; Q7TMA5; 21 sites.
DR iPTMnet; Q7TMA5; -.
DR PhosphoSitePlus; Q7TMA5; -.
DR jPOST; Q7TMA5; -.
DR PaxDb; Q7TMA5; -.
DR PRIDE; Q7TMA5; -.
DR GeneID; 54225; -.
DR KEGG; rno:54225; -.
DR CTD; 338; -.
DR RGD; 2129; Apob.
DR VEuPathDB; HostDB:ENSRNOG00000005542; -.
DR eggNOG; KOG0654; Eukaryota.
DR eggNOG; KOG4338; Eukaryota.
DR InParanoid; Q7TMA5; -.
DR OMA; DYEMMIK; -.
DR OrthoDB; 5350at2759; -.
DR PhylomeDB; Q7TMA5; -.
DR TreeFam; TF331316; -.
DR Reactome; R-RNO-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-RNO-3000471; Scavenging by Class B Receptors.
DR Reactome; R-RNO-3000480; Scavenging by Class A Receptors.
DR Reactome; R-RNO-3000497; Scavenging by Class H Receptors.
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-432142; Platelet sensitization by LDL.
DR Reactome; R-RNO-5686938; Regulation of TLR by endogenous ligand.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-8866423; VLDL assembly.
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR Reactome; R-RNO-8963888; Chylomicron assembly.
DR Reactome; R-RNO-8963901; Chylomicron remodeling.
DR Reactome; R-RNO-8964026; Chylomicron clearance.
DR Reactome; R-RNO-8964038; LDL clearance.
DR Reactome; R-RNO-8964041; LDL remodeling.
DR Reactome; R-RNO-8964046; VLDL clearance.
DR Reactome; R-RNO-9707616; Heme signaling.
DR Reactome; R-RNO-975634; Retinoid metabolism and transport.
DR PRO; PR:Q7TMA5; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Bgee; ENSRNOG00000005542; Expressed in liver and 12 other tissues.
DR ExpressionAtlas; Q7TMA5; baseline and differential.
DR Genevisible; Q7TMA5; RN.
DR GO; GO:0042627; C:chylomicron; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR GO; GO:0070971; C:endoplasmic reticulum exit site; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0034364; C:high-density lipoprotein particle; IDA:RGD.
DR GO; GO:0034363; C:intermediate-density lipoprotein particle; ISO:RGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0005811; C:lipid droplet; IEA:UniProtKB-SubCell.
DR GO; GO:0034362; C:low-density lipoprotein particle; IDA:RGD.
DR GO; GO:0034359; C:mature chylomicron; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0034361; C:very-low-density lipoprotein particle; IDA:RGD.
DR GO; GO:0031983; C:vesicle lumen; IDA:RGD.
DR GO; GO:0012506; C:vesicle membrane; IDA:RGD.
DR GO; GO:0120020; F:cholesterol transfer activity; ISO:RGD.
DR GO; GO:0008201; F:heparin binding; ISO:RGD.
DR GO; GO:0035473; F:lipase binding; ISO:RGD.
DR GO; GO:0050750; F:low-density lipoprotein particle receptor binding; ISO:RGD.
DR GO; GO:0005543; F:phospholipid binding; ISO:RGD.
DR GO; GO:0048844; P:artery morphogenesis; ISO:RGD.
DR GO; GO:0071379; P:cellular response to prostaglandin stimulus; IEP:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0033344; P:cholesterol efflux; ISO:RGD.
DR GO; GO:0042632; P:cholesterol homeostasis; ISO:RGD.
DR GO; GO:0008203; P:cholesterol metabolic process; ISO:RGD.
DR GO; GO:0030301; P:cholesterol transport; ISO:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0009566; P:fertilization; ISO:RGD.
DR GO; GO:0030317; P:flagellated sperm motility; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0016042; P:lipid catabolic process; ISO:RGD.
DR GO; GO:0006629; P:lipid metabolic process; IDA:RGD.
DR GO; GO:0042158; P:lipoprotein biosynthetic process; ISO:RGD.
DR GO; GO:0042159; P:lipoprotein catabolic process; ISO:RGD.
DR GO; GO:0042157; P:lipoprotein metabolic process; ISO:RGD.
DR GO; GO:0042953; P:lipoprotein transport; ISO:RGD.
DR GO; GO:0034383; P:low-density lipoprotein particle clearance; ISO:RGD.
DR GO; GO:0034374; P:low-density lipoprotein particle remodeling; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0010886; P:positive regulation of cholesterol storage; ISO:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR GO; GO:0010884; P:positive regulation of lipid storage; ISO:RGD.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:0045540; P:regulation of cholesterol biosynthetic process; ISO:RGD.
DR GO; GO:0009743; P:response to carbohydrate; IDA:RGD.
DR GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0010033; P:response to organic substance; IEP:RGD.
DR GO; GO:0010269; P:response to selenium ion; IEP:RGD.
DR GO; GO:0009615; P:response to virus; ISO:RGD.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR GO; GO:0019433; P:triglyceride catabolic process; IMP:RGD.
DR GO; GO:0006642; P:triglyceride mobilization; ISO:RGD.
DR CDD; cd00043; CYCLIN; 1.
DR Gene3D; 1.25.10.20; -; 1.
DR Gene3D; 2.30.230.10; -; 1.
DR InterPro; IPR022176; ApoB100_C.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR015819; Lipid_transp_b-sht_shell.
DR InterPro; IPR009454; Lipid_transpt_open_b-sht.
DR InterPro; IPR011030; Lipovitellin_superhlx_dom.
DR InterPro; IPR015816; Vitellinogen_b-sht_N.
DR InterPro; IPR015255; Vitellinogen_open_b-sht.
DR InterPro; IPR001747; Vitellogenin_N.
DR Pfam; PF12491; ApoB100_C; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR Pfam; PF06448; DUF1081; 1.
DR Pfam; PF09172; DUF1943; 1.
DR Pfam; PF01347; Vitellogenin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SMART; SM01169; DUF1943; 1.
DR SMART; SM00638; LPD_N; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
DR SUPFAM; SSF48431; SSF48431; 1.
DR SUPFAM; SSF56968; SSF56968; 2.
DR PROSITE; PS51211; VITELLOGENIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Atherosclerosis; Cholesterol metabolism; Chylomicron;
KW Cytoplasm; Disulfide bond; Glycoprotein; Heparin-binding; LDL;
KW Lipid droplet; Lipid metabolism; Lipid transport; Lipoprotein; Palmitate;
KW Phosphoprotein; Reference proteome; RNA editing; Secreted; Signal;
KW Steroid metabolism; Sterol metabolism; Transport; VLDL.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..4743
FT /note="Apolipoprotein B-100"
FT /id="PRO_0000293536"
FT CHAIN 28..2146
FT /note="Apolipoprotein B-48"
FT /id="PRO_0000293537"
FT DOMAIN 33..660
FT /note="Vitellogenin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT REGION 29..113
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 219..293
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 890..947
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 2010..2145
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 3123..3198
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 3136..3146
FT /note="Basic (possible receptor binding region)"
FT /evidence="ECO:0000250"
FT REGION 3336..3356
FT /note="LDL receptor binding"
FT /evidence="ECO:0000250"
FT REGION 3346..3479
FT /note="Heparin-binding"
FT /evidence="ECO:0000250"
FT REGION 3349..3357
FT /note="Basic (possible receptor binding region)"
FT /evidence="ECO:0000250"
FT MOD_RES 1973
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P04114"
FT MOD_RES 2006
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 3981
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04114"
FT MOD_RES 3985
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P04114"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 971
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1491
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2662
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2791
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2897
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2944
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3063
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3186
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3715
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3828
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 4232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 65..84
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 173..199
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 232..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 372..377
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 466..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
FT DISULFID 954..964
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00557"
SQ 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
