POL_FIVPE
ID POL_FIVPE Reviewed; 1124 AA.
AC P16088;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Pol polyprotein;
DE Contains:
DE RecName: Full=Protease;
DE AltName: Full=Retropepsin;
DE EC=3.4.23.-;
DE Contains:
DE RecName: Full=Reverse transcriptase/ribonuclease H;
DE Short=RT;
DE EC=2.7.7.49;
DE EC=3.1.26.13;
DE AltName: Full=Exoribonuclease H;
DE EC=3.1.13.2;
DE Contains:
DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase;
DE Short=dUTPase;
DE EC=3.6.1.23;
DE Contains:
DE RecName: Full=Integrase;
DE Short=IN;
DE EC=2.7.7.- {ECO:0000250|UniProtKB:P04585};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P04585};
GN Name=pol;
OS Feline immunodeficiency virus (isolate Petaluma) (FIV).
OC Viruses; Riboviria; Pararnavirae; Artverviricota; Revtraviricetes;
OC Ortervirales; Retroviridae; Orthoretrovirinae; Lentivirus.
OX NCBI_TaxID=11674;
OH NCBI_TaxID=9681; Felidae (cat family).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Clone 34TF10;
RX PubMed=2762293; DOI=10.1073/pnas.86.15.5743;
RA Talbott R.L., Sparger E.E., Lovelace K.M., Fitch W.M., Pedersen N.C.,
RA Luciw P.A., Elder J.H.;
RT "Nucleotide sequence and genomic organization of feline immunodeficiency
RT virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:5743-5747(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC STRAIN=Clone FIV-14;
RX PubMed=2813380; DOI=10.1073/pnas.86.20.8088;
RA Olmsted R.A., Hirsch V.M., Purcell R.H., Johnson P.R.;
RT "Nucleotide sequence analysis of feline immunodeficiency virus: genome
RT organization and relationship to other lentiviruses.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:8088-8092(1989).
RN [3]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=8383214; DOI=10.1128/jvi.67.4.1869-1876.1993;
RA Elder J.H., Schnoelzer M., Hasselkus-Light C.S., Henson M., Lerner D.A.,
RA Phillips T.R., Wagaman P.C., Kent S.B.H.;
RT "Identification of proteolytic processing sites within the Gag and Pol
RT polyproteins of feline immunodeficiency virus.";
RL J. Virol. 67:1869-1876(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154.
RX PubMed=7664111; DOI=10.1038/nsb0695-480;
RA Wlodawer A., Gustchina A., Reshetnikova L., Lubkowski J., Zdanov J.A.,
RA Hui K.Y., Angleton E.L., Farmerie W.G., Goodenow M.M., Bhatt D., Zhang L.,
RA Dunn B.M.;
RT "Structure of an inhibitor complex of the proteinase from feline
RT immunodeficiency virus.";
RL Nat. Struct. Biol. 2:480-488(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 42-154.
RX PubMed=9271500; DOI=10.1021/bi9707436;
RA Laco G.S., Schalk-Hihi C., Lubkowski J., Morris G., Zdanov A., Olson A.,
RA Elder J.H., Wlodawer A., Gustchina A.;
RT "Crystal structures of the inactive D30N mutant of feline immunodeficiency
RT virus protease complexed with a substrate and an inhibitor.";
RL Biochemistry 36:10696-10708(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 711-827.
RX PubMed=8976551; DOI=10.1002/pro.5560051205;
RA Prasad G.S., Stura E.A., McRee D.E., Laco G.S., Hasselkus-Light C.,
RA Elder J.H., Stout C.D.;
RT "Crystal structure of dUTP pyrophosphatase from feline immunodeficiency
RT virus.";
RL Protein Sci. 5:2429-2437(1996).
CC -!- FUNCTION: During replicative cycle of retroviruses, the reverse-
CC transcribed viral DNA is integrated into the host chromosome by the
CC viral integrase enzyme. RNase H activity is associated with the reverse
CC transcriptase.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different
CC cleavage modes: 1. sequence-specific internal cleavage of RNA. Human
CC immunodeficiency virus type 1 and Moloney murine leukemia virus
CC enzymes prefer to cleave the RNA strand one nucleotide away from the
CC RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides
CC from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides
CC away from the primer terminus.; EC=3.1.26.13;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-end directed exonucleolytic cleavage of viral RNA-DNA
CC hybrid.; EC=3.1.13.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dUTP + H2O = diphosphate + dUMP + H(+); Xref=Rhea:RHEA:10248,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:61555, ChEBI:CHEBI:246422; EC=3.6.1.23;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405};
CC -!- PTM: Cleavage sites that yield the mature proteins remain to be
CC determined.
CC -!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
CC {ECO:0000305}.
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DR EMBL; M25381; AAB59937.1; ALT_SEQ; Genomic_RNA.
DR PIR; B33543; GNLJFP.
DR RefSeq; NP_040973.1; NC_001482.1.
DR PDB; 1B11; X-ray; 1.90 A; A=42-154.
DR PDB; 1DUT; X-ray; 1.90 A; A/B=711-843.
DR PDB; 1F7D; X-ray; 1.40 A; A/B=711-846.
DR PDB; 1F7K; X-ray; 2.20 A; A/B=711-846.
DR PDB; 1F7N; X-ray; 2.20 A; A/B=711-846.
DR PDB; 1F7O; X-ray; 2.20 A; A/B/C=711-846.
DR PDB; 1F7P; X-ray; 2.30 A; A/B/C=711-846.
DR PDB; 1F7Q; X-ray; 2.26 A; A/B/C=711-846.
DR PDB; 1F7R; X-ray; 2.50 A; A=711-846.
DR PDB; 1FIV; X-ray; 2.00 A; A=42-154.
DR PDB; 2FIV; X-ray; 2.00 A; A/B=39-154.
DR PDB; 2HAH; X-ray; 1.70 A; A=39-154.
DR PDB; 3FIV; X-ray; 1.85 A; A/B=39-154.
DR PDB; 3OGP; X-ray; 1.70 A; A/B=39-154.
DR PDB; 3OGQ; X-ray; 1.80 A; A/B=39-154.
DR PDB; 4FIV; X-ray; 1.80 A; A=42-154.
DR PDB; 4MQ3; X-ray; 1.08 A; A=904-1029.
DR PDB; 4PA1; X-ray; 1.84 A; A=904-1052.
DR PDB; 5FIV; X-ray; 1.90 A; A=42-154.
DR PDB; 6FIV; X-ray; 1.90 A; A=42-154.
DR PDBsum; 1B11; -.
DR PDBsum; 1DUT; -.
DR PDBsum; 1F7D; -.
DR PDBsum; 1F7K; -.
DR PDBsum; 1F7N; -.
DR PDBsum; 1F7O; -.
DR PDBsum; 1F7P; -.
DR PDBsum; 1F7Q; -.
DR PDBsum; 1F7R; -.
DR PDBsum; 1FIV; -.
DR PDBsum; 2FIV; -.
DR PDBsum; 2HAH; -.
DR PDBsum; 3FIV; -.
DR PDBsum; 3OGP; -.
DR PDBsum; 3OGQ; -.
DR PDBsum; 4FIV; -.
DR PDBsum; 4MQ3; -.
DR PDBsum; 4PA1; -.
DR PDBsum; 5FIV; -.
DR PDBsum; 6FIV; -.
DR SMR; P16088; -.
DR DrugBank; DB07365; 1-Naphthyl-L-alanine.
DR DrugBank; DB03800; Deoxyuridine monophosphate.
DR DrugBank; DB02333; Deoxyuridine-5'-Triphosphate.
DR DrugBank; DB08253; NAM NAPTHYLAMINOALANINE.
DR DrugBank; DB01891; Tl-3-093.
DR DrugBank; DB03435; Uridine-5'-Diphosphate.
DR MEROPS; A02.007; -.
DR GeneID; 1489989; -.
DR KEGG; vg:1489989; -.
DR BRENDA; 3.4.23.B4; 2231.
DR EvolutionaryTrace; P16088; -.
DR Proteomes; UP000242267; Genome.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004533; F:exoribonuclease H activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:InterPro.
DR GO; GO:0046081; P:dUTP catabolic process; IEA:InterPro.
DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR CDD; cd05482; HIV_retropepsin_like; 1.
DR CDD; cd07557; trimeric_dUTPase; 1.
DR Gene3D; 1.10.10.200; -; 1.
DR Gene3D; 2.30.30.10; -; 1.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 2.70.40.10; -; 1.
DR Gene3D; 3.30.420.10; -; 2.
DR Gene3D; 3.30.70.270; -; 3.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR008181; dUTPase.
DR InterPro; IPR029054; dUTPase-like.
DR InterPro; IPR036157; dUTPase-like_sf.
DR InterPro; IPR033704; dUTPase_trimeric.
DR InterPro; IPR017856; Integrase-like_N.
DR InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR InterPro; IPR001037; Integrase_C_retrovir.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR003308; Integrase_Zn-bd_dom_N.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR034170; Retropepsin-like_cat_dom.
DR InterPro; IPR018061; Retropepsins.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR010659; RVT_connect.
DR InterPro; IPR010661; RVT_thumb.
DR Pfam; PF00692; dUTPase; 1.
DR Pfam; PF00552; IN_DBD_C; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00077; RVP; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF06815; RVT_connect; 1.
DR Pfam; PF06817; RVT_thumb; 1.
DR SUPFAM; SSF46919; SSF46919; 1.
DR SUPFAM; SSF50122; SSF50122; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF51283; SSF51283; 1.
DR SUPFAM; SSF53098; SSF53098; 2.
DR SUPFAM; SSF56672; SSF56672; 1.
DR TIGRFAMs; TIGR00576; dut; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS51027; INTEGRASE_DBD; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50876; ZF_INTEGRASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aspartyl protease; DNA integration; DNA recombination;
KW DNA-binding; Endonuclease; Hydrolase; Metal-binding;
KW Multifunctional enzyme; Nuclease; Nucleotide metabolism;
KW Nucleotidyltransferase; Protease; Reference proteome;
KW RNA-directed DNA polymerase; Transferase; Viral genome integration;
KW Virus entry into host cell; Zinc; Zinc-finger.
FT CHAIN 1..154
FT /note="Protease"
FT /id="PRO_0000038841"
FT CHAIN 155..690
FT /note="Reverse transcriptase/ribonuclease H"
FT /id="PRO_0000038842"
FT CHAIN 691..843
FT /note="Deoxyuridine 5'-triphosphate nucleotidohydrolase"
FT /id="PRO_0000038843"
FT CHAIN 844..1124
FT /note="Integrase"
FT /id="PRO_0000038844"
FT DOMAIN 63..144
FT /note="Peptidase A2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00275"
FT DOMAIN 200..389
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 592..712
FT /note="RNase H type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT DOMAIN 899..1049
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT ZN_FING 848..889
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT DNA_BIND 1067..1115
FT /note="Integrase-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00506"
FT ACT_SITE 68
FT /note="For protease activity"
FT BINDING 601
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 601
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 634
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 654
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 704
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00408"
FT BINDING 857
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 861
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 885
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00450"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:3OGP"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3OGP"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:3OGP"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3FIV"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:3OGP"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3OGP"
FT STRAND 87..96
FT /evidence="ECO:0007829|PDB:3OGP"
FT STRAND 99..113
FT /evidence="ECO:0007829|PDB:3OGP"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3OGP"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:3OGP"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:3OGP"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:3OGP"
FT TURN 146..149
FT /evidence="ECO:0007829|PDB:3OGP"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3OGP"
FT STRAND 713..718
FT /evidence="ECO:0007829|PDB:1F7D"
FT STRAND 726..731
FT /evidence="ECO:0007829|PDB:1F7D"
FT STRAND 736..738
FT /evidence="ECO:0007829|PDB:1F7D"
FT STRAND 743..747
FT /evidence="ECO:0007829|PDB:1F7D"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:1F7N"
FT STRAND 758..763
FT /evidence="ECO:0007829|PDB:1F7D"
FT HELIX 766..769
FT /evidence="ECO:0007829|PDB:1F7D"
FT TURN 770..772
FT /evidence="ECO:0007829|PDB:1F7D"
FT STRAND 773..776
FT /evidence="ECO:0007829|PDB:1F7D"
FT STRAND 778..780
FT /evidence="ECO:0007829|PDB:1F7O"
FT STRAND 789..794
FT /evidence="ECO:0007829|PDB:1F7D"
FT STRAND 796..798
FT /evidence="ECO:0007829|PDB:1F7D"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:1F7D"
FT STRAND 807..815
FT /evidence="ECO:0007829|PDB:1F7D"
FT STRAND 830..832
FT /evidence="ECO:0007829|PDB:1F7R"
FT STRAND 905..913
FT /evidence="ECO:0007829|PDB:4MQ3"
FT STRAND 916..923
FT /evidence="ECO:0007829|PDB:4MQ3"
FT TURN 924..926
FT /evidence="ECO:0007829|PDB:4MQ3"
FT STRAND 929..935
FT /evidence="ECO:0007829|PDB:4MQ3"
FT HELIX 939..952
FT /evidence="ECO:0007829|PDB:4MQ3"
FT STRAND 956..961
FT /evidence="ECO:0007829|PDB:4MQ3"
FT TURN 964..966
FT /evidence="ECO:0007829|PDB:4MQ3"
FT HELIX 969..978
FT /evidence="ECO:0007829|PDB:4MQ3"
FT STRAND 981..986
FT /evidence="ECO:0007829|PDB:4MQ3"
FT TURN 990..992
FT /evidence="ECO:0007829|PDB:4MQ3"
FT HELIX 994..1010
FT /evidence="ECO:0007829|PDB:4MQ3"
FT HELIX 1011..1013
FT /evidence="ECO:0007829|PDB:4MQ3"
FT STRAND 1014..1016
FT /evidence="ECO:0007829|PDB:4MQ3"
FT HELIX 1017..1029
FT /evidence="ECO:0007829|PDB:4MQ3"
FT HELIX 1041..1051
FT /evidence="ECO:0007829|PDB:4PA1"
SQ SEQUENCE 1124 AA; 127494 MW; EE8214169BE39CF9 CRC64;
KEFGKLEGGA SCSPSESNAA SSNAICTSNG GETIGFVNYN KVGTTTTLEK RPEILIFVNG
YPIKFLLDTG ADITILNRRD FQVKNSIENG RQNMIGVGGG KRGTNYINVH LEIRDENYKT
QCIFGNVCVL EDNSLIQPLL GRDNMIKFNI RLVMAQISDK IPVVKVKMKD PNKGPQIKQW
PLTNEKIEAL TEIVERLEKE GKVKRADSNN PWNTPVFAIK KKSGKWRMLI DFRELNKLTE
KGAEVQLGLP HPAGLQIKKQ VTVLDIGDAY FTIPLDPDYA PYTAFTLPRK NNAGPGRRFV
WCSLPQGWIL SPLIYQSTLD NIIQPFIRQN PQLDIYQYMD DIYIGSNLSK KEHKEKVEEL
RKLLLWWGFE TPEDKLQEEP PYTWMGYELH PLTWTIQQKQ LDIPEQPTLN ELQKLAGKIN
WASQAIPDLS IKALTNMMRG NQNLNSTRQW TKEARLEVQK AKKAIEEQVQ LGYYDPSKEL
YAKLSLVGPH QISYQVYQKD PEKILWYGKM SRQKKKAENT CDIALRACYK IREESIIRIG
KEPRYEIPTS REAWESNLIN SPYLKAPPPE VEYIHAALNI KRALSMIKDA PIPGAETWYI
DGGRKLGKAA KAAYWTDTGK WRVMDLEGSN QKAEIQALLL ALKAGSEEMN IITDSQYVIN
IILQQPDMME GIWQEVLEEL EKKTAIFIDW VPGHKGIPGN EEVDKLCQTM MIIEGDGILD
KRSEDAGYDL LAAKEIHLLP GEVKVIPTGV KLMLPKGYWG LIIGKSSIGS KGLDVLGGVI
DEGYRGEIGV IMINVSRKSI TLMERQKIAQ LIILPCKHEV LEQGKVVMDS ERGDNGYGST
GVFSSWVDRI EEAEINHEKF HSDPQYLRTE FNLPKMVAEE IRRKCPVCRI IGEQVGGQLK
IGPGIWQMDC THFDGKIILV GIHVESGYIW AQIISQETAD CTVKAVLQLL SAHNVTELQT
DNGPNFKNQK MEGVLNYMGV KHKFGIPGNP QSQALVENVN HTLKVWIQKF LPETTSLDNA
LSLAVHSLNF KRRGRIGGMA PYELLAQQES LRIQDYFSAI PQKLQAQWIY YKDQKDKKWK
GPMRVEYWGQ GSVLLKDEEK GYFLIPRRHI RRVPEPCALP EGDE
