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 27-MAR-2024, entry version 175. 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; OC Feline immunodeficiency virus. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; Segment. 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; 2.70.40.10; -; 1. DR Gene3D; 3.30.70.270; -; 3. DR Gene3D; 2.40.70.10; Acid Proteases; 1. DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1. DR Gene3D; 2.30.30.10; Integrase, C-terminal domain superfamily, retroviral; 1. DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2. 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 NCBIfam; TIGR00576; dut; 1. DR PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1. DR PANTHER; PTHR41694:SF5; RIBONUCLEASE H; 1. 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; SSF50630; Acid proteases; 1. DR SUPFAM; SSF50122; DNA-binding domain of retroviral integrase; 1. DR SUPFAM; SSF56672; DNA/RNA polymerases; 1. DR SUPFAM; SSF51283; dUTPase-like; 1. DR SUPFAM; SSF46919; N-terminal Zn binding domain of HIV integrase; 1. DR SUPFAM; SSF53098; Ribonuclease H-like; 2. 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 //