ID ABEC3_MOUSE Reviewed; 429 AA. AC Q99J72; Q8C7L0; Q8C8V7; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 2. DT 26-NOV-2014, entry version 105. DE RecName: Full=DNA dC->dU-editing enzyme APOBEC-3; DE EC=3.5.4.-; DE AltName: Full=Apolipoprotein B mRNA-editing complex 3; DE Short=Arp3; DE AltName: Full=CEM-15; DE Short=CEM15; GN Name=Apobec3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND RP VARIANTS ARG-34; 37-ILE-ASP-38; 112-VAL-LEU-113; 134-ILE-ARG-135; RP ASN-139; LYS-181; 233-VAL-HIS-LEU-235; GLY-258; ILE-306 AND HIS-404. RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Retina; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORM 4), AND VARIANTS. RC STRAIN=C57BL/6J; TISSUE=Spleen; RA Mariani R., Landau N.R.; RL Submitted (FEB-2004) to UniProtKB. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12466850; DOI=10.1038/nature01262; RA Waterston R.H., Lindblad-Toh K., Birney E., Rogers J., Abril J.F., RA Agarwal P., Agarwala R., Ainscough R., Alexandersson M., An P., RA Antonarakis S.E., Attwood J., Baertsch R., Bailey J., Barlow K., RA Beck S., Berry E., Birren B., Bloom T., Bork P., Botcherby M., RA Bray N., Brent M.R., Brown D.G., Brown S.D., Bult C., Burton J., RA Butler J., Campbell R.D., Carninci P., Cawley S., Chiaromonte F., RA Chinwalla A.T., Church D.M., Clamp M., Clee C., Collins F.S., RA Cook L.L., Copley R.R., Coulson A., Couronne O., Cuff J., Curwen V., RA Cutts T., Daly M., David R., Davies J., Delehaunty K.D., Deri J., RA Dermitzakis E.T., Dewey C., Dickens N.J., Diekhans M., Dodge S., RA Dubchak I., Dunn D.M., Eddy S.R., Elnitski L., Emes R.D., Eswara P., RA Eyras E., Felsenfeld A., Fewell G.A., Flicek P., Foley K., RA Frankel W.N., Fulton L.A., Fulton R.S., Furey T.S., Gage D., RA Gibbs R.A., Glusman G., Gnerre S., Goldman N., Goodstadt L., RA Grafham D., Graves T.A., Green E.D., Gregory S., Guigo R., Guyer M., RA Hardison R.C., Haussler D., Hayashizaki Y., Hillier L.W., Hinrichs A., RA Hlavina W., Holzer T., Hsu F., Hua A., Hubbard T., Hunt A., RA Jackson I., Jaffe D.B., Johnson L.S., Jones M., Jones T.A., Joy A., RA Kamal M., Karlsson E.K., Karolchik D., Kasprzyk A., Kawai J., RA Keibler E., Kells C., Kent W.J., Kirby A., Kolbe D.L., Korf I., RA Kucherlapati R.S., Kulbokas E.J., Kulp D., Landers T., Leger J.P., RA Leonard S., Letunic I., Levine R., Li J., Li M., Lloyd C., Lucas S., RA Ma B., Maglott D.R., Mardis E.R., Matthews L., Mauceli E., Mayer J.H., RA McCarthy M., McCombie W.R., McLaren S., McLay K., McPherson J.D., RA Meldrim J., Meredith B., Mesirov J.P., Miller W., Miner T.L., RA Mongin E., Montgomery K.T., Morgan M., Mott R., Mullikin J.C., RA Muzny D.M., Nash W.E., Nelson J.O., Nhan M.N., Nicol R., Ning Z., RA Nusbaum C., O'Connor M.J., Okazaki Y., Oliver K., Overton-Larty E., RA Pachter L., Parra G., Pepin K.H., Peterson J., Pevzner P., Plumb R., RA Pohl C.S., Poliakov A., Ponce T.C., Ponting C.P., Potter S., Quail M., RA Reymond A., Roe B.A., Roskin K.M., Rubin E.M., Rust A.G., Santos R., RA Sapojnikov V., Schultz B., Schultz J., Schwartz M.S., Schwartz S., RA Scott C., Seaman S., Searle S., Sharpe T., Sheridan A., Shownkeen R., RA Sims S., Singer J.B., Slater G., Smit A., Smith D.R., Spencer B., RA Stabenau A., Stange-Thomann N., Sugnet C., Suyama M., Tesler G., RA Thompson J., Torrents D., Trevaskis E., Tromp J., Ucla C., RA Ureta-Vidal A., Vinson J.P., Von Niederhausern A.C., Wade C.M., RA Wall M., Weber R.J., Weiss R.B., Wendl M.C., West A.P., RA Wetterstrand K., Wheeler R., Whelan S., Wierzbowski J., Willey D., RA Williams S., Wilson R.K., Winter E., Worley K.C., Wyman D., Yang S., RA Yang S.P., Zdobnov E.M., Zody M.C., Lander E.S.; RT "Initial sequencing and comparative analysis of the mouse genome."; RL Nature 420:520-562(2002). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS RP ARG-34; 37-ILE-ASP-38; 112-VAL-LEU-113; 134-ILE-ARG-135; ASN-139; RP LYS-181; 233-VAL-HIS-LEU-235; GLY-258; ILE-306 AND HIS-404. RC TISSUE=Mammary tumor; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP DNA C TO U EDITING ACTIVITY, AND TISSUE SPECIFICITY. RX PubMed=12859895; DOI=10.1016/S0092-8674(03)00515-4; RA Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R., RA Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.; RT "Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif."; RL Cell 114:21-31(2003). RN [6] RP FUNCTION IN RETROTRANSPOSITION, AND SUBCELLULAR LOCATION. RX PubMed=16527742; DOI=10.1016/j.cub.2006.01.031; RA Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I., RA Landau N.R., Weitzman M.D.; RT "APOBEC3A is a potent inhibitor of adeno-associated virus and RT retrotransposons."; RL Curr. Biol. 16:480-485(2006). RN [7] RP DOMAIN CMP/DCMP DEAMINASE ZINC-BINDING, SUBUNIT, AND MUTAGENESIS OF RP GLU-73 AND GLU-290. RX PubMed=17020885; DOI=10.1074/jbc.M604980200; RA Hakata Y., Landau N.R.; RT "Reversed functional organization of mouse and human APOBEC3 cytidine RT deaminase domains."; RL J. Biol. Chem. 281:36624-36631(2006). RN [8] RP FUNCTION IN SFV RESTRICTION. RX PubMed=16378963; DOI=10.1128/JVI.80.2.605-614.2006; RA Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A., RA Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O.; RT "Restriction of foamy viruses by APOBEC cytidine deaminases."; RL J. Virol. 80:605-614(2006). RN [9] RP FUNCTION IN MMTV RESTRICTION, AND INTERACTION WITH MMTV NUCLEOCAPSID RP PROTEIN P14. RX PubMed=17259974; DOI=10.1038/nature05540; RA Okeoma C.M., Lovsin N., Peterlin B.M., Ross S.R.; RT "APOBEC3 inhibits mouse mammary tumour virus replication in vivo."; RL Nature 445:927-930(2007). RN [10] RP REVIEW. RX PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350; RA Chiu Y.L., Greene W.C.; RT "The APOBEC3 cytidine deaminases: an innate defensive network opposing RT exogenous retroviruses and endogenous retroelements."; RL Annu. Rev. Immunol. 26:317-353(2008). RN [11] RP FUNCTION IN FRMLV RESTRICTION. RX PubMed=18786991; DOI=10.1128/JVI.01311-08; RA Takeda E., Tsuji-Kawahara S., Sakamoto M., Langlois M.A., RA Neuberger M.S., Rada C., Miyazawa M.; RT "Mouse APOBEC3 restricts friend leukemia virus infection and RT pathogenesis in vivo."; RL J. Virol. 82:10998-11008(2008). CC -!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an CC inhibitor of retrovirus replication and retrotransposon mobility CC via deaminase-dependent and -independent mechanisms. Selectively CC targets single-stranded DNA and does not deaminate double-stranded CC DNA or single-or double-stranded RNA. Exhibits antiviral activity CC against HIV-1, simian immunodeficiency viruses (SIVs), mouse CC mammary tumor virus (MMTV) and friend murine leukemia virus CC (FrMLV) and may inhibit the mobility of LTR retrotransposons. CC {ECO:0000269|PubMed:16378963, ECO:0000269|PubMed:16527742, CC ECO:0000269|PubMed:17259974, ECO:0000269|PubMed:18786991}. CC -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer. Interacts with mouse mammary tumor virus CC (MMTV) nucleocapsid protein p14. {ECO:0000269|PubMed:17020885, CC ECO:0000269|PubMed:17259974}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16527742}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q99J72-1; Sequence=Displayed; CC Name=2; CC IsoId=Q99J72-2; Sequence=VSP_009832; CC Name=3; CC IsoId=Q99J72-3; Sequence=VSP_009831, VSP_009833; CC Name=4; CC IsoId=Q99J72-4; Sequence=VSP_009831; CC Note=Lacks exon V. Found in cell line MDTF.; CC -!- TISSUE SPECIFICITY: Expressed in spleen, node and lung. CC {ECO:0000269|PubMed:12859895}. CC -!- DOMAIN: The CMP/dCMP deaminase zinc-binding 1 domain confers CC deoxycytidine deaminase activity, whereas the CMP/dCMP deaminase CC zinc-binding 2 domain mediates RNA-dependent oligomerization and CC virion incorporation. {ECO:0000269|PubMed:17020885}. CC -!- MISCELLANEOUS: Probable human APOBEC3G ortholog. CC -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 CMP/dCMP deaminase zinc-binding domains. 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; AK044394; BAC31901.1; -; mRNA. DR EMBL; AK049998; BAC34023.1; -; mRNA. DR EMBL; AC113595; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC003314; AAH03314.1; -; mRNA. DR CCDS; CCDS27654.1; -. [Q99J72-4] DR CCDS; CCDS49669.1; -. [Q99J72-1] DR UniGene; Mm.284059; -. DR UniGene; Mm.432615; -. DR ProteinModelPortal; Q99J72; -. DR SMR; Q99J72; 26-197, 258-404. DR STRING; 10090.ENSMUSP00000105249; -. DR PhosphoSite; Q99J72; -. DR MaxQB; Q99J72; -. DR PRIDE; Q99J72; -. DR Ensembl; ENSMUST00000165537; ENSMUSP00000132391; ENSMUSG00000009585. [Q99J72-4] DR MGI; MGI:1933111; Apobec3. DR eggNOG; NOG135704; -. DR GeneTree; ENSGT00530000062933; -. DR HOGENOM; HOG000033755; -. DR HOVERGEN; HBG050434; -. DR InParanoid; Q99J72; -. DR PhylomeDB; Q99J72; -. DR PRO; PR:Q99J72; -. DR Bgee; Q99J72; -. DR CleanEx; MM_APOBEC3; -. DR ExpressionAtlas; Q99J72; baseline and differential. DR Genevestigator; Q99J72; -. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0016814; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB. DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR013158; APOBEC_N. DR InterPro; IPR016193; Cytidine_deaminase-like. DR Pfam; PF08210; APOBEC_N; 2. DR SUPFAM; SSF53927; SSF53927; 2. DR PROSITE; PS00903; CYT_DCMP_DEAMINASES; 2. PE 1: Evidence at protein level; KW Alternative splicing; Antiviral defense; Complete proteome; Cytoplasm; KW Hydrolase; Immunity; Innate immunity; Metal-binding; Polymorphism; KW Reference proteome; Repeat; Zinc. FT CHAIN 1 429 DNA dC->dU-editing enzyme APOBEC-3. FT /FTId=PRO_0000171772. FT DOMAIN 71 108 CMP/dCMP deaminase zinc-binding 1. FT DOMAIN 288 319 CMP/dCMP deaminase zinc-binding 2. FT ACT_SITE 73 73 Proton donor. {ECO:0000250}. FT METAL 71 71 Zinc. {ECO:0000250}. FT METAL 105 105 Zinc. {ECO:0000250}. FT METAL 108 108 Zinc. {ECO:0000250}. FT METAL 288 288 Zinc. {ECO:0000250}. FT METAL 316 316 Zinc. {ECO:0000250}. FT METAL 319 319 Zinc. {ECO:0000250}. FT VAR_SEQ 198 230 Missing (in isoform 3 and isoform 4). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_009831. FT VAR_SEQ 409 429 SWGLQDLVNDFGNLQLGPPMS -> VRTTLLQGPAS (in FT isoform 2). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_009832. FT VAR_SEQ 409 429 SWGLQDLVNDFGNLQLGPPMS -> SRSHAS (in FT isoform 3). FT {ECO:0000303|PubMed:16141072}. FT /FTId=VSP_009833. FT VARIANT 20 20 L -> V (in cell line MDTF). FT VARIANT 31 31 K -> E (in cell line MDTF). FT VARIANT 34 35 GY -> PF (in cell line MDTF). FT VARIANT 34 34 G -> R (in cell lines L1.2 and 3T3). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072}. FT VARIANT 37 38 KG -> ID (in cell lines L1.2 and 3T3). FT VARIANT 38 38 G -> K (in cell line MDTF; requires 2 FT nucleotide substitutions). FT VARIANT 111 111 Q -> R (in cell line L1.2). FT VARIANT 112 113 IV -> VL (in cell lines L1.2 and 3T3). FT VARIANT 112 112 I -> V (in cell line MDTF). FT VARIANT 128 128 S -> F (in cell line MDTF). FT VARIANT 134 139 VQDPET -> IRNPEN (in cell line MDTF). FT VARIANT 134 135 VQ -> IR (in cell lines L1.2 and 3T3). FT VARIANT 139 140 TQ -> NQL (in cell line 3T3). FT VARIANT 139 139 T -> N (in cell line L1.2). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072}. FT VARIANT 148 148 Q -> L (in cell line MDTF). FT VARIANT 162 163 KK -> EE (in cell line MDTF). FT VARIANT 181 181 R -> K (in cell lines L1.2 and 3T3). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072}. FT VARIANT 230 235 GRRMDP -> RRRVHL (in cell line 3T3). FT VARIANT 233 235 MDP -> VHL. FT VARIANT 234 235 DP -> SL (in cell line MDTF). FT VARIANT 248 248 Q -> L (in cell line MDTF). FT VARIANT 258 259 RM -> GV (in cell line 3T3). FT VARIANT 258 258 R -> G (in cell line L1.2). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072}. FT VARIANT 264 264 C -> F (in cell line MDTF). FT VARIANT 269 269 Q -> W (in cell line MDTF; requires 2 FT nucleotide substitutions). FT VARIANT 274 274 A -> E (in cell line MDTF). FT VARIANT 284 296 Missing (in cell line MDTF). FT VARIANT 306 306 T -> I (in cell lines L1.2 and 3T3). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072}. FT VARIANT 314 314 S -> G (in cell line EL4). FT VARIANT 328 328 R -> K (in cell line MDTF). FT VARIANT 381 381 N -> S (in cell line MDTF). FT VARIANT 387 387 W -> R (in splenocytes). FT VARIANT 394 395 II -> KT (in cell line MDTF). FT VARIANT 399 399 T -> A (in cell line L1.2). FT VARIANT 404 404 R -> C (in cell lines MDTF and 3T3). FT VARIANT 404 404 R -> H (in cell line L1.2). FT {ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:16141072}. FT MUTAGEN 73 73 E->A: Decrease in cytidine deaminase and FT antiviral activity. FT {ECO:0000269|PubMed:17020885}. FT MUTAGEN 73 73 E->A: Decrease in cytidine deaminase and FT antiviral activity; when associated with FT A-290. {ECO:0000269|PubMed:17020885}. FT MUTAGEN 290 290 E->A: Decrease in cytidine deaminase and FT antiviral activity; when associated with FT A-73. {ECO:0000269|PubMed:17020885}. FT MUTAGEN 290 290 E->A: No effect on cytidine deaminase and FT antiviral activity. FT {ECO:0000269|PubMed:17020885}. FT CONFLICT 203 203 P -> S (in Ref. 3; AC113595). FT {ECO:0000305}. FT CONFLICT 227 227 C -> W (in Ref. 3; AC113595). FT {ECO:0000305}. FT CONFLICT 230 230 G -> R (in Ref. 2; no nucleotide entry). FT {ECO:0000305}. FT CONFLICT 410 414 WGLQD -> RSHAS (in Ref. 1; BAC34023). FT {ECO:0000305}. SQ SEQUENCE 429 AA; 50948 MW; 2B4361CDD81C99E5 CRC64; MGPFCLGCSH RKCYSPIRNL ISQETFKFHF KNLGYAKGRK DTFLCYEVTR KDCDSPVSLH HGVFKNKDNI HAEICFLYWF HDKVLKVLSP REEFKITWYM SWSPCFECAE QIVRFLATHH NLSLDIFSSR LYNVQDPETQ QNLCRLVQEG AQVAAMDLYE FKKCWKKFVD NGGRRFRPWK RLLTNFRYQD SKLQEILRPC YIPVPSSSSS TLSNICLTKG LPETRFCVEG RRMDPLSEEE FYSQFYNQRV KHLCYYHRMK PYLCYQLEQF NGQAPLKGCL LSEKGKQHAE ILFLDKIRSM ELSQVTITCY LTWSPCPNCA WQLAAFKRDR PDLILHIYTS RLYFHWKRPF QKGLCSLWQS GILVDVMDLP QFTDCWTNFV NPKRPFWPWK GLEIISRRTQ RRLRRIKESW GLQDLVNDFG NLQLGPPMS //