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Database: UniProt
Entry: Q8IW19
LinkDB: Q8IW19
Original site: Q8IW19 
ID   APLF_HUMAN              Reviewed;         511 AA.
AC   Q8IW19; A8K476; Q53P47; Q53PB9; Q53QU0;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   01-OCT-2014, entry version 98.
DE   RecName: Full=Aprataxin and PNK-like factor;
DE            EC=4.2.99.18;
DE   AltName: Full=Apurinic-apyrimidinic endonuclease APLF;
DE   AltName: Full=PNK and APTX-like FHA domain-containing protein;
DE   AltName: Full=XRCC1-interacting protein 1;
GN   Name=APLF; Synonyms=C2orf13, PALF, XIP1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
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   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION,
RP   POLY-ADP-RIBOSYLATION, AND INTERACTION WITH LIG4; PARP1; XRCC4 AND
RP   XRCC5.
RX   PubMed=17396150; DOI=10.1038/sj.emboj.7601663;
RA   Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S.,
RA   Yasui A.;
RT   "A novel human AP endonuclease with conserved zinc-finger-like motifs
RT   involved in DNA strand break responses.";
RL   EMBO J. 26:2094-2103(2007).
RN   [5]
RP   SUBCELLULAR LOCATION, INTERACTION WITH XRCC1, PHOSPHORYLATION AT
RP   SER-116, AND MUTAGENESIS OF SER-116.
RX   PubMed=17507382; DOI=10.1074/jbc.C700060200;
RA   Bekker-Jensen S., Fugger K., Danielsen J.R., Gromova I., Sehested M.,
RA   Celis J., Bartek J., Lukas J., Mailand N.;
RT   "Human Xip1 (C2orf13) is a novel regulator of cellular responses to
RT   DNA strand breaks.";
RL   J. Biol. Chem. 282:19638-19643(2007).
RN   [6]
RP   FUNCTION, INTERACTION WITH PARP1; XRCC1; XRCC4 AND XRCC5, SUBCELLULAR
RP   LOCATION, AND PHOSPHORYLATION.
RX   PubMed=17353262; DOI=10.1128/MCB.02269-06;
RA   Iles N., Rulten S., El-Khamisy S.F., Caldecott K.W.;
RT   "APLF (C2orf13) is a novel human protein involved in the cellular
RT   response to chromosomal DNA strand breaks.";
RL   Mol. Cell. Biol. 27:3793-3803(2007).
RN   [7]
RP   INTERACTION WITH XRCC4, AND PHOSPHORYLATION.
RX   PubMed=18077224; DOI=10.1016/j.dnarep.2007.10.008;
RA   Macrae C.J., McCulloch R.D., Ylanko J., Durocher D., Koch C.A.;
RT   "APLF (C2orf13) facilitates nonhomologous end-joining and undergoes
RT   ATM-dependent hyperphosphorylation following ionizing radiation.";
RL   DNA Repair 7:292-302(2008).
RN   [8]
RP   SUBCELLULAR LOCATION, AND ADP-RIBOSE-BINDING.
RX   PubMed=18474613; DOI=10.1128/MCB.02243-07;
RA   Rulten S.L., Cortes-Ledesma F., Guo L., Iles N.J., Caldecott K.W.;
RT   "APLF (C2orf13) is a novel component of poly(ADP-ribose) signaling in
RT   mammalian cells.";
RL   Mol. Cell. Biol. 28:4620-4628(2008).
RN   [9]
RP   SUBCELLULAR LOCATION, DOMAIN PBZ-TYPE, POLY-ADP-RIBOSYLATION,
RP   ADP-RIBOSE-BINDING, AND MUTAGENESIS OF ARG-376; CYS-379; CYS-385;
RP   CYS-421 AND CYS-427.
RX   PubMed=18172500; DOI=10.1038/nature06420;
RA   Ahel I., Ahel D., Matsusaka T., Clark A.J., Pines J., Boulton S.J.,
RA   West S.C.;
RT   "Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint
RT   proteins.";
RL   Nature 451:81-85(2008).
RN   [10]
RP   STRUCTURE BY NMR OF 368-451 ALONE AND IN COMPLEX WITH ADP-RIBOSE
RP   ANALOG, AND POLY-ADP-RIBOSE BINDING SITES.
RX   PubMed=20098424; DOI=10.1038/nsmb.1747;
RA   Eustermann S., Brockmann C., Mehrotra P.V., Yang J.C., Loakes D.,
RA   West S.C., Ahel I., Neuhaus D.;
RT   "Solution structures of the two PBZ domains from human APLF and their
RT   interaction with poly(ADP-ribose).";
RL   Nat. Struct. Mol. Biol. 17:241-243(2010).
RN   [11]
RP   STRUCTURE BY NMR OF 360-448, LINKER REGION, AND POLY-ADP-RIBOSE
RP   BINDING SITES.
RX   PubMed=20439749; DOI=10.1073/pnas.1000556107;
RA   Li G.Y., McCulloch R.D., Fenton A.L., Cheung M., Meng L., Ikura M.,
RA   Koch C.A.;
RT   "Structure and identification of ADP-ribose recognition motifs of APLF
RT   and role in the DNA damage response.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:9129-9134(2010).
CC   -!- FUNCTION: Nuclease involved in single-strand and double-strand DNA
CC       break repair. Recruited to sites of DNA damage through interaction
CC       with poly(ADP-ribose), a polymeric post-translational modification
CC       synthesized transiently at sites of chromosomal damage to
CC       accelerate DNA strand break repair reactions. Displays apurinic-
CC       apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in
CC       vitro. Also able to introduce nicks at hydroxyuracil and other
CC       types of pyrimidine base damage. {ECO:0000269|PubMed:17353262,
CC       ECO:0000269|PubMed:17396150}.
CC   -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or
CC       apyrimidinic site in DNA is broken by a beta-elimination reaction,
CC       leaving a 3'-terminal unsaturated sugar and a product with a
CC       terminal 5'-phosphate. {ECO:0000269|PubMed:17396150}.
CC   -!- SUBUNIT: Interacts with LIG4, PARP1, XRCC1, XRCC4 and XRCC5.
CC       {ECO:0000269|PubMed:17353262, ECO:0000269|PubMed:17396150,
CC       ECO:0000269|PubMed:17507382, ECO:0000269|PubMed:18077224,
CC       ECO:0000269|PubMed:20098424}.
CC   -!- INTERACTION:
CC       P49917:LIG4; NbExp=2; IntAct=EBI-1256044, EBI-847896;
CC       P09874:PARP1; NbExp=3; IntAct=EBI-1256044, EBI-355676;
CC       P18887:XRCC1; NbExp=10; IntAct=EBI-1256044, EBI-947466;
CC       Q13426:XRCC4; NbExp=4; IntAct=EBI-1256044, EBI-717592;
CC       P13010:XRCC5; NbExp=12; IntAct=EBI-1256044, EBI-357997;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Note=Localizes
CC       to DNA damage sites. Accumulates at single-strand breaks and
CC       double-strand breaks via the PBZ-type zinc fingers.
CC   -!- DOMAIN: The PBZ-type zinc fingers (also named CYR) mediate non-
CC       covalent poly(ADP-ribose)-binding. Poly(ADP-ribose)-binding is
CC       dependent on the presence of zinc and promotes its recruitment to
CC       DNA damage sites. {ECO:0000269|PubMed:18172500}.
CC   -!- DOMAIN: The FHA-like domain mediates interaction with XRCC1 and
CC       XRCC4. {ECO:0000269|PubMed:18172500}.
CC   -!- PTM: Poly-ADP-ribosylated. In addition to binding non covalently
CC       poly(ADP-ribose) via its PBZ-type zinc fingers, the protein is
CC       also covalently poly-ADP-ribosylated by PARP1.
CC   -!- PTM: Phosphorylated in an ATM-dependent manner upon double-strand
CC       DNA break. {ECO:0000269|PubMed:17353262,
CC       ECO:0000269|PubMed:17507382, ECO:0000269|PubMed:18077224}.
CC   -!- SIMILARITY: Belongs to the APLF family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 FHA-like domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 2 PBZ-type zinc fingers. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY14945.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK290841; BAF83530.1; -; mRNA.
DR   EMBL; AC105054; AAY24113.1; -; Genomic_DNA.
DR   EMBL; AC127383; AAY24008.1; -; Genomic_DNA.
DR   EMBL; AC130709; AAY14945.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BC041144; AAH41144.1; -; mRNA.
DR   CCDS; CCDS1888.1; -.
DR   RefSeq; NP_775816.1; NM_173545.2.
DR   UniGene; Hs.720369; -.
DR   PDB; 2KQB; NMR; -; A=368-451.
DR   PDB; 2KQC; NMR; -; A=368-451.
DR   PDB; 2KQD; NMR; -; A=368-451.
DR   PDB; 2KQE; NMR; -; A=368-451.
DR   PDB; 2KUO; NMR; -; A=360-448.
DR   PDBsum; 2KQB; -.
DR   PDBsum; 2KQC; -.
DR   PDBsum; 2KQD; -.
DR   PDBsum; 2KQE; -.
DR   PDBsum; 2KUO; -.
DR   ProteinModelPortal; Q8IW19; -.
DR   SMR; Q8IW19; 359-451.
DR   BioGrid; 128334; 8.
DR   DIP; DIP-39136N; -.
DR   IntAct; Q8IW19; 14.
DR   MINT; MINT-3037419; -.
DR   STRING; 9606.ENSP00000307004; -.
DR   PhosphoSite; Q8IW19; -.
DR   DMDM; 73619699; -.
DR   MaxQB; Q8IW19; -.
DR   PaxDb; Q8IW19; -.
DR   PRIDE; Q8IW19; -.
DR   Ensembl; ENST00000303795; ENSP00000307004; ENSG00000169621.
DR   GeneID; 200558; -.
DR   KEGG; hsa:200558; -.
DR   UCSC; uc002sep.3; human.
DR   CTD; 200558; -.
DR   GeneCards; GC02P068694; -.
DR   HGNC; HGNC:28724; APLF.
DR   HPA; HPA034642; -.
DR   HPA; HPA034643; -.
DR   MIM; 611035; gene.
DR   neXtProt; NX_Q8IW19; -.
DR   PharmGKB; PA164715842; -.
DR   eggNOG; NOG85452; -.
DR   HOGENOM; HOG000033995; -.
DR   HOVERGEN; HBG095728; -.
DR   InParanoid; Q8IW19; -.
DR   KO; K13295; -.
DR   OMA; HIINCES; -.
DR   OrthoDB; EOG73805W; -.
DR   PhylomeDB; Q8IW19; -.
DR   TreeFam; TF326160; -.
DR   ChiTaRS; APLF; human.
DR   EvolutionaryTrace; Q8IW19; -.
DR   GenomeRNAi; 200558; -.
DR   NextBio; 89940; -.
DR   PRO; PR:Q8IW19; -.
DR   ArrayExpress; Q8IW19; -.
DR   Bgee; Q8IW19; -.
DR   CleanEx; HS_APLF; -.
DR   Genevestigator; Q8IW19; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; IDA:MGI.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IDA:UniProtKB.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IDA:UniProtKB.
DR   GO; GO:0004520; F:endodeoxyribonuclease activity; IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR   GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IDA:GOC.
DR   GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IDA:GOC.
DR   GO; GO:0051106; P:positive regulation of DNA ligation; IGI:MGI.
DR   GO; GO:0000012; P:single strand break repair; IMP:UniProtKB.
DR   Gene3D; 2.60.200.20; -; 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_domain.
DR   InterPro; IPR019406; Znf_C2H2_APLF-like.
DR   Pfam; PF10283; zf-CCHH; 2.
DR   SUPFAM; SSF49879; SSF49879; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Coiled coil; Complete proteome;
KW   Cytoplasm; DNA damage; DNA repair; Lyase; Metal-binding;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN         1    511       Aprataxin and PNK-like factor.
FT                                /FTId=PRO_0000089342.
FT   DOMAIN        1    108       FHA-like.
FT   ZN_FING     377    398       PBZ-type 1.
FT   ZN_FING     419    440       PBZ-type 2.
FT   REGION      406    416       Flexible linker.
FT   COILED      487    511       {ECO:0000255}.
FT   BINDING     376    376       Poly-ADP-ribose.
FT   BINDING     381    381       Poly-ADP-ribose.
FT   BINDING     386    386       Poly-ADP-ribose.
FT   BINDING     387    387       Poly-ADP-ribose.
FT   BINDING     423    423       Poly-ADP-ribose.
FT   BINDING     428    428       Poly-ADP-ribose.
FT   BINDING     429    429       Poly-ADP-ribose.
FT   MOD_RES     116    116       Phosphoserine; by ATM.
FT                                {ECO:0000269|PubMed:17507382}.
FT   VARIANT     100    100       I -> V (in dbSNP:rs11902811).
FT                                /FTId=VAR_032299.
FT   VARIANT     224    224       S -> T (in dbSNP:rs35002937).
FT                                /FTId=VAR_061557.
FT   VARIANT     336    336       L -> F (in dbSNP:rs13404469).
FT                                /FTId=VAR_032300.
FT   MUTAGEN     116    116       S->A: Decreases phosphorylation by ATM.
FT                                {ECO:0000269|PubMed:17507382}.
FT   MUTAGEN     376    376       R->A: Abolishes poly(ADP-ribose)-binding
FT                                and poly-ADP-ribosylation by PARP1; when
FT                                associated with A-421 and A-427.
FT                                {ECO:0000269|PubMed:18172500}.
FT   MUTAGEN     379    379       C->A: Abolishes poly(ADP-ribose)-binding
FT                                and poly-ADP-ribosylation by PARP1; when
FT                                associated with A-385; A-421 and A-427.
FT                                {ECO:0000269|PubMed:18172500}.
FT   MUTAGEN     385    385       C->A: Abolishes poly(ADP-ribose)-binding
FT                                and poly-ADP-ribosylation by PARP1; when
FT                                associated with A-379; A-421 and A-427.
FT                                {ECO:0000269|PubMed:18172500}.
FT   MUTAGEN     421    421       C->A: Abolishes poly(ADP-ribose)-binding
FT                                and poly-ADP-ribosylation by PARP1; when
FT                                associated with A-379; A-385 and A-427.
FT                                Abolishes poly(ADP-ribose)-binding and
FT                                poly-ADP-ribosylation by PARP1; when
FT                                associated with A-376 and A-427.
FT                                {ECO:0000269|PubMed:18172500}.
FT   MUTAGEN     427    427       C->A: Abolishes poly(ADP-ribose)-binding
FT                                and poly-ADP-ribosylation by PARP1; when
FT                                associated with A-379; A-385 and A-421.
FT                                Abolishes poly(ADP-ribose)-binding and
FT                                poly-ADP-ribosylation by PARP1; when
FT                                associated with A-376 and A-421.
FT                                {ECO:0000269|PubMed:18172500}.
FT   CONFLICT    313    313       Missing (in Ref. 1; BAF83530).
FT                                {ECO:0000305}.
FT   STRAND      371    374
FT   TURN        380    383
FT   HELIX       392    395
FT   TURN        412    414
FT   HELIX       424    426
FT   HELIX       432    437
SQ   SEQUENCE   511 AA;  56956 MW;  CBBF0096843298DA CRC64;
     MSGGFELQPR DGGPRVALAP GETVIGRGPL LGITDKRVSR RHAILEVAGG QLRIKPIHTN
     PCFYQSSEKS QLLPLKPNLW CYLNPGDSFS LLVDKYIFRI LSIPSEVEMQ CTLRNSQVLD
     EDNILNETPK SPVINLPHET TGASQLEGST EIAKTQMTPT NSVSFLGENR DCNKQQPILA
     ERKRILPTWM LAEHLSDQNL SVPAISGGNV IQGSGKEEIC KDKSQLNTTQ QGRRQLISSG
     SSENTSAEQD TGEECKNTDQ EESTISSKEM PQSFSAITLS NTEMNNIKTN AQRNKLPIEE
     LGKVSKHKIA TKRTPHKEDE AMSCSENCSS AQGDSLQDES QGSHSESSSN PSNPETLHAK
     ATDSVLQGSE GNKVKRTSCM YGANCYRKNP VHFQHFSHPG DSDYGGVQIV GQDETDDRPE
     CPYGPSCYRK NPQHKIEYRH NTLPVRNVLD EDNDNVGQPN EYDLNDSFLD DEEEDYEPTD
     EDSDWEPGKE DEEKEDVEEL LKEAKRFMKR K
//
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