PARP_DROME
ID PARP_DROME Reviewed; 994 AA.
AC P35875; A8Y590; Q7PLT6; Q8MSB5; Q8MU87; Q9W5Q5; Q9W5S1;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Poly [ADP-ribose] polymerase;
DE Short=PARP;
DE EC=2.4.2.30 {ECO:0000305|PubMed:17827147};
DE AltName: Full=NAD(+) ADP-ribosyltransferase;
DE Short=ADPRT;
DE AltName: Full=Poly[ADP-ribose] synthase;
DE AltName: Full=Protein ADP-ribosyltransferase Parp {ECO:0000250|UniProtKB:P09874};
DE EC=2.4.2.- {ECO:0000250|UniProtKB:P09874};
GN Name=Parp; ORFNames=CG40411;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM II).
RC TISSUE=Embryo;
RX PubMed=8475096; DOI=10.1073/pnas.90.8.3481;
RA Uchida K., Hanai S., Ishikawa K., Ozawa Y., Uchida M., Sugimura T.,
RA Miwa M.;
RT "Cloning of cDNA encoding Drosophila poly(ADP-ribose) polymerase: leucine
RT zipper in the auto-modification domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:3481-3485(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS I AND
RP II), TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=9565614; DOI=10.1074/jbc.273.19.11881;
RA Hanai S., Uchida M., Kobayashi S., Miwa M., Uchida K.;
RT "Genomic organization of Drosophila poly(ADP-ribose) polymerase and
RT distribution of its mRNA during development.";
RL J. Biol. Chem. 273:11881-11886(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM E), FUNCTION, SUBCELLULAR LOCATION, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12183365; DOI=10.1101/gad.1003902;
RA Tulin A., Stewart D., Spradling A.C.;
RT "The Drosophila heterochromatic gene encoding poly(ADP-ribose) polymerase
RT (PARP) is required to modulate chromatin structure during development.";
RL Genes Dev. 16:2108-2119(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-994 (ISOFORM II).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=17827147; DOI=10.1074/jbc.m705989200;
RA Pinnola A., Naumova N., Shah M., Tulin A.V.;
RT "Nucleosomal core histones mediate dynamic regulation of poly(ADP-ribose)
RT polymerase 1 protein binding to chromatin and induction of its enzymatic
RT activity.";
RL J. Biol. Chem. 282:32511-32519(2007).
CC -!- FUNCTION: Poly-ADP-ribosyltransferase that mediates poly-ADP-
CC ribosylation of proteins and plays a key role in DNA repair
CC (PubMed:17827147). Mediates glutamate, aspartate or serine ADP-
CC ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is
CC transferred to the acceptor carboxyl group of target residues and
CC further ADP-ribosyl groups are transferred to the 2'-position of the
CC terminal adenosine moiety, building up a polymer with an average chain
CC length of 20-30 units (By similarity). Mainly mediates glutamate and
CC aspartate ADP-ribosylation of target proteins in absence of CG1218/HPF1
CC (By similarity). Following interaction with CG1218/HPF1, catalyzes
CC serine ADP-ribosylation of target proteins; CG1218/HPF1 conferring
CC serine specificity by completing the Parp active site (By similarity).
CC {ECO:0000250|UniProtKB:P09874, ECO:0000269|PubMed:17827147}.
CC -!- FUNCTION: [Isoform E]: Plays a fundamental role in organizing chromatin
CC on a global scale (PubMed:12183365). Autoregulates Parp transcription
CC by influencing the chromatin structure of its heterochromatic
CC environment (PubMed:12183365). {ECO:0000269|PubMed:12183365}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-
CC ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30;
CC Evidence={ECO:0000305|PubMed:17827147};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + NAD(+) = H(+) + nicotinamide + O-(ADP-D-
CC ribosyl)-L-seryl-[protein]; Xref=Rhea:RHEA:58232, Rhea:RHEA-
CC COMP:9863, Rhea:RHEA-COMP:15091, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:29999, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:142556; Evidence={ECO:0000250|UniProtKB:P09874};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58233;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-
CC aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-
CC COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-
CC glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-
CC COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540;
CC Evidence={ECO:0000250|UniProtKB:P09874};
CC -!- INTERACTION:
CC P35875; Q24368: Iswi; NbExp=4; IntAct=EBI-266172, EBI-367628;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00264,
CC ECO:0000269|PubMed:12183365, ECO:0000269|PubMed:17827147}. Chromosome
CC {ECO:0000269|PubMed:17827147}. Nucleus, nucleolus
CC {ECO:0000269|PubMed:12183365}. Note=Highly enriched in nucleoli,
CC heterochromatic chromosomal regions, and diverse euchromatic sites in
CC the cells of most embryonic and adult tissues (PubMed:12183365).
CC Localizes in chromatin and nucleoplasm (PubMed:17827147).
CC {ECO:0000269|PubMed:12183365, ECO:0000269|PubMed:17827147}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=II; Synonyms=B, Long;
CC IsoId=P35875-1; Sequence=Displayed;
CC Name=I; Synonyms=Short;
CC IsoId=P35875-2; Sequence=VSP_004536;
CC Name=E; Synonyms=Embryonic;
CC IsoId=P35875-3; Sequence=VSP_013203, VSP_013204;
CC -!- TISSUE SPECIFICITY: Expressed in adult female oocytes, anal plates of
CC stage 12 embryos and in cells around the central nervous system in
CC later embryos. {ECO:0000269|PubMed:9565614}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
CC embryos, pupae and adults. Expression is highest in embryos.
CC {ECO:0000269|PubMed:12183365, ECO:0000269|PubMed:9565614}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50807.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; D13806; BAA02964.1; -; mRNA.
DR EMBL; AF051548; AAC24518.1; -; Genomic_DNA.
DR EMBL; AF051544; AAC24518.1; JOINED; Genomic_DNA.
DR EMBL; AF051545; AAC24518.1; JOINED; Genomic_DNA.
DR EMBL; AF051546; AAC24518.1; JOINED; Genomic_DNA.
DR EMBL; AF051547; AAC24518.1; JOINED; Genomic_DNA.
DR EMBL; AF533701; AAM93435.1; -; mRNA.
DR EMBL; AE014297; EDP28045.1; -; Genomic_DNA.
DR EMBL; BT015238; AAT94467.1; -; mRNA.
DR EMBL; AY118947; AAM50807.1; ALT_INIT; mRNA.
DR PIR; A47474; A47474.
DR RefSeq; NP_001104452.1; NM_001110982.3. [P35875-1]
DR AlphaFoldDB; P35875; -.
DR SMR; P35875; -.
DR BioGRID; 78234; 42.
DR DIP; DIP-23413N; -.
DR IntAct; P35875; 2.
DR STRING; 7227.FBpp0112608; -.
DR PaxDb; P35875; -.
DR DNASU; 3355109; -.
DR EnsemblMetazoa; FBtr0113885; FBpp0112608; FBgn0010247. [P35875-1]
DR GeneID; 3355109; -.
DR KEGG; dme:Dmel_CG40411; -.
DR CTD; 3355109; -.
DR FlyBase; FBgn0010247; Parp.
DR VEuPathDB; VectorBase:FBgn0010247; -.
DR eggNOG; KOG1037; Eukaryota.
DR GeneTree; ENSGT00940000156058; -.
DR HOGENOM; CLU_004841_0_1_1; -.
DR InParanoid; P35875; -.
DR OMA; RSAMMEF; -.
DR PhylomeDB; P35875; -.
DR BRENDA; 2.4.2.30; 1994.
DR Reactome; R-DME-110362; POLB-Dependent Long Patch Base Excision Repair.
DR Reactome; R-DME-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-DME-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DME-5685939; HDR through MMEJ (alt-NHEJ).
DR Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DME-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DME-5696400; Dual Incision in GG-NER.
DR BioGRID-ORCS; 3355109; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Parp; fly.
DR GenomeRNAi; 3355109; -.
DR PRO; PR:P35875; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0010247; Expressed in midgut and 12 other tissues.
DR GO; GO:0015030; C:Cajal body; IDA:FlyBase.
DR GO; GO:0005694; C:chromosome; IDA:FlyBase.
DR GO; GO:0000791; C:euchromatin; IDA:FlyBase.
DR GO; GO:0035363; C:histone locus body; IDA:FlyBase.
DR GO; GO:0005730; C:nucleolus; IDA:FlyBase.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0005703; C:polytene chromosome puff; IDA:FlyBase.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042393; F:histone binding; IPI:FlyBase.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IDA:FlyBase.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030576; P:Cajal body organization; IMP:FlyBase.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0008069; P:dorsal/ventral axis specification, ovarian follicular epithelium; IGI:FlyBase.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR GO; GO:0035080; P:heat shock-mediated polytene chromosome puffing; IMP:FlyBase.
DR GO; GO:0045087; P:innate immune response; IMP:FlyBase.
DR GO; GO:0051457; P:maintenance of protein location in nucleus; IMP:FlyBase.
DR GO; GO:0007000; P:nucleolus organization; IMP:FlyBase.
DR GO; GO:0035079; P:polytene chromosome puffing; TAS:FlyBase.
DR GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; IMP:FlyBase.
DR GO; GO:0061059; P:positive regulation of peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
DR GO; GO:1900182; P:positive regulation of protein localization to nucleus; IMP:CACAO.
DR GO; GO:0006471; P:protein ADP-ribosylation; IMP:FlyBase.
DR GO; GO:0070212; P:protein poly-ADP-ribosylation; IBA:GO_Central.
DR GO; GO:0043484; P:regulation of RNA splicing; IMP:FlyBase.
DR Gene3D; 1.20.142.10; -; 1.
DR Gene3D; 2.20.25.630; -; 1.
DR Gene3D; 3.30.1740.10; -; 2.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR012982; PADR1.
DR InterPro; IPR038650; PADR1_dom_sf.
DR InterPro; IPR008288; PARP.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004102; Poly(ADP-ribose)pol_reg_dom.
DR InterPro; IPR036616; Poly(ADP-ribose)pol_reg_dom_sf.
DR InterPro; IPR036930; WGR_dom_sf.
DR InterPro; IPR008893; WGR_domain.
DR InterPro; IPR001510; Znf_PARP.
DR InterPro; IPR036957; Znf_PARP_sf.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF08063; PADR1; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02877; PARP_reg; 1.
DR Pfam; PF05406; WGR; 1.
DR Pfam; PF00645; zf-PARP; 2.
DR PIRSF; PIRSF000489; NAD_ADPRT; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM01335; PADR1; 1.
DR SMART; SM00773; WGR; 1.
DR SMART; SM01336; zf-PARP; 2.
DR SUPFAM; SSF142921; SSF142921; 1.
DR SUPFAM; SSF47587; SSF47587; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS51060; PARP_ALPHA_HD; 1.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS00347; PARP_ZN_FINGER_1; 1.
DR PROSITE; PS50064; PARP_ZN_FINGER_2; 2.
DR PROSITE; PS51977; WGR; 1.
PE 1: Evidence at protein level;
KW ADP-ribosylation; Alternative splicing; Chromatin regulator; Chromosome;
KW DNA-binding; Glycosyltransferase; Metal-binding; NAD;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Repeat; Transferase;
KW Zinc; Zinc-finger.
FT CHAIN 1..994
FT /note="Poly [ADP-ribose] polymerase"
FT /id="PRO_0000211325"
FT DOMAIN 380..471
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT DOMAIN 525..622
FT /note="WGR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01321"
FT DOMAIN 644..761
FT /note="PARP alpha-helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00398"
FT DOMAIN 770..994
FT /note="PARP catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT ZN_FING 7..89
FT /note="PARP-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT ZN_FING 111..200
FT /note="PARP-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00264"
FT REGION 199..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..507
FT /note="Automodification domain"
FT MOTIF 208..210
FT /note="Nuclear localization signal"
FT MOTIF 223..228
FT /note="Nuclear localization signal"
FT COMPBIAS 202..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 971
FT /note="For poly [ADP-ribose] polymerase activity"
FT /evidence="ECO:0000250|UniProtKB:P09874"
FT VAR_SEQ 376..565
FT /note="Missing (in isoform I)"
FT /evidence="ECO:0000305"
FT /id="VSP_004536"
FT VAR_SEQ 607..613
FT /note="NEYEQRD -> MHFSEIH (in isoform E)"
FT /evidence="ECO:0000303|PubMed:12183365"
FT /id="VSP_013203"
FT VAR_SEQ 614..994
FT /note="Missing (in isoform E)"
FT /evidence="ECO:0000303|PubMed:12183365"
FT /id="VSP_013204"
SQ SEQUENCE 994 AA; 113792 MW; ACA85A270DD29E08 CRC64;
MDIELPYLAE YARTGRATCK GCKSTISKDT LRIAVMVQSA FHDAKVPNWF HKTCFFKNQR
PSSVGDIQNI GNLRFADQKE LTDLVENIQE VISAQLGKKR SKAFNLALKD FGIEYAKSSR
STCRGCEQKI NKDLVRLRKT VYDTEVGMKY GGQPLWHHLE CFAQLRSELG WFASGEDMPG
FQSLADDDQA KVKNAIPPIK SEELPDTKRA KMELSDTNEE GEKKQRLKDQ NDAYFRFRDD
IKNKMKKKDI DILLKFNNQQ PVTGDTEKLF DQTADLLTFG AIESCSECNS CQFIVNKSGY
ICNGNHSEWT KCNKLLKEPT RSACIVPKEL KALYNFLNTV KEIPSTRIFN NFPPNKSTFS
RSLLKTNKNN DVLVRPTIPR ISPPLYNLKF SIIGLKNQHK ELRKRIENLG GKFEVKISEN
TIAIISTELE IQKKSTRMKF AEELGIHIVP IEFLDFVEAD TEGAIKYINS TCICSWGTDP
KSRIPKETTK SLNSNSIYTK SMPVSRTFKV KDGLAVDPDS GLEDIAHVYV DSNNKYSVVL
GLTDIQRNKN SYYKVQLLKA DKKEKYWIFR SWGRIGTNIG NSKLEEFDTS ESAKRNFKEI
YADKTGNEYE QRDNFVKRTG RMYPIEIQYD DDQKLVKHES HFFTSKLEIS VQNLIKLIFD
IDSMNKTLME FHIDMDKMPL GKLSAHQIQS AYRVVKEIYN VLECGSNTAK LIDATNRFYT
LIPHNFGVQL PTLIETHQQI EDLRQMLDSL AEIEVAYSII KSEDVSDACN PLDNHYAQIK
TQLVALDKNS EEFSILSQYV KNTHASTHKS YDLKIVDVFK VSRQGEARRF KPFKKLHNRK
LLWHGSRLTN FVGILSHGLR IAPPEAPPTG YMFGKGIYFA DMVSKSANYC CTSQQNSTGL
MLLSEVALGD MMECTSAKYI NKLSNNKHSC FGRGRTMPDP TKSYIRSDGV EIPYGETITD
EHLKSSLLYN EYIVYDVAQV NIQYLFRMEF KYSY
