ID   APLF_MOUSE              Reviewed;         499 AA.
AC   Q9D842; Q8BZL5; Q99LX6;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 2.
DT   24-JAN-2024, entry version 150.
DE   RecName: Full=Aprataxin and PNK-like factor;
DE            EC=3.1.-.- {ECO:0000250|UniProtKB:Q8IW19};
DE   AltName: Full=Apurinic-apyrimidinic endonuclease APLF;
GN   Name=Aplf;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J; TISSUE=Diencephalon, and Small intestine;
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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Mammary gland;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [4]
RP   FUNCTION.
RX   PubMed=21211721; DOI=10.1016/j.molcel.2010.12.006;
RA   Rulten S.L., Fisher A.E., Robert I., Zuma M.C., Rouleau M., Ju L.,
RA   Poirier G., Reina-San-Martin B., Caldecott K.W.;
RT   "PARP-3 and APLF function together to accelerate nonhomologous end-
RT   joining.";
RL   Mol. Cell 41:33-45(2011).
RN   [5]
RP   FUNCTION.
RX   PubMed=27875275; DOI=10.1242/jcs.194035;
RA   Syed K.M., Joseph S., Mukherjee A., Majumder A., Teixeira J.M., Dutta D.,
RA   Pillai M.R.;
RT   "Histone chaperone APLF regulates induction of pluripotency in murine
RT   fibroblasts.";
RL   J. Cell Sci. 129:4576-4591(2016).
RN   [6]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX   PubMed=33277378; DOI=10.1242/jcs.246900;
RA   Varghese P.C., Rajam S.M., Nandy D., Jory A., Mukherjee A., Dutta D.;
RT   "Histone chaperone APLF level dictates the implantation of mouse embryos.";
RL   J. Cell Sci. 134:0-0(2021).
CC   -!- FUNCTION: Histone chaperone involved in single-strand and double-strand
CC       DNA break repair (By similarity). Recruited to sites of DNA damage
CC       through interaction with branched poly-ADP-ribose chains, a polymeric
CC       post-translational modification synthesized transiently at sites of
CC       chromosomal damage to accelerate DNA strand break repair reactions (By
CC       similarity). Following recruitment to DNA damage sites, acts as a
CC       histone chaperone that mediates histone eviction during DNA repair and
CC       promotes recruitment of histone variant MACROH2A1 (PubMed:27875275).
CC       Also has a nuclease activity: displays apurinic-apyrimidinic (AP)
CC       endonuclease and 3'-5' exonuclease activities in vitro (By similarity).
CC       Also able to introduce nicks at hydroxyuracil and other types of
CC       pyrimidine base damage (By similarity). Together with PARP3, promotes
CC       the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA
CC       ligation during non-homologous end-joining (NHEJ) (PubMed:21211721).
CC       Also acts as a negative regulator of cell pluripotency by promoting
CC       histone exchange (PubMed:27875275). Required for the embryo
CC       implantation during the epithelial to mesenchymal transition in females
CC       (PubMed:33277378). {ECO:0000250|UniProtKB:Q8IW19,
CC       ECO:0000269|PubMed:21211721, ECO:0000269|PubMed:27875275,
CC       ECO:0000269|PubMed:33277378}.
CC   -!- SUBUNIT: Interacts with LIG4 (By similarity). Interacts with PARP1 (By
CC       similarity). Interacts with XRCC4. Interacts (via KBM motif) with XRCC5
CC       and XRCC6; promoting recruitment to DNA damage sites (By similarity).
CC       Interacts with XRCC1 (By similarity). Interacts (via C-terminal
CC       disordered region) with histones; interacts with histone H2A, H2B and
CC       H3-H4 (By similarity). {ECO:0000250|UniProtKB:Q8IW19}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33277378}. Chromosome
CC       {ECO:0000250|UniProtKB:Q8IW19}. Cytoplasm, cytosol
CC       {ECO:0000269|PubMed:33277378}. Note=Localizes to DNA damage sites.
CC       Accumulates at single-strand breaks and double-strand breaks via the
CC       PBZ-type zinc fingers. {ECO:0000250|UniProtKB:Q8IW19}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9D842-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9D842-2; Sequence=VSP_014983, VSP_014984;
CC       Name=3;
CC         IsoId=Q9D842-3; Sequence=VSP_014982, VSP_014984;
CC   -!- DEVELOPMENTAL STAGE: Present in the 4-cell stage (PubMed:33277378).
CC       Expression is enhanced in early morula and late morula stage embryos
CC       (PubMed:33277378). Down-regulated during the first differentiation to
CC       form inner cell mass and trophectoderm within a blastocyst (32-cell
CC       stage) (PubMed:33277378). {ECO:0000269|PubMed:33277378}.
CC   -!- DOMAIN: The PBZ-type zinc fingers (also named CYR) mediate non-covalent
CC       poly-ADP-ribose-binding. Specifically recognizes branched poly-ADP-
CC       ribose chains generated by PARP2. Poly-ADP-ribose-binding is dependent
CC       on the presence of zinc and promotes its recruitment to DNA damage
CC       sites. {ECO:0000250|UniProtKB:Q8IW19}.
CC   -!- DOMAIN: The KBM (Ku-binding motif) mediates interaction with XRCC5/Ku80
CC       and XRCC6/Ku70 and recruitment to DNA damage sites.
CC       {ECO:0000250|UniProtKB:Q8IW19}.
CC   -!- DOMAIN: The FHA-like domain mediates interaction with XRCC1 and XRCC4.
CC       {ECO:0000250|UniProtKB:Q8IW19}.
CC   -!- DOMAIN: The NAP1L motif is required for the histone chaperone activity.
CC       {ECO:0000250|UniProtKB:Q8IW19}.
CC   -!- PTM: Poly-ADP-ribosylated. In addition to binding non covalently poly-
CC       ADP-ribose via its PBZ-type zinc fingers, the protein is also
CC       covalently poly-ADP-ribosylated by PARP1.
CC       {ECO:0000250|UniProtKB:Q8IW19}.
CC   -!- PTM: Phosphorylated in an ATM-dependent manner upon double-strand DNA
CC       break. {ECO:0000250|UniProtKB:Q8IW19}.
CC   -!- SIMILARITY: Belongs to the APLF family. {ECO:0000305}.
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DR   EMBL; AK008513; BAB25711.1; -; mRNA.
DR   EMBL; AK034191; BAC28625.1; -; mRNA.
DR   EMBL; BC002179; AAH02179.1; -; mRNA.
DR   CCDS; CCDS20324.1; -. [Q9D842-3]
DR   CCDS; CCDS51839.1; -. [Q9D842-1]
DR   RefSeq; NP_001163960.1; NM_001170489.1. [Q9D842-1]
DR   RefSeq; NP_077213.2; NM_024251.4. [Q9D842-3]
DR   AlphaFoldDB; Q9D842; -.
DR   SMR; Q9D842; -.
DR   BioGRID; 215153; 5.
DR   STRING; 10090.ENSMUSP00000032130; -.
DR   iPTMnet; Q9D842; -.
DR   PhosphoSitePlus; Q9D842; -.
DR   SwissPalm; Q9D842; -.
DR   EPD; Q9D842; -.
DR   jPOST; Q9D842; -.
DR   MaxQB; Q9D842; -.
DR   PaxDb; 10090-ENSMUSP00000032130; -.
DR   PeptideAtlas; Q9D842; -.
DR   ProteomicsDB; 296375; -. [Q9D842-1]
DR   ProteomicsDB; 296376; -. [Q9D842-2]
DR   ProteomicsDB; 296377; -. [Q9D842-3]
DR   Pumba; Q9D842; -.
DR   Antibodypedia; 30942; 291 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000032130.8; ENSMUSP00000032130.3; ENSMUSG00000030051.11. [Q9D842-1]
DR   Ensembl; ENSMUST00000065997.5; ENSMUSP00000066232.3; ENSMUSG00000030051.11. [Q9D842-3]
DR   GeneID; 72103; -.
DR   KEGG; mmu:72103; -.
DR   UCSC; uc009ctq.2; mouse. [Q9D842-3]
DR   UCSC; uc009ctr.2; mouse. [Q9D842-1]
DR   UCSC; uc012eon.1; mouse. [Q9D842-2]
DR   AGR; MGI:1919353; -.
DR   CTD; 200558; -.
DR   MGI; MGI:1919353; Aplf.
DR   VEuPathDB; HostDB:ENSMUSG00000030051; -.
DR   eggNOG; ENOG502R7QZ; Eukaryota.
DR   GeneTree; ENSGT00390000010591; -.
DR   HOGENOM; CLU_043152_0_0_1; -.
DR   InParanoid; Q9D842; -.
DR   OMA; PCFYRSS; -.
DR   OrthoDB; 2971338at2759; -.
DR   PhylomeDB; Q9D842; -.
DR   TreeFam; TF326160; -.
DR   BioGRID-ORCS; 72103; 1 hit in 114 CRISPR screens.
DR   ChiTaRS; Aplf; mouse.
DR   PRO; PR:Q9D842; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9D842; Protein.
DR   Bgee; ENSMUSG00000030051; Expressed in otic placode and 166 other cell types or tissues.
DR   ExpressionAtlas; Q9D842; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; ISS:UniProtKB.
DR   GO; GO:0160002; F:ADP-D-ribose modification-dependent protein binding; ISS:UniProtKB.
DR   GO; GO:0004520; F:DNA endonuclease activity; ISS:UniProtKB.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; ISS:UniProtKB.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0140713; F:histone chaperone activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB.
DR   GO; GO:0072572; F:poly-ADP-D-ribose binding; ISS:UniProtKB.
DR   GO; GO:0044183; F:protein folding chaperone; ISO:MGI.
DR   GO; GO:0006974; P:DNA damage response; ISS:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; ISO:MGI.
DR   GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; ISS:UniProtKB.
DR   GO; GO:0006302; P:double-strand break repair; IMP:MGI.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR   GO; GO:0007566; P:embryo implantation; IMP:UniProtKB.
DR   GO; GO:0051106; P:positive regulation of DNA ligation; ISO:MGI.
DR   GO; GO:0071168; P:protein localization to chromatin; ISO:MGI.
DR   GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
DR   GO; GO:0045191; P:regulation of isotype switching; IMP:MGI.
DR   GO; GO:0000012; P:single strand break repair; ISS:UniProtKB.
DR   CDD; cd22717; FHA_APLF; 1.
DR   Gene3D; 2.60.200.20; -; 1.
DR   InterPro; IPR039253; APLF.
DR   InterPro; IPR019406; APLF_PBZ.
DR   InterPro; IPR041388; FHA_2.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   PANTHER; PTHR21315:SF2; APRATAXIN AND PNK-LIKE FACTOR; 1.
DR   PANTHER; PTHR21315; UNCHARACTERIZED; 1.
DR   Pfam; PF17913; FHA_2; 1.
DR   Pfam; PF10283; zf-CCHH; 2.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   Genevisible; Q9D842; MM.
PE   1: Evidence at protein level;
KW   ADP-ribosylation; Alternative splicing; Chromosome; Coiled coil; Cytoplasm;
KW   DNA damage; DNA repair; Hydrolase; Metal-binding; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc; Zinc-finger.
FT   CHAIN           1..499
FT                   /note="Aprataxin and PNK-like factor"
FT                   /id="PRO_0000089343"
FT   DOMAIN          1..108
FT                   /note="FHA-like"
FT   ZN_FING         372..393
FT                   /note="PBZ-type 1"
FT   ZN_FING         414..435
FT                   /note="PBZ-type 2"
FT   REGION          134..183
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..292
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          305..358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..411
FT                   /note="Flexible linker"
FT                   /evidence="ECO:0000250, ECO:0000250|UniProtKB:Q8IW19"
FT   REGION          440..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           182..191
FT                   /note="KBM"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT   MOTIF           463..487
FT                   /note="NAP1L motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT   COMPBIAS        134..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        222..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        449..485
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         371
FT                   /ligand="a glycoprotein"
FT                   /ligand_id="ChEBI:CHEBI:17089"
FT                   /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT                   /ligand_part_id="ChEBI:CHEBI:157741"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT   BINDING         376
FT                   /ligand="a glycoprotein"
FT                   /ligand_id="ChEBI:CHEBI:17089"
FT                   /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT                   /ligand_part_id="ChEBI:CHEBI:157741"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT   BINDING         381
FT                   /ligand="a glycoprotein"
FT                   /ligand_id="ChEBI:CHEBI:17089"
FT                   /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT                   /ligand_part_id="ChEBI:CHEBI:157741"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT   BINDING         382
FT                   /ligand="a glycoprotein"
FT                   /ligand_id="ChEBI:CHEBI:17089"
FT                   /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT                   /ligand_part_id="ChEBI:CHEBI:157741"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT   BINDING         418
FT                   /ligand="a glycoprotein"
FT                   /ligand_id="ChEBI:CHEBI:17089"
FT                   /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT                   /ligand_part_id="ChEBI:CHEBI:157741"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT   BINDING         423
FT                   /ligand="a glycoprotein"
FT                   /ligand_id="ChEBI:CHEBI:17089"
FT                   /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT                   /ligand_part_id="ChEBI:CHEBI:157741"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT   BINDING         424
FT                   /ligand="a glycoprotein"
FT                   /ligand_id="ChEBI:CHEBI:17089"
FT                   /ligand_part="poly[(1''->2')-ADP-alpha-D-ribose] group"
FT                   /ligand_part_id="ChEBI:CHEBI:157741"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT   MOD_RES         116
FT                   /note="Phosphoserine; by ATM"
FT                   /evidence="ECO:0000250|UniProtKB:Q8IW19"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..108
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014983"
FT   VAR_SEQ         1..32
FT                   /note="MPSDFFLQPLDGGPRVPVGPGQTVIGRGPLLG -> MPSVPEGGGYE (in
FT                   isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014982"
FT   VAR_SEQ         493..499
FT                   /note="SSLHLKH -> RFMRRKK (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014984"
FT   CONFLICT        178
FT                   /note="R -> H (in Ref. 2; AAH02179)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        470
FT                   /note="S -> F (in Ref. 1; BAB25711)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   499 AA;  54968 MW;  4B41A9C0C8937963 CRC64;
     MPSDFFLQPL DGGPRVPVGP GQTVIGRGPL LGITDKRVSR RHAILEVVDS QLRIKPIHRN
     PCFYQSSEKS QHSPMETQVW SQLHPGDSFS LLLDKYAFRV FSAESEVEME CTLRNSQMLD
     EDDILSEMQK SPVVNLPDKT TGASQLQGSP EITKTKCPTI DPMSSSGECR AFSEHQPRPT
     QRKRILPAWM LAESLSDQSL STPAEGGDKD VIQRSGKAGT CEDRTPGNTS WHGKKRLSPS
     GNSKSVSAEQ DPGKKCRKAD QEGPGVSSEN VPESSSSNIV KDPDVDIVKT NKQKDGILIE
     ELGEVSKHKA ATKPTTNEEG ESCARVQSKS PPEKSQGCHP ESSSAPSSPD ALHTDTADPV
     LGCSEESKVR RTACMYGANC YRRNPLHFQH FSHPGDSDYG EVHGTDEGVI GDRPECPYGA
     SCYRKNPQHK MEYRHSALPA RVALDEDDDD VGQPSDDEDE EDYEPTDEDS DWHPGKDDEE
     QEDVDELLKE AKSSLHLKH
//