ID   APEX2_MOUSE             Reviewed;         516 AA.
AC   Q68G58; Q8BJP7; Q8BTR7; Q8BUZ2; Q8BYE9; Q8R018; Q8R328; Q9CS12;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   24-JAN-2024, entry version 140.
DE   RecName: Full=DNA-(apurinic or apyrimidinic site) endonuclease 2;
DE            EC=3.1.11.2 {ECO:0000250|UniProtKB:Q9UBZ4};
DE   AltName: Full=APEX nuclease 2;
DE   AltName: Full=Apurinic-apyrimidinic endonuclease 2;
DE            Short=AP endonuclease 2;
GN   Name=Apex2; Synonyms=Ape2;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), INTERACTION WITH
RP   PCNA, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=129/Sv, and C57BL/6J; TISSUE=B-cell;
RX   PubMed=12573260; DOI=10.1016/s0888-7543(02)00009-5;
RA   Ide Y., Tsuchimoto D., Tominaga Y., Iwamoto Y., Nakabeppu Y.;
RT   "Characterization of the genomic structure and expression of the mouse
RT   Apex2 gene.";
RL   Genomics 81:47-57(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1/2/4/5).
RC   STRAIN=NOD; TISSUE=Adipose tissue, Head, and Thymus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   STRAIN=FVB/N-3; 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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=15319281; DOI=10.1182/blood-2004-04-1476;
RA   Ide Y., Tsuchimoto D., Tominaga Y., Nakashima M., Watanabe T., Sakumi K.,
RA   Ohno M., Nakabeppu Y.;
RT   "Growth retardation and dyslymphopoiesis accompanied by G2/M arrest in
RT   APEX2-null mice.";
RL   Blood 104:4097-4103(2004).
RN   [5]
RP   FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX   PubMed=18025127; DOI=10.1084/jem.20071289;
RA   Guikema J.E., Linehan E.K., Tsuchimoto D., Nakabeppu Y., Strauss P.R.,
RA   Stavnezer J., Schrader C.E.;
RT   "APE1- and APE2-dependent DNA breaks in immunoglobulin class switch
RT   recombination.";
RL   J. Exp. Med. 204:3017-3026(2007).
RN   [6]
RP   FUNCTION.
RX   PubMed=19556307; DOI=10.1093/intimm/dxp061;
RA   Sabouri Z., Okazaki I.M., Shinkura R., Begum N., Nagaoka H., Tsuchimoto D.,
RA   Nakabeppu Y., Honjo T.;
RT   "Apex2 is required for efficient somatic hypermutation but not for class
RT   switch recombination of immunoglobulin genes.";
RL   Int. Immunol. 21:947-955(2009).
CC   -!- FUNCTION: Functions as a weak apurinic/apyrimidinic (AP)
CC       endodeoxyribonuclease in the DNA base excision repair (BER) pathway of
CC       DNA lesions induced by oxidative and alkylating agents (By similarity).
CC       Initiates repair of AP sites in DNA by catalyzing hydrolytic incision
CC       of the phosphodiester backbone immediately adjacent to the damage,
CC       generating a single-strand break with 5'-deoxyribose phosphate and 3'-
CC       hydroxyl ends (By similarity). Also displays double-stranded DNA 3'-5'
CC       exonuclease, 3'-phosphodiesterase activities. Shows robust 3'-5'
CC       exonuclease activity on 3'-recessed heteroduplex DNA and is able to
CC       remove mismatched nucleotides preferentially (By similarity). Shows
CC       fairly strong 3'-phosphodiesterase activity involved in the removal of
CC       3'-damaged termini formed in DNA by oxidative agents. In the nucleus
CC       functions in the PCNA-dependent BER pathway (By similarity). Plays a
CC       role in reversing blocked 3' DNA ends, problematic lesions that
CC       preclude DNA synthesis (By similarity). Required for somatic
CC       hypermutation (SHM) and DNA cleavage step of class switch recombination
CC       (CSR) of immunoglobulin genes (PubMed:18025127, PubMed:19556307).
CC       Required for proper cell cycle progression during proliferation of
CC       peripheral lymphocytes (PubMed:15319281).
CC       {ECO:0000250|UniProtKB:Q9UBZ4, ECO:0000269|PubMed:12573260,
CC       ECO:0000269|PubMed:15319281, ECO:0000269|PubMed:18025127,
CC       ECO:0000269|PubMed:19556307}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC         nucleoside 5'-phosphates.; EC=3.1.11.2;
CC         Evidence={ECO:0000250|UniProtKB:Q9UBZ4};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P27695};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P27695};
CC       Note=Probably binds two magnesium or manganese ions per subunit.
CC       {ECO:0000250|UniProtKB:P27695};
CC   -!- ACTIVITY REGULATION: 3'-5' exonuclease activity is activated by sodium
CC       and manganese (By similarity). 3'-5' exonuclease and 3'-
CC       phosphodiesterase activities are stimulated in presence of PCNA (By
CC       similarity). {ECO:0000250|UniProtKB:Q9UBZ4}.
CC   -!- SUBUNIT: Interacts with PCNA (PubMed:12573260). This interaction is
CC       increased by misincorporation of uracil in nuclear DNA (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UBZ4, ECO:0000269|PubMed:12573260}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12573260}. Cytoplasm
CC       {ECO:0000269|PubMed:12573260}. Mitochondrion
CC       {ECO:0000269|PubMed:12573260}. Note=Together with PCNA, is
CC       redistributed in discrete nuclear foci in presence of oxidative DNA
CC       damaging agents. {ECO:0000250|UniProtKB:Q9UBZ4}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=1;
CC         IsoId=Q68G58-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q68G58-2; Sequence=VSP_015346;
CC       Name=3;
CC         IsoId=Q68G58-3; Sequence=VSP_015349, VSP_015350;
CC       Name=4;
CC         IsoId=Q68G58-4; Sequence=VSP_015347, VSP_015352;
CC       Name=5;
CC         IsoId=Q68G58-5; Sequence=VSP_015348, VSP_015351;
CC   -!- TISSUE SPECIFICITY: Expressed in lymphocytes, thymocytes and
CC       splenocytes (at protein level). Highly expressed in the thymus and
CC       weakly expressed in the bone marrow, spleen, eye, kidney, lung, brain
CC       and uterus. {ECO:0000269|PubMed:12573260, ECO:0000269|PubMed:15319281}.
CC   -!- INDUCTION: Up-regulated in both the nucleus and the cytosol of B cells
CC       stimulated to switch. {ECO:0000269|PubMed:18025127}.
CC   -!- DOMAIN: The PCNA interacting protein (PIP) box mediates interaction
CC       with PCNA and recruitment to DNA single-strand breaks.
CC       {ECO:0000250|UniProtKB:Q9UBZ4}.
CC   -!- DISRUPTION PHENOTYPE: Mice show abnormalities in proliferating
CC       haemopoietic organs, such as dyshematopoiesis, defect in lymphopoiesis,
CC       and delayed S-phase and G2/M-phase arrest.
CC       {ECO:0000269|PubMed:15319281, ECO:0000269|PubMed:18025127}.
CC   -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC       {ECO:0000305}.
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DR   EMBL; AB072498; BAB88654.1; -; mRNA.
DR   EMBL; AB085235; BAC11807.1; -; Genomic_DNA.
DR   EMBL; AK021248; BAB32346.1; -; mRNA.
DR   EMBL; AK040145; BAC30522.1; -; mRNA.
DR   EMBL; AK050858; BAC34436.1; -; mRNA.
DR   EMBL; AK080916; BAC38077.1; -; mRNA.
DR   EMBL; AK081677; BAC38287.1; -; mRNA.
DR   EMBL; AK088918; BAC40652.1; -; mRNA.
DR   EMBL; BC026769; AAH26769.1; -; mRNA.
DR   EMBL; BC078633; AAH78633.1; -; mRNA.
DR   CCDS; CCDS30463.1; -. [Q68G58-1]
DR   RefSeq; NP_084219.1; NM_029943.2.
DR   RefSeq; XP_011246180.1; XM_011247878.2.
DR   AlphaFoldDB; Q68G58; -.
DR   SMR; Q68G58; -.
DR   BioGRID; 218805; 3.
DR   IntAct; Q68G58; 1.
DR   STRING; 10090.ENSMUSP00000108340; -.
DR   iPTMnet; Q68G58; -.
DR   PhosphoSitePlus; Q68G58; -.
DR   MaxQB; Q68G58; -.
DR   PaxDb; 10090-ENSMUSP00000108341; -.
DR   ProteomicsDB; 281794; -. [Q68G58-1]
DR   ProteomicsDB; 281795; -. [Q68G58-2]
DR   ProteomicsDB; 281796; -. [Q68G58-3]
DR   ProteomicsDB; 281797; -. [Q68G58-4]
DR   ProteomicsDB; 281798; -. [Q68G58-5]
DR   Pumba; Q68G58; -.
DR   Antibodypedia; 26902; 188 antibodies from 26 providers.
DR   DNASU; 77622; -.
DR   Ensembl; ENSMUST00000112725.8; ENSMUSP00000108345.2; ENSMUSG00000025269.17. [Q68G58-5]
DR   Ensembl; ENSMUST00000112727.10; ENSMUSP00000108347.4; ENSMUSG00000025269.17. [Q68G58-4]
DR   GeneID; 77622; -.
DR   KEGG; mmu:77622; -.
DR   UCSC; uc009uoi.1; mouse. [Q68G58-5]
DR   AGR; MGI:1924872; -.
DR   CTD; 27301; -.
DR   MGI; MGI:1924872; Apex2.
DR   VEuPathDB; HostDB:ENSMUSG00000025269; -.
DR   eggNOG; KOG1294; Eukaryota.
DR   GeneTree; ENSGT00530000063540; -.
DR   InParanoid; Q68G58; -.
DR   OrthoDB; 169291at2759; -.
DR   BioGRID-ORCS; 77622; 13 hits in 114 CRISPR screens.
DR   ChiTaRS; Apex2; mouse.
DR   PRO; PR:Q68G58; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q68G58; Protein.
DR   Bgee; ENSMUSG00000025269; Expressed in epiblast (generic) and 154 other cell types or tissues.
DR   ExpressionAtlas; Q68G58; baseline and differential.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR   GO; GO:0008311; F:double-stranded DNA 3'-5' DNA exonuclease activity; IBA:GO_Central.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   CDD; cd09088; Ape2-like_AP-endo; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   InterPro; IPR004808; AP_endonuc_1.
DR   InterPro; IPR020847; AP_endonuclease_F1_BS.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR   InterPro; IPR010666; Znf_GRF.
DR   NCBIfam; TIGR00633; xth; 1.
DR   PANTHER; PTHR22748; AP ENDONUCLEASE; 1.
DR   PANTHER; PTHR22748:SF4; DNA-(APURINIC OR APYRIMIDINIC SITE) ENDONUCLEASE 2; 1.
DR   Pfam; PF03372; Exo_endo_phos; 1.
DR   Pfam; PF06839; zf-GRF; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
DR   PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
DR   PROSITE; PS51999; ZF_GRF; 1.
DR   Genevisible; Q68G58; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Cytoplasm; DNA damage; DNA recombination;
KW   DNA repair; DNA-binding; Endonuclease; Exonuclease; Hydrolase; Magnesium;
KW   Metal-binding; Mitochondrion; Nuclease; Nucleus; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..516
FT                   /note="DNA-(apurinic or apyrimidinic site) endonuclease 2"
FT                   /id="PRO_0000200015"
FT   ZN_FING         467..516
FT                   /note="GRF-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"
FT   REGION          357..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          389..396
FT                   /note="Required for the interaction and colocalization with
FT                   PCNA in nuclear foci in presence of oxidative-induced DNA
FT                   damaging agents"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UBZ4"
FT   COMPBIAS        372..386
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        155
FT                   /evidence="ECO:0000250|UniProtKB:P27695"
FT   ACT_SITE        196
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P27695"
FT   ACT_SITE        303
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00764"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00764"
FT   BINDING         47
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00764"
FT   BINDING         196
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00764"
FT   BINDING         198
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00764"
FT   BINDING         302
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00764"
FT   BINDING         303
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00764"
FT   BINDING         467
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"
FT   BINDING         470
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"
FT   BINDING         493
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"
FT   BINDING         507
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01343"
FT   SITE            198
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250|UniProtKB:P27695"
FT   SITE            276
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P27695"
FT   SITE            303
FT                   /note="Interaction with DNA substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P27695"
FT   VAR_SEQ         79
FT                   /note="S -> SECSCPSP (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_015346"
FT   VAR_SEQ         213..266
FT                   /note="ECFEEDPGRKWMDGLLSNPGDEAGPHIGLFMDSYRYLHPKQQRAFTCWSVVS
FT                   GA -> LPVAACGHTNLVPEWEAGPVWERTMREIMEGFCDLLHSVRIFHHHTASLLRPS
FT                   Y (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_015347"
FT   VAR_SEQ         213..260
FT                   /note="ECFEEDPGRKWMDGLLSNPGDEAGPHIGLFMDSYRYLHPKQQRAFTCW ->
FT                   LPVAACGHTNLVPEWEAGPVWERTMREIMEVKTRFCSRPLKFTESPCL (in
FT                   isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_015348"
FT   VAR_SEQ         213..246
FT                   /note="ECFEEDPGRKWMDGLLSNPGDEAGPHIGLFMDSY -> VRFPLNHRPQFCSV
FT                   HPASQNWEFGTRGSFFYGKK (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015349"
FT   VAR_SEQ         247..516
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_015350"
FT   VAR_SEQ         261..516
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_015351"
FT   VAR_SEQ         267..516
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_015352"
FT   CONFLICT        110
FT                   /note="G -> S (in Ref. 2; BAC38077)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183
FT                   /note="A -> P (in Ref. 2; BAB32346)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        372
FT                   /note="C -> F (in Ref. 3; AAH78633)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        433
FT                   /note="V -> M (in Ref. 3; AAH78633)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   516 AA;  57340 MW;  ED32A88D9CEABB85 CRC64;
     MLRVVSWNIN GIRSPLQGLA CQEPSSCPTA LRRVLDELDA DIVCLQETKV TRDVLTEPLA
     IVEGYNSYFS FSRSRSGYSG VATFCKDSAT PVAAEEGLSG VFATLNGDIG CYGNMDEFTQ
     EELRVLDSEG RALLTQHKIR TLEGKEKTLT LINVYCPHAD PGKPERLTFK MRFYRLLQMR
     AEALLAAGSH VIILGDLNTA HRPIDHCDAS SLECFEEDPG RKWMDGLLSN PGDEAGPHIG
     LFMDSYRYLH PKQQRAFTCW SVVSGARHLN YGSRLDYVLG DRALVIDTFQ ASFLLPEVMG
     SDHCPVGAVL NVSCVPAKQC PALCTRFLPE FAGTQLKILR FLVPLEQEPV REQQVLQPSH
     QIQAQRQPRK ACMHSTRLRK SQGGPKRKQK NLMSYFQPSS SLSQTSGVEL PTLPLVGPLT
     TPKTAEEVAT ATVLEEKNKV PESKDEKGER TAFWKSMLSG PSPMPLCGGH REPCVMRTVK
     KTGPNFGRQF YMCARPRGPP SDPSSRCNFF LWSRPS
//