APTX_MOUSE
ID APTX_MOUSE Reviewed; 342 AA.
AC Q7TQC5; Q8BPA7; Q8C2B5; Q8K3D1; Q9CQ59;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Aprataxin;
DE EC=3.6.1.71 {ECO:0000269|PubMed:16964241};
DE EC=3.6.1.72 {ECO:0000250|UniProtKB:O74859};
DE AltName: Full=Forkhead-associated domain histidine triad-like protein;
DE Short=FHA-HIT;
GN Name=Aptx;
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).
RC STRAIN=BALB/cJ, and C57BL/6J;
RA Huang C.-H.;
RT "Identification of FHA-HIT as a novel nuclear protein involved in cell-
RT cycle regulation.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Chen Y., Huang C.-H.;
RT "Differential polyadenylation of mouse FHA-HIT transcript.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Embryonic stem cell, Pituitary, 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=Czech II; 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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=11586300; DOI=10.1038/ng1001-189;
RA Moreira M.-C., Barbot C., Tachi N., Kozuka N., Uchida E., Gibson T.,
RA Mendonca P., Costa M., Barros J., Yanagisawa T., Watanabe M., Ikeda Y.,
RA Aoki M., Nagata T., Coutinho P., Sequeiros J., Koenig M.;
RT "The gene mutated in ataxia-ocular apraxia 1 encodes the new HIT/Zn-finger
RT protein aprataxin.";
RL Nat. Genet. 29:189-193(2001).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16964241; DOI=10.1038/nature05164;
RA Ahel I., Rass U., El-Khamisy S.F., Katyal S., Clements P.M., McKinnon P.J.,
RA Caldecott K.W., West S.C.;
RT "The neurodegenerative disease protein aprataxin resolves abortive DNA
RT ligation intermediates.";
RL Nature 443:713-716(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-127 AND SER-134, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, 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).
CC -!- FUNCTION: DNA-binding protein involved in single-strand DNA break
CC repair, double-strand DNA break repair and base excision repair.
CC Resolves abortive DNA ligation intermediates formed either at base
CC excision sites, or when DNA ligases attempt to repair non-ligatable
CC breaks induced by reactive oxygen species. Catalyzes the release of
CC adenylate groups covalently linked to 5'-phosphate termini, resulting
CC in the production of 5'-phosphate termini that can be efficiently
CC rejoined (PubMed:16964241). Also able to hydrolyze adenosine 5'-
CC monophosphoramidate (AMP-NH(2)) and diadenosine tetraphosphate
CC (AppppA), but with lower catalytic activity (By similarity). Likewise,
CC catalyzes the release of 3'-linked guanosine (DNAppG) and inosine
CC (DNAppI) from DNA, but has higher specific activity with 5'-linked
CC adenosine (AppDNA) (By similarity). {ECO:0000250|UniProtKB:O74859,
CC ECO:0000250|UniProtKB:Q7Z2E3, ECO:0000269|PubMed:16964241}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end adenosine-5'-diphospho-5'-(2'-deoxyribonucleoside)-
CC DNA + H2O = a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + AMP
CC + 2 H(+); Xref=Rhea:RHEA:52128, Rhea:RHEA-COMP:13180, Rhea:RHEA-
CC COMP:13181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412,
CC ChEBI:CHEBI:136413, ChEBI:CHEBI:456215; EC=3.6.1.71;
CC Evidence={ECO:0000269|PubMed:16964241};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 5'-end adenosine-5'-diphospho-5'-ribonucleoside-2'-
CC deoxyribonucleotide-DNA + H2O = a 5'-end 5'-monophospho-
CC ribonucleoside-2'-deoxyribonucleotide-DNA + AMP + 2 H(+);
CC Xref=Rhea:RHEA:52132, Rhea:RHEA-COMP:13182, Rhea:RHEA-COMP:13183,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:136414,
CC ChEBI:CHEBI:136415, ChEBI:CHEBI:456215; EC=3.6.1.71;
CC Evidence={ECO:0000269|PubMed:16964241};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'-end 2'-deoxyribonucleotide-3'-diphospho-5'-guanosine-DNA
CC + H2O = a 3'-end 2'-deoxyribonucleotide 3'-phosphate-DNA + GMP + 2
CC H(+); Xref=Rhea:RHEA:52140, Rhea:RHEA-COMP:13186, Rhea:RHEA-
CC COMP:13187, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58115,
CC ChEBI:CHEBI:136419, ChEBI:CHEBI:136420; EC=3.6.1.72;
CC Evidence={ECO:0000250|UniProtKB:O74859};
CC -!- SUBUNIT: Interacts with single-strand break repair proteins XRCC1,
CC XRCC4, ADPRT/PARP1 and p53/TP53. Interacts with NCL. Interacts (via
CC FHA-like domain) with MDC1 (phosphorylated).
CC {ECO:0000250|UniProtKB:Q7Z2E3}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q7Z2E3}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q7Z2E3}. Note=Upon genotoxic stress, colocalizes
CC with XRCC1 at sites of DNA damage. Colocalizes with MDC1 at sites of
CC DNA double-strand breaks. Interaction with NCL is required for
CC nucleolar localization (By similarity). {ECO:0000250|UniProtKB:Q7Z2E3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7TQC5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TQC5-2; Sequence=VSP_010542;
CC Name=3;
CC IsoId=Q7TQC5-3; Sequence=VSP_010543;
CC Name=4;
CC IsoId=Q7TQC5-4; Sequence=VSP_010543, VSP_010544;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, liver,
CC kidney, spleen, lung, muscle, brain stem, spinal cord, cerebellum and
CC brain. {ECO:0000269|PubMed:11586300}.
CC -!- DOMAIN: The histidine triad, also called HIT motif, forms part of the
CC binding loop for the alpha-phosphate of purine mononucleotide.
CC {ECO:0000250|UniProtKB:Q7Z2E3}.
CC -!- DOMAIN: The FHA-like domain mediates interaction with NCL; XRCC1 and
CC XRCC4. {ECO:0000250}.
CC -!- DOMAIN: The HIT domain is required for enzymatic activity.
CC {ECO:0000250}.
CC -!- DOMAIN: The C2H2-type zinc finger mediates DNA-binding. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP86334.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY040780; AAK91771.1; -; mRNA.
DR EMBL; AY040782; AAK91773.1; -; Genomic_DNA.
DR EMBL; AY208844; AAP86334.1; ALT_INIT; mRNA.
DR EMBL; AK005286; BAB23933.2; -; mRNA.
DR EMBL; AK010516; BAB26998.2; -; mRNA.
DR EMBL; AK077351; BAC36763.1; -; mRNA.
DR EMBL; AK088928; BAC40657.1; -; mRNA.
DR EMBL; BC021872; AAH21872.2; -; mRNA.
DR CCDS; CCDS38711.1; -. [Q7TQC5-1]
DR CCDS; CCDS38712.1; -. [Q7TQC5-3]
DR RefSeq; NP_001020615.1; NM_001025444.3. [Q7TQC5-3]
DR RefSeq; NP_001020616.1; NM_001025445.2. [Q7TQC5-2]
DR RefSeq; NP_079821.3; NM_025545.4. [Q7TQC5-1]
DR RefSeq; XP_006538229.1; XM_006538166.3. [Q7TQC5-3]
DR RefSeq; XP_006538230.1; XM_006538167.3. [Q7TQC5-3]
DR RefSeq; XP_006538231.1; XM_006538168.3. [Q7TQC5-3]
DR RefSeq; XP_006538232.1; XM_006538169.3. [Q7TQC5-3]
DR RefSeq; XP_006538233.1; XM_006538170.3. [Q7TQC5-3]
DR RefSeq; XP_006538234.1; XM_006538171.3. [Q7TQC5-2]
DR AlphaFoldDB; Q7TQC5; -.
DR SMR; Q7TQC5; -.
DR BioGRID; 211452; 1.
DR STRING; 10090.ENSMUSP00000124264; -.
DR iPTMnet; Q7TQC5; -.
DR PhosphoSitePlus; Q7TQC5; -.
DR EPD; Q7TQC5; -.
DR MaxQB; Q7TQC5; -.
DR PaxDb; Q7TQC5; -.
DR PeptideAtlas; Q7TQC5; -.
DR PRIDE; Q7TQC5; -.
DR ProteomicsDB; 283190; -. [Q7TQC5-1]
DR ProteomicsDB; 283191; -. [Q7TQC5-2]
DR ProteomicsDB; 283192; -. [Q7TQC5-3]
DR ProteomicsDB; 283193; -. [Q7TQC5-4]
DR Antibodypedia; 10716; 252 antibodies from 30 providers.
DR DNASU; 66408; -.
DR Ensembl; ENSMUST00000030119; ENSMUSP00000030119; ENSMUSG00000028411. [Q7TQC5-3]
DR Ensembl; ENSMUST00000068125; ENSMUSP00000124264; ENSMUSG00000028411. [Q7TQC5-1]
DR Ensembl; ENSMUST00000108103; ENSMUSP00000103738; ENSMUSG00000028411. [Q7TQC5-4]
DR GeneID; 66408; -.
DR KEGG; mmu:66408; -.
DR UCSC; uc008sho.1; mouse. [Q7TQC5-1]
DR UCSC; uc008shr.2; mouse. [Q7TQC5-4]
DR CTD; 54840; -.
DR MGI; MGI:1913658; Aptx.
DR VEuPathDB; HostDB:ENSMUSG00000028411; -.
DR eggNOG; KOG0562; Eukaryota.
DR eggNOG; KOG2134; Eukaryota.
DR GeneTree; ENSGT00940000156806; -.
DR HOGENOM; CLU_066882_2_0_1; -.
DR InParanoid; Q7TQC5; -.
DR OMA; PLCWLIS; -.
DR OrthoDB; 1290702at2759; -.
DR PhylomeDB; Q7TQC5; -.
DR TreeFam; TF313308; -.
DR BRENDA; 3.6.1.71; 3474.
DR BioGRID-ORCS; 66408; 3 hits in 110 CRISPR screens.
DR ChiTaRS; Aptx; mouse.
DR PRO; PR:Q7TQC5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q7TQC5; protein.
DR Bgee; ENSMUSG00000028411; Expressed in seminiferous tubule of testis and 246 other tissues.
DR ExpressionAtlas; Q7TQC5; baseline and differential.
DR Genevisible; Q7TQC5; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003684; F:damaged DNA binding; ISO:MGI.
DR GO; GO:0033699; F:DNA 5'-adenosine monophosphate hydrolase activity; IMP:UniProtKB.
DR GO; GO:0120108; F:DNA-3'-diphospho-5'-guanosine diphosphatase; IEA:UniProtKB-EC.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; TAS:MGI.
DR GO; GO:0030983; F:mismatched DNA binding; IBA:GO_Central.
DR GO; GO:0008967; F:phosphoglycolate phosphatase activity; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0046403; F:polynucleotide 3'-phosphatase activity; ISO:MGI.
DR GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR GO; GO:1990165; F:single-strand break-containing DNA binding; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0006266; P:DNA ligation; IDA:MGI.
DR GO; GO:0006302; P:double-strand break repair; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
DR GO; GO:0000012; P:single strand break repair; IMP:UniProtKB.
DR CDD; cd00060; FHA; 1.
DR Gene3D; 3.30.428.10; -; 1.
DR InterPro; IPR026963; Aprataxin-like.
DR InterPro; IPR041388; FHA_2.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR019808; Histidine_triad_CS.
DR InterPro; IPR011146; HIT-like.
DR InterPro; IPR036265; HIT-like_sf.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR InterPro; IPR032566; Znf-C2HE.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR12486:SF4; PTHR12486:SF4; 2.
DR Pfam; PF17913; FHA_2; 1.
DR Pfam; PF16278; zf-C2HE; 1.
DR SUPFAM; SSF49879; SSF49879; 1.
DR SUPFAM; SSF54197; SSF54197; 1.
DR PROSITE; PS00892; HIT_1; 1.
DR PROSITE; PS51084; HIT_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..342
FT /note="Aprataxin"
FT /id="PRO_0000109840"
FT DOMAIN 30..79
FT /note="FHA-like"
FT DOMAIN 168..273
FT /note="HIT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT ZN_FING 317..339
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..102
FT /note="Interactions with ADPRT/PARP1 and NCL"
FT /evidence="ECO:0000250"
FT REGION 114..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 193..197
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT REGION 255..256
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT MOTIF 118..122
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 258..262
FT /note="Histidine triad motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00464"
FT COMPBIAS 114..129
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 260
FT /note="Tele-AMP-histidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 174
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 251
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 262
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT SITE 277
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2E3"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..66
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010542"
FT VAR_SEQ 1..7
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_010543"
FT VAR_SEQ 67..161
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010544"
FT CONFLICT 86
FT /note="K -> L (in Ref. 4; AAH21872)"
FT /evidence="ECO:0000305"
FT CONFLICT 237
FT /note="D -> E (in Ref. 4; AAH21872)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 342 AA; 38723 MW; A8D77F2F4B362F03 CRC64;
MPEAVAKMRV CWLVRQDSRH QRIKLPHLEA VVIGRSPETK ITDKKCSRQQ VQLKAECNKG
YVKVQQMGVN PTSIDSGVIG KDQEKKLLPG QVLHMVNGLY PYIVEFEEVA ESPNLTQRKR
KRSDCDSEEM EAESGTGLAP GSSPSQCSVS PKKDKNGATK KESLGHWSQG LKMSMKDPKM
QVYKDDQVVV IKDKYPKARH HWLVLPWASI SSLKVVTSEH LELLKHMHAV GEKVIADFAG
SSKLRFRLGY HAIPSMSHVH LHVISQDFDS PCLKNKKHWN SFNTEYFLES QAVIKMVQEA
GRVTVKDGTC ELLKLPLRCH ECQQLLPSIP QLKEHLRKHW GG
