HIPK1_MOUSE
ID HIPK1_MOUSE Reviewed; 1210 AA.
AC O88904; A6H5Z7; Q80TV5; Q9QUQ8; Q9QZR3; Q9WVN7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Homeodomain-interacting protein kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=Nuclear body-associated kinase 2;
DE AltName: Full=Protein kinase Myak;
GN Name=Hipk1; Synonyms=Kiaa0630, Myak, Nbak2;
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 [MRNA] (ISOFORM 1), AND INTERACTION WITH NKX1-2 AND
RP NKX2-5.
RC STRAIN=BALB/cJ;
RX PubMed=9748262; DOI=10.1074/jbc.273.40.25875;
RA Kim Y.H., Choi C.Y., Lee S.-J., Conti M.A., Kim Y.;
RT "Homeodomain-interacting protein kinases, a novel family of co-repressors
RT for homeodomain transcription factors.";
RL J. Biol. Chem. 273:25875-25879(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=CD-1; TISSUE=Testis;
RX PubMed=10694743;
RX DOI=10.1002/(sici)1098-2795(200004)55:4<372::aid-mrd3>3.0.co;2-a;
RA Shang E., Wang X., Huang J., Yoshida W., Kuroiwa A., Wolgemuth D.J.;
RT "Murine Myak, a member of a family of yeast YAK1-related genes, is highly
RT expressed in hormonally modulated epithelia in the reproductive system and
RT in the embryonic central nervous system.";
RL Mol. Reprod. Dev. 55:372-378(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Sather S.L., Johnson N.L., Johnson G.L.;
RT "Protein kinases associated with PML/CBP nuclear bodies and filamentous
RT threads regulate transcription and inhibit cell growth.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 608-1209 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [6]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH DAXX,
RP AUTOPHOSPHORYLATION, AND MUTAGENESIS OF LYS-219.
RX PubMed=12529400; DOI=10.1128/mcb.23.3.950-960.2003;
RA Ecsedy J.A., Michaelson J.S., Leder P.;
RT "Homeodomain-interacting protein kinase 1 modulates Daxx localization,
RT phosphorylation, and transcriptional activity.";
RL Mol. Cell. Biol. 23:950-960(2003).
RN [7]
RP INTERACTION WITH TP53, AUTOPHOSPHORYLATION, AND FUNCTION.
RX PubMed=12702766; DOI=10.1073/pnas.0530308100;
RA Kondo S., Lu Y., Debbas M., Lin A.W., Sarosi I., Itie A., Wakeham A.,
RA Tuan J., Saris C., Elliott G., Ma W., Benchimol S., Lowe S.W., Mak T.W.,
RA Thukral S.K.;
RT "Characterization of cells and gene-targeted mice deficient for the p53-
RT binding kinase homeodomain-interacting protein kinase 1 (HIPK1).";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5431-5436(2003).
RN [8]
RP FUNCTION IN ANGIOGENESIS.
RX PubMed=16917507; DOI=10.1038/sj.emboj.7601273;
RA Aikawa Y., Nguyen L.A., Isono K., Takakura N., Tagata Y., Schmitz M.L.,
RA Koseki H., Kitabayashi I.;
RT "Roles of HIPK1 and HIPK2 in AML1- and p300-dependent transcription,
RT hematopoiesis and blood vessel formation.";
RL EMBO J. 25:3955-3965(2006).
RN [9]
RP DESUMOYLATION BY SENP1, AND SUBCELLULAR LOCATION.
RX PubMed=18219322; DOI=10.1038/sj.cdd.4402303;
RA Li X., Luo Y., Yu L., Lin Y., Luo D., Zhang H., He Y., Kim Y.-O., Kim Y.,
RA Tang S., Min W.;
RT "SENP1 mediates TNF-induced desumoylation and cytoplasmic translocation of
RT HIPK1 to enhance ASK1-dependent apoptosis.";
RL Cell Death Differ. 15:739-750(2008).
RN [10]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=20231426; DOI=10.1182/blood-2009-07-235093;
RA Hattangadi S.M., Burke K.A., Lodish H.F.;
RT "Homeodomain-interacting protein kinase 2 plays an important role in normal
RT terminal erythroid differentiation.";
RL Blood 115:4853-4861(2010).
RN [11]
RP FUNCTION IN EYE DEVELOPMENT, DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=20579985; DOI=10.1016/j.febslet.2010.06.020;
RA Inoue T., Kagawa T., Inoue-Mochita M., Isono K., Ohtsu N., Nobuhisa I.,
RA Fukushima M., Tanihara H., Taga T.;
RT "Involvement of the Hipk family in regulation of eyeball size, lens
RT formation and retinal morphogenesis.";
RL FEBS Lett. 584:3233-3238(2010).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in transcription
CC regulation and TNF-mediated cellular apoptosis. Plays a role as a
CC corepressor for homeodomain transcription factors. Phosphorylates DAXX
CC and MYB. Phosphorylates DAXX in response to stress, and mediates its
CC translocation from the nucleus to the cytoplasm. Inactivates MYB
CC transcription factor activity by phosphorylation. Prevents MAP3K5-JNK
CC activation in the absence of TNF. TNF triggers its translocation to the
CC cytoplasm in response to stress stimuli, thus activating nuclear
CC MAP3K5-JNK by derepression and promoting apoptosis. May be involved in
CC anti-oxidative stress responses. Involved in the regulation of eye
CC size, lens formation and retinal lamination during late embryogenesis.
CC Promotes angiogenesis and to be involved in erythroid differentiation.
CC May be involved in malignant squamous cell tumor formation.
CC Phosphorylates PAGE4 at 'Thr-51' which is critical for the ability of
CC PAGE4 to potentiate the transcriptional activator activity of JUN (By
CC similarity). {ECO:0000250|UniProtKB:Q86Z02,
CC ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:16917507,
CC ECO:0000269|PubMed:20231426, ECO:0000269|PubMed:20579985}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with Nkx1-2, Nkx2-5, MYB, PARK7, DAXX and p53/TP53.
CC Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in
CC response to TNF. This complex formation promotes MAP3K5-JNK activation
CC and subsequent apoptosis. {ECO:0000269|PubMed:12529400,
CC ECO:0000269|PubMed:12702766, ECO:0000269|PubMed:9748262}.
CC -!- INTERACTION:
CC O88904; O35613: Daxx; NbExp=3; IntAct=EBI-692945, EBI-77304;
CC O88904; P23804: Mdm2; NbExp=3; IntAct=EBI-692945, EBI-641788;
CC O88904; Q5EBH1: Rassf5; NbExp=5; IntAct=EBI-692945, EBI-960530;
CC O88904; Q9UER7: DAXX; Xeno; NbExp=3; IntAct=EBI-692945, EBI-77321;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12529400,
CC ECO:0000269|PubMed:18219322, ECO:0000269|PubMed:20579985}. Cytoplasm
CC {ECO:0000269|PubMed:12529400, ECO:0000269|PubMed:18219322,
CC ECO:0000269|PubMed:20579985}. Nucleus speckle
CC {ECO:0000269|PubMed:12529400}. Note=Predominantly nuclear. Translocates
CC from nucleus to cytoplasm in response to stress stimuli via SENP1-
CC mediated desumoylation. {ECO:0000269|PubMed:18219322}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=2b, Myak-L;
CC IsoId=O88904-1; Sequence=Displayed;
CC Name=2; Synonyms=2a;
CC IsoId=O88904-2; Sequence=VSP_013133;
CC Name=3; Synonyms=Myak-S;
CC IsoId=O88904-3; Sequence=VSP_013132, VSP_013134;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with high levels in
CC reproductive tissues. Expressed in the epithelial layer of mammary
CC gland, uterus and epididymis, in the corpus luteum, and in post-meiotic
CC round spermatids. {ECO:0000269|PubMed:10694743,
CC ECO:0000269|PubMed:12529400}.
CC -!- DEVELOPMENTAL STAGE: Highest at 12 dpc, where it is expressed primarily
CC in the central nervous system. Highly induced during primary fetal
CC liver erythropoiesis. Expressed in the inner retina during late
CC embryogenesis, predominantly in cytoplasm.
CC {ECO:0000269|PubMed:10694743, ECO:0000269|PubMed:20231426,
CC ECO:0000269|PubMed:20579985}.
CC -!- PTM: Phosphorylated and activated by JNK1 (By similarity).
CC Autophosphorylated. {ECO:0000250}.
CC -!- PTM: Sumoylated. When conjugated it is directed to nuclear speckles.
CC SENP1-mediated desumoylation is mediated by TNF in response to stress
CC stimuli, triggering transient translocation from nucleus to cytoplasm.
CC {ECO:0000269|PubMed:18219322}.
CC -!- DISRUPTION PHENOTYPE: Small eyes with deficient lens, abnormal retinal
CC lamination, and thickened retinas. {ECO:0000269|PubMed:20579985}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. HIPK subfamily. {ECO:0000305}.
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DR EMBL; AF077658; AAC63010.1; -; mRNA.
DR EMBL; AF071070; AAD41592.1; -; mRNA.
DR EMBL; AF071071; AAD41593.1; -; mRNA.
DR EMBL; AF170303; AAD52568.1; -; mRNA.
DR EMBL; AF170304; AAD52569.1; -; mRNA.
DR EMBL; BC145697; AAI45698.1; -; mRNA.
DR EMBL; BC145699; AAI45700.1; -; mRNA.
DR EMBL; AK122333; BAC65615.1; -; mRNA.
DR CCDS; CCDS38576.1; -. [O88904-1]
DR CCDS; CCDS79992.1; -. [O88904-2]
DR PIR; T14357; T14357.
DR RefSeq; NP_001288233.1; NM_001301304.1. [O88904-1]
DR RefSeq; NP_001288235.1; NM_001301306.1. [O88904-2]
DR RefSeq; NP_034562.2; NM_010432.2. [O88904-1]
DR AlphaFoldDB; O88904; -.
DR SMR; O88904; -.
DR BioGRID; 200306; 2.
DR IntAct; O88904; 5.
DR MINT; O88904; -.
DR STRING; 10090.ENSMUSP00000029438; -.
DR iPTMnet; O88904; -.
DR PhosphoSitePlus; O88904; -.
DR EPD; O88904; -.
DR jPOST; O88904; -.
DR MaxQB; O88904; -.
DR PaxDb; O88904; -.
DR PRIDE; O88904; -.
DR ProteomicsDB; 273113; -. [O88904-1]
DR ProteomicsDB; 273114; -. [O88904-2]
DR ProteomicsDB; 273115; -. [O88904-3]
DR Antibodypedia; 20149; 339 antibodies from 30 providers.
DR DNASU; 15257; -.
DR Ensembl; ENSMUST00000029438; ENSMUSP00000029438; ENSMUSG00000008730. [O88904-1]
DR Ensembl; ENSMUST00000106845; ENSMUSP00000102458; ENSMUSG00000008730. [O88904-2]
DR Ensembl; ENSMUST00000118317; ENSMUSP00000113998; ENSMUSG00000008730. [O88904-1]
DR GeneID; 15257; -.
DR KEGG; mmu:15257; -.
DR UCSC; uc008qtg.2; mouse. [O88904-1]
DR UCSC; uc012cve.1; mouse. [O88904-2]
DR CTD; 204851; -.
DR MGI; MGI:1314873; Hipk1.
DR VEuPathDB; HostDB:ENSMUSG00000008730; -.
DR eggNOG; KOG0667; Eukaryota.
DR GeneTree; ENSGT00940000155356; -.
DR HOGENOM; CLU_003045_1_0_1; -.
DR InParanoid; O88904; -.
DR OMA; SQERSNN; -.
DR OrthoDB; 59821at2759; -.
DR PhylomeDB; O88904; -.
DR TreeFam; TF105417; -.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR BioGRID-ORCS; 15257; 6 hits in 77 CRISPR screens.
DR ChiTaRS; Hipk1; mouse.
DR PRO; PR:O88904; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O88904; protein.
DR Bgee; ENSMUSG00000008730; Expressed in vestibular membrane of cochlear duct and 238 other tissues.
DR ExpressionAtlas; O88904; baseline and differential.
DR Genevisible; O88904; MM.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:DFLAT.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0034333; P:adherens junction assembly; IMP:CACAO.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:DFLAT.
DR GO; GO:0060059; P:embryonic retina morphogenesis in camera-type eye; IMP:DFLAT.
DR GO; GO:0072577; P:endothelial cell apoptotic process; ISO:MGI.
DR GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IGI:MGI.
DR GO; GO:0061072; P:iris morphogenesis; IMP:DFLAT.
DR GO; GO:0060235; P:lens induction in camera-type eye; IMP:DFLAT.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IMP:DFLAT.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR GO; GO:0010842; P:retina layer formation; IMP:DFLAT.
DR GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cytoplasm; Isopeptide bond; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Ubl conjugation.
FT CHAIN 1..1210
FT /note="Homeodomain-interacting protein kinase 1"
FT /id="PRO_0000085994"
FT DOMAIN 190..518
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 835..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 885..1093
FT /note="Interaction with TP53"
FT /evidence="ECO:0000269|PubMed:12702766"
FT REGION 891..998
FT /note="Required for localization to nuclear speckles"
FT /evidence="ECO:0000250"
FT REGION 902..926
FT /note="SUMO interaction motifs (SIM); required for nuclear
FT localization and kinase activity"
FT /evidence="ECO:0000250"
FT REGION 938..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 844..847
FT /note="Nuclear localization signal 1 (NLS1)"
FT /evidence="ECO:0000250"
FT COMPBIAS 938..964
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 315
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 196..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Z02"
FT MOD_RES 1200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86Z02"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 25
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q86Z02"
FT CROSSLNK 120
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86Z02"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86Z02"
FT CROSSLNK 991
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q86Z02"
FT CROSSLNK 1203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 661..719
FT /note="TGLQATTKHSGFPVRMDNAVPIVPQAPAAQPLQIQSGVLTQGSCTPLMVATL
FT HPQVATI -> KSEQAEGNEGLGETESSPGGQESGSGVSQGETTGGAQEQIHNPWTTSN
FT NKAFWIPCEDG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10694743"
FT /id="VSP_013132"
FT VAR_SEQ 702..746
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_013133"
FT VAR_SEQ 720..1209
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10694743"
FT /id="VSP_013134"
FT MUTAGEN 219
FT /note="K->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:12529400"
FT CONFLICT 732
FT /note="Missing (in Ref. 1; AAC63010)"
FT /evidence="ECO:0000305"
FT CONFLICT 921
FT /note="K -> E (in Ref. 1; AAC63010)"
FT /evidence="ECO:0000305"
FT CONFLICT 953
FT /note="H -> Y (in Ref. 5; BAC65615)"
FT /evidence="ECO:0000305"
FT CONFLICT 954
FT /note="P -> S (in Ref. 1; AAC63010 and 5; BAC65615)"
FT /evidence="ECO:0000305"
FT CONFLICT 1134
FT /note="S -> F (in Ref. 1; AAC63010)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1210 AA; 130723 MW; 26D264B883220640 CRC64;
MASQLQVFSP PSVSSSAFCS AKKLKIEPSG WDVSGQSSND KYYTHSKTLP ATQGQASSSH
QVANFNLPAY DQGLLLPAPA VEHIVVTAAD SSGSAATATF QSSQTLTHRS NVSLLEPYQK
CGLKRKSEEV ESNGSVQIIE EHPPLMLQNR TVVGAAATTT TVTTKSSSSS GEGDYQLVQH
EILCSMTNSY EVLEFLGRGT FGQVAKCWKR STKEIVAIKI LKNHPSYARQ GQIEVSILSR
LSSENADEYN FVRSYECFQH KNHTCLVFEM LEQNLYDFLK QNKFSPLPLK YIRPILQQVA
TALMKLKSLG LIHADLKPEN IMLVDPVRQP YRVKVIDFGS ASHVSKAVCS TYLQSRYYRA
PEIILGLPFC EAIDMWSLGC VIAELFLGWP LYPGASEYDQ IRYISQTQGL PAEYLLSAGT
KTTRFFNRDP NLGYPLWRLK TPEEHELETG IKSKEARKYI FNCLDDMAQV NMSTDLEGTD
MLAEKADRRE YIDLLKKMLT IDADKRITPL KTLNHQFVTM SHLLDFPHSS HVKSCFQNME
ICKRRVHMYD TVSQIKSPFT THVAPNTSTN LTMSFSNQLN TVHNQASVLA SSSTAAAATL
SLANSDVSLL NYQSALYPSS AAPVPGVAQQ GVSLQPGTTQ ICTQTDPFQQ TFIVCPPAFQ
TGLQATTKHS GFPVRMDNAV PIVPQAPAAQ PLQIQSGVLT QGSCTPLMVA TLHPQVATIT
PQYAVPFTLS CAAGRPALVE QTAAVLQAWP GGTQQILLPS AWQQLPGVAL HNSVQPAAVI
PEAMGSSQQL ADWRNAHSHG NQYSTIMQQP SLLTNHVTLA TAQPLNVGVA HVVRQQQSSS
LPSKKNKQSA PVSSKSSLEV LPSQVYSLVG SSPLRTTSSY NSLVPVQDQH QPIIIPDTPS
PPVSVITIRS DTDEEEDNKY KPNSSSLKAR SNVISYVTVN DSPDSDSSLS SPHPTDTLSA
LRGNSGTLLE GPGRPAADGI GTRTIIVPPL KTQLGDCTVA TQASGLLSSK TKPVASVSGQ
SSGCCITPTG YRAQRGGASA VQPLNLSQNQ QSSSASTSQE RSSNPAPRRQ QAFVAPLSQA
PYAFQHGSPL HSTGHPHLAP APAHLPSQPH LYTYAAPTSA AALGSTSSIA HLFSPQGSSR
HAAAYTTHPS TLVHQVPVSV GPSLLTSASV APAQYQHQFA TQSYIGSSRG STIYTGYPLS
PTKISQYSYL
