ID   TNKS1_MOUSE             Reviewed;        1320 AA.
AC   Q6PFX9; Q8BX62;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 167.
DE   RecName: Full=Poly [ADP-ribose] polymerase tankyrase-1 {ECO:0000305};
DE            EC=2.4.2.30 {ECO:0000250|UniProtKB:O95271};
DE   AltName: Full=ADP-ribosyltransferase diphtheria toxin-like 5;
DE            Short=ARTD5;
DE   AltName: Full=Protein poly-ADP-ribosyltransferase tankyrase-1 {ECO:0000305};
DE            EC=2.4.2.- {ECO:0000250|UniProtKB:O95271};
DE   AltName: Full=TRF1-interacting ankyrin-related ADP-ribose polymerase 1;
DE            Short=Tankyrase I;
DE   AltName: Full=Tankyrase-1;
DE            Short=TANK1;
GN   Name=Tnks; Synonyms=Tnks1;
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] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; 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).
CC   -!- FUNCTION: Poly-ADP-ribosyltransferase involved in various processes
CC       such as Wnt signaling pathway, telomere length and vesicle trafficking.
CC       Acts as an activator of the Wnt signaling pathway by mediating poly-
CC       ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of
CC       the beta-catenin destruction complex: poly-ADP-ribosylated target
CC       proteins are recognized by RNF146, which mediates their ubiquitination
CC       and subsequent degradation. Also mediates PARsylation of BLZF1 and
CC       CASC3, followed by recruitment of RNF146 and subsequent ubiquitination.
CC       Mediates PARsylation of TERF1, thereby contributing to the regulation
CC       of telomere length. Involved in centrosome maturation during
CC       prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also
CC       regulate vesicle trafficking and modulate the subcellular distribution
CC       of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly
CC       through PARsylation of NUMA1. Stimulates 26S proteasome activity.
CC       {ECO:0000250|UniProtKB:O95271}.
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:0000250|UniProtKB:O95271};
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:0000305};
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:0000305};
CC   -!- SUBUNIT: Oligomerizes and associates with TNKS2. Interacts with the
CC       cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to
CC       the N-terminus of telomeric TERF1 via the ANK repeats. Found in a
CC       complex with POT1; TERF1 and TINF2. Interacts with AXIN1. Interacts
CC       with AXIN2. Interacts with BLZF1 and CASC3. Interacts with NUMA1.
CC       {ECO:0000250|UniProtKB:O95271}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95271}. Golgi
CC       apparatus membrane {ECO:0000250|UniProtKB:O95271}; Peripheral membrane
CC       protein {ECO:0000250|UniProtKB:O95271}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:O95271}. Nucleus, nuclear pore complex
CC       {ECO:0000250|UniProtKB:O95271}. Chromosome, telomere
CC       {ECO:0000250|UniProtKB:O95271}. Cytoplasm, cytoskeleton, spindle pole
CC       {ECO:0000250|UniProtKB:O95271}. Note=Associated with the Golgi and with
CC       juxtanuclear SLC2A4/GLUT4-vesicles. A minor proportion is also found at
CC       nuclear pore complexes and around the pericentriolar matrix of mitotic
CC       centromeres. During interphase, a small fraction of TNKS is found in
CC       the nucleus, associated with TERF1. Localizes to spindle poles at
CC       mitosis onset via interaction with NUMA1.
CC       {ECO:0000250|UniProtKB:O95271}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6PFX9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6PFX9-2; Sequence=VSP_041320;
CC   -!- PTM: Phosphorylated on serine residues by MAPK kinases upon insulin
CC       stimulation. Phosphorylated during mitosis.
CC       {ECO:0000250|UniProtKB:O95271}.
CC   -!- PTM: Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to
CC       its degradation. {ECO:0000250|UniProtKB:O95271}.
CC   -!- PTM: ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is
CC       recognized by RNF146, followed by ubiquitination.
CC       {ECO:0000250|UniProtKB:O95271}.
CC   -!- SIMILARITY: Belongs to the ARTD/PARP family. {ECO:0000305}.
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DR   EMBL; AK048860; BAC33475.1; -; mRNA.
DR   EMBL; AC122458; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC057370; AAH57370.1; -; mRNA.
DR   CCDS; CCDS22242.1; -. [Q6PFX9-1]
DR   RefSeq; NP_780300.2; NM_175091.3. [Q6PFX9-1]
DR   PDB; 3UTM; X-ray; 2.00 A; A/B=308-655.
DR   PDB; 4N4T; X-ray; 2.32 A; A/B=1097-1307.
DR   PDB; 5HKP; X-ray; 2.20 A; A/B=308-655.
DR   PDB; 6CF6; X-ray; 1.93 A; A/B=308-655.
DR   PDBsum; 3UTM; -.
DR   PDBsum; 4N4T; -.
DR   PDBsum; 5HKP; -.
DR   PDBsum; 6CF6; -.
DR   AlphaFoldDB; Q6PFX9; -.
DR   SMR; Q6PFX9; -.
DR   BioGRID; 204263; 22.
DR   DIP; DIP-61463N; -.
DR   IntAct; Q6PFX9; 21.
DR   MINT; Q6PFX9; -.
DR   STRING; 10090.ENSMUSP00000033929; -.
DR   BindingDB; Q6PFX9; -.
DR   ChEMBL; CHEMBL3232702; -.
DR   GlyGen; Q6PFX9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6PFX9; -.
DR   PhosphoSitePlus; Q6PFX9; -.
DR   EPD; Q6PFX9; -.
DR   MaxQB; Q6PFX9; -.
DR   PaxDb; 10090-ENSMUSP00000033929; -.
DR   PeptideAtlas; Q6PFX9; -.
DR   ProteomicsDB; 258936; -. [Q6PFX9-1]
DR   ProteomicsDB; 258937; -. [Q6PFX9-2]
DR   Antibodypedia; 22078; 405 antibodies from 36 providers.
DR   DNASU; 21951; -.
DR   Ensembl; ENSMUST00000033929.6; ENSMUSP00000033929.5; ENSMUSG00000031529.6. [Q6PFX9-1]
DR   GeneID; 21951; -.
DR   KEGG; mmu:21951; -.
DR   UCSC; uc009lku.1; mouse. [Q6PFX9-1]
DR   AGR; MGI:1341087; -.
DR   CTD; 8658; -.
DR   MGI; MGI:1341087; Tnks.
DR   VEuPathDB; HostDB:ENSMUSG00000031529; -.
DR   eggNOG; KOG4177; Eukaryota.
DR   GeneTree; ENSGT00940000156161; -.
DR   HOGENOM; CLU_004303_0_0_1; -.
DR   InParanoid; Q6PFX9; -.
DR   OMA; TAETINC; -.
DR   OrthoDB; 5477658at2759; -.
DR   PhylomeDB; Q6PFX9; -.
DR   TreeFam; TF326036; -.
DR   Reactome; R-MMU-201681; TCF dependent signaling in response to WNT.
DR   Reactome; R-MMU-4641257; Degradation of AXIN.
DR   Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR   Reactome; R-MMU-8948751; Regulation of PTEN stability and activity.
DR   BioGRID-ORCS; 21951; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Tnks; mouse.
DR   PRO; PR:Q6PFX9; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q6PFX9; Protein.
DR   Bgee; ENSMUSG00000031529; Expressed in manus and 234 other cell types or tissues.
DR   ExpressionAtlas; Q6PFX9; baseline and differential.
DR   GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0097431; C:mitotic spindle pole; ISS:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR   GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042393; F:histone binding; ISO:MGI.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0031670; P:cellular response to nutrient; IEA:Ensembl.
DR   GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR   GO; GO:1904908; P:negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric; ISO:MGI.
DR   GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:MGI.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:1904355; P:positive regulation of telomere capping; ISO:MGI.
DR   GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0070213; P:protein auto-ADP-ribosylation; ISS:UniProtKB.
DR   GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:MGI.
DR   GO; GO:0070212; P:protein poly-ADP-ribosylation; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISS:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd09524; SAM_tankyrase1_2; 1.
DR   CDD; cd01438; tankyrase_like; 1.
DR   Gene3D; 3.90.228.10; -; 1.
DR   Gene3D; 6.20.320.10; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 5.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   IDEAL; IID50231; -.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   PANTHER; PTHR24189:SF66; M-PHASE PHOSPHOPROTEIN 8; 1.
DR   PANTHER; PTHR24189; MYOTROPHIN; 1.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12796; Ank_2; 5.
DR   Pfam; PF13637; Ank_4; 2.
DR   Pfam; PF00644; PARP; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 17.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 3.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 15.
DR   PROSITE; PS51059; PARP_CATALYTIC; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   Genevisible; Q6PFX9; MM.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Alternative splicing; ANK repeat;
KW   Cell cycle; Cell division; Chromosome; Cytoplasm; Cytoskeleton;
KW   Glycosyltransferase; Golgi apparatus; Membrane; Metal-binding; Mitosis;
KW   mRNA transport; NAD; Nuclear pore complex; Nucleotidyltransferase; Nucleus;
KW   Phosphoprotein; Protein transport; Reference proteome; Repeat; Telomere;
KW   Transferase; Translocation; Transport; Ubl conjugation;
KW   Wnt signaling pathway; Zinc.
FT   CHAIN           1..1320
FT                   /note="Poly [ADP-ribose] polymerase tankyrase-1"
FT                   /id="PRO_0000409511"
FT   REPEAT          174..202
FT                   /note="ANK 1"
FT   REPEAT          208..237
FT                   /note="ANK 2"
FT   REPEAT          241..270
FT                   /note="ANK 3"
FT   REPEAT          274..303
FT                   /note="ANK 4"
FT   REPEAT          361..390
FT                   /note="ANK 5"
FT   REPEAT          394..423
FT                   /note="ANK 6"
FT   REPEAT          427..456
FT                   /note="ANK 7"
FT   REPEAT          514..546
FT                   /note="ANK 8"
FT   REPEAT          550..579
FT                   /note="ANK 9"
FT   REPEAT          583..612
FT                   /note="ANK 10"
FT   REPEAT          676..705
FT                   /note="ANK 11"
FT   REPEAT          709..738
FT                   /note="ANK 12"
FT   REPEAT          742..771
FT                   /note="ANK 13"
FT   REPEAT          775..803
FT                   /note="ANK 14"
FT   REPEAT          829..858
FT                   /note="ANK 15"
FT   REPEAT          862..891
FT                   /note="ANK 16"
FT   REPEAT          895..924
FT                   /note="ANK 17"
FT   REPEAT          928..957
FT                   /note="ANK 18"
FT   DOMAIN          1019..1082
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   DOMAIN          1105..1310
FT                   /note="PARP catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00397"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          111..152
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..44
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1227
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O95271"
FT   BINDING         1230
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O95271"
FT   BINDING         1235
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O95271"
FT   BINDING         1238
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O95271"
FT   VAR_SEQ         1..344
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_041320"
FT   CONFLICT        969
FT                   /note="L -> V (in Ref. 1; BAC33475)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1025
FT                   /note="S -> I (in Ref. 1; BAC33475)"
FT                   /evidence="ECO:0000305"
FT   HELIX           317..338
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           341..347
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   TURN            350..354
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           365..371
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           375..383
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           398..404
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           408..416
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           431..437
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           441..449
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           464..467
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           471..491
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           495..501
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   TURN            502..504
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   TURN            512..514
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           518..524
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           530..539
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           554..560
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           564..572
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           587..593
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           597..605
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           620..623
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   HELIX           626..633
FT                   /evidence="ECO:0007829|PDB:6CF6"
FT   STRAND          1100..1103
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   HELIX           1109..1120
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   TURN            1126..1132
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   STRAND          1138..1147
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   HELIX           1149..1165
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   STRAND          1172..1177
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   HELIX           1182..1188
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   HELIX           1192..1194
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   STRAND          1203..1209
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   HELIX           1211..1215
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   TURN            1216..1219
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   HELIX           1221..1223
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   TURN            1228..1230
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   STRAND          1236..1238
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   STRAND          1240..1248
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   STRAND          1251..1256
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   STRAND          1269..1273
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   STRAND          1284..1288
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   HELIX           1290..1292
FT                   /evidence="ECO:0007829|PDB:4N4T"
FT   STRAND          1293..1303
FT                   /evidence="ECO:0007829|PDB:4N4T"
SQ   SEQUENCE   1320 AA;  140944 MW;  A90360DC665FFCC0 CRC64;
     MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGPTPASPTA GGLAPFASPR
     HGLALPEGDG SRDPPDRPRS PDPVDGAVCT VAAPAAVPAA SAAVGVAPTP AGGGGGGGNN
     SASSASSPTS SSSSSPSSPG SSLAESPEAA GVGSTATLGA GAAGLGPGVP AVSGALRELL
     EACRNGDVSR VKRLVDAANV NAKDMAGRKS SPLHFAAGFG RKDVVEHLLQ MGANVHARDD
     GGLIPLHNAC SFGHAEVVSL LLCQGADPNA RDNWNYTPLH EAAIKGKIDV CIVLLQHGAD
     PNIRNTDGKS ALDLADPSAK AVLTGEYKKD ELLEAARSGN EEKLMALLTP LNVNCHASDG
     RKSTPLHLAA GYNRVRIVQL LLQHGADVHA KDKGGLVPLH NACSYGHYEV TELLLKHGAC
     VNAMDLWQFT PLHEAASKNR VEVCSLLLSH GADPTLVNCH GKSAVDMAPT PELRERLTYE
     FKGHSLLQAA READLAKVKK TLALEIINFK QPQSHETALH CAVASLHPKR KQVAELLLRK
     GANVNEKNKD FMTPLHVAAE RAHNDVMEVL HKHGAKMNAL DSLGQTALHR AALAGHLQTC
     RLLLSYGSDP SIISLQGFTA AQMGNEAVQQ ILSESTPMRT SDVDYRLLEA SKAGDLETVK
     QLCSPQNVNC RDLEGRHSTP LHFAAGYNRV SVVEYLLHHG ADVHAKDKGG LVPLHNACSY
     GHYEVAELLV RHGASVNVAD LWKFTPLHEA AAKGKYEICK LLLKHGADPT KKNRDGNTPL
     DLVKEGDTDI QDLLRGDAAL LDAAKKGCLA RVQKLCTPEN INCRDTQGRN STPLHLAAGY
     NNLEVAEYLL EHGADVNAQD KGGLIPLHNA ASYGHVDIAA LLIKYNTCVN ATDKWAFTPL
     HEAAQKGRTQ LCALLLAHGA DPTMKNQEGQ TPLDLATADD IRALLIDAMP PEALPTCFKP
     QATVVSASLI SPASTPSCLS AASSIDNLTG PLTDLAVGGA SNAGDGAAGA ERKEGEVAGL
     DMNISQFLKS LGLEHLRDIF ETEQITLDVL ADMGHEELKE IGINAYGHRH KLIKGVERLL
     GGQQGTNPYL TFHCVNQGTI LLDLAPEDKE YQSVEEEMQS TIREHRDGGN AGGIFNRYNV
     IRIQKVVNKK LRERFCHRQK EVSEENHNHH NERMLFHGSP FINAIIHKGF DERHAYIGGM
     FGAGIYFAEN SSKSNQYVYG IGGGTGCPTH KDRSCYICHR QMLFCRVTLG KSFLQFSTMK
     MAHAPPGHHS VIGRPSVNGL AYAEYVIYRG EQAYPEYLIT YQIMKPEAPS QTATAAEQKT
//