ID A0A2K5MCR0_CERAT Unreviewed; 1315 AA.
AC A0A2K5MCR0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Poly [ADP-ribose] polymerase {ECO:0000256|RuleBase:RU362114};
DE Short=PARP {ECO:0000256|RuleBase:RU362114};
DE EC=2.4.2.- {ECO:0000256|RuleBase:RU362114};
GN Name=TNKS2 {ECO:0000313|Ensembl:ENSCATP00000022995.1};
OS Cercocebus atys (Sooty mangabey) (Cercocebus torquatus atys).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Cercocebus.
OX NCBI_TaxID=9531 {ECO:0000313|Ensembl:ENSCATP00000022995.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000022995.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00033987};
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR STRING; 9531.ENSCATP00000022995; -.
DR Ensembl; ENSCATT00000047207.1; ENSCATP00000022995.1; ENSCATG00000035054.1.
DR GeneTree; ENSGT00940000159911; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000035054; Expressed in thymus and 12 other cell types or tissues.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005635; C:nuclear envelope; IEA:Ensembl.
DR GO; GO:0000242; C:pericentriolar material; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:1990404; F:NAD+-protein ADP-ribosyltransferase activity; IEA:Ensembl.
DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:1904355; P:positive regulation of telomere capping; IEA:Ensembl.
DR GO; GO:0070213; P:protein auto-ADP-ribosylation; IEA:Ensembl.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; IEA:Ensembl.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:Ensembl.
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 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; 6.
DR Pfam; PF13637; Ank_4; 1.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF07647; SAM_2; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 15.
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; 14.
DR PROSITE; PS50088; ANK_REPEAT; 15.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000256|RuleBase:RU362114}; Membrane {ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|RuleBase:RU362114};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Reference proteome {ECO:0000313|Proteomes:UP000233060};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU362114};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 124..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 206..238
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 239..271
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 272..304
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 359..391
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 392..424
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 425..457
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 512..547
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 548..580
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 581..613
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 674..706
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 707..739
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 740..772
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 827..859
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 860..892
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 893..925
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1026..1085
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 1108..1313
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1315 AA; 141911 MW; 95C10329C5DC3750 CRC64;
MAVGLSPFSR RRSLSPHISH KPFSAPRSPK PARPVPGHCA RAERRHVRSQ GLAELAGGAL
PASAAASLQV SDGGFALPPP LRGSRGAGSQ ARGARWRGHG TEPDPVTAGS RAARALSASS
PGGLALLLVG PGLLLPLLAL LLAVAAARIM SGRRCAGGGA ASASAAAEAM EPAARELFEA
CRNGDVERVK RLVTPEKVNS RDTAGRKSTP LHFAAGFGRK DVVEYLLQNG ANVQARDDGG
LIPLHNACSF GHAEVVNLLL RHGADPNARD NWNYTPLHEA AIKGKIDVCI VLLQHGAEPT
IRNTDGRTAL DLADPSAKAV LTGEYKKDEL LESARSGNEE KMMALLTPLN VNCHASDGRK
STPLHLAAGY NRVKIVQLLL QHGADVHAKD KGDLVPLHNA CSYGHYEVTE LLVKHGACVN
AMDLWQFTPL HEAASKNRVE VCSLLLSYGA DPTLLNCHNK SAIDLAPTPQ LKERLAYEFK
GHSLLQAARE ADVTRIKKHL SLEMVNFKHP QTHETALHCA AASPYPKRKQ ICELLLRKGA
NINEKTKEFL TPLHVASEKA HNDVVEVVVK HEAKVNALDN LGQTSLHRAA YCGHLQTCRL
LLSYGCDPNI ISLQGFTALQ MGNENVQQLL QEGISLGNSE ADRQLLEAAK AGDVETVKKL
CTVQSVNCRD IEGRQSTPLH FAAGYNRVSV VEYLLQHGAD VHAKDKGGLV PLHNACSYGH
YEVAELLVKH GAVVNVADLW KFTPLHEAAA KGKYEICKLL LQHGADPTKK NRDGNTPLDL
VKDGDTDIQD LLRGDAALLD AAKKGCLARV KKLSSPDNVN CRDTQGRHST PLHLAAGYNN
LEVAEYLLQH GADVNAQDKG GLIPLHNAAS YGHVDVAALL IKYNACVNAT DKWAFTPLHE
AAQKGRTQLC ALLLAHGADP TLKNQEGQTP LDLVSADDVS ALLTAAMPPS ALPSCYKPQV
LNGVRSPGAA ADALSSGPSS PSSLSAASSL DNLSGSFSEL SSVVSSSGTE GASGLEKKEV
PGVDFSITQF VRNLGLEHLM DIFEREQITL DVLVEMGHKE LKEIGINAYG HRHKLIKGVE
RLISGQQGLN PYLTLNTSGS GTILIDLSPD DKEFQSVEEE MQSTVREHRD GGHAGGIFNR
YNILKIQKVC NKKLWERYTH RRKEVSEENH NHANERMLFH GSPFVNAIIH KGFDERHAYI
GGMFGAGIYF AENSSKSNQY VYGIGGGTGC PVHKDRSCYI CHRQLLFCRV TLGKSFLQFS
AMKMAHSPPG HHSVTGRPSV NGLALAEYVI YRGEQAYPEY LITYQIMRPE GMVDG
//
