ID W5KSG1_ASTMX Unreviewed; 1724 AA.
AC W5KSG1;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 27-MAR-2024, entry version 45.
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};
OS Astyanax mexicanus (Blind cave fish) (Astyanax fasciatus mexicanus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC Characoidei; Characidae; Astyanax.
OX NCBI_TaxID=7994 {ECO:0000313|Ensembl:ENSAMXP00000010523.2, ECO:0000313|Proteomes:UP000018467};
RN [1] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RA Jeffery W., Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000018467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=female {ECO:0000313|Proteomes:UP000018467};
RX PubMed=25329095; DOI=10.1038/ncomms6307;
RA McGaugh S.E., Gross J.B., Aken B., Blin M., Borowsky R., Chalopin D.,
RA Hinaux H., Jeffery W.R., Keene A., Ma L., Minx P., Murphy D., O'Quin K.E.,
RA Retaux S., Rohner N., Searle S.M., Stahl B.A., Tabin C., Volff J.N.,
RA Yoshizawa M., Warren W.C.;
RT "The cavefish genome reveals candidate genes for eye loss.";
RL Nat. Commun. 5:5307-5307(2014).
RN [3] {ECO:0000313|Ensembl:ENSAMXP00000010523.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR Ensembl; ENSAMXT00000010523.2; ENSAMXP00000010523.2; ENSAMXG00000010209.2.
DR eggNOG; KOG2633; Eukaryota.
DR GeneTree; ENSGT00940000165390; -.
DR HOGENOM; CLU_003288_1_0_1; -.
DR InParanoid; W5KSG1; -.
DR Proteomes; UP000018467; Unassembled WGS sequence.
DR Bgee; ENSAMXG00000010209; Expressed in pharyngeal gill and 10 other cell types or tissues.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 4.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR14453; PARP/ZINC FINGER CCCH TYPE DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14453:SF101; POLY [ADP-RIBOSE] POLYMERASE; 1.
DR Pfam; PF01661; Macro; 4.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00506; A1pp; 4.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52949; Macro domain-like; 4.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS51154; MACRO; 4.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|RuleBase:RU362114};
KW NAD {ECO:0000256|RuleBase:RU362114};
KW Reference proteome {ECO:0000313|Proteomes:UP000018467};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 490..675
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 701..875
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 889..1063
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1124..1297
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1435..1509
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1522..1724
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 1067..1127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1123
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1724 AA; 189528 MW; 608CD7F7509DEBE5 CRC64;
MLFYPSLQKA LRGKSPDLSE ITTKFSFPVC KEVLGFIETN EKHKNEFQDQ LKKVHANLVF
DKIPSTQEIK LEMDVDMESL AVLHLGPAWE GTARRQADAF LMKYSTAELA AEVELWKRIK
EDCHQLISSD VDISFEETKG KIVLVGLKEV VSTLSTKVQN LLKEAATELE VEMNTVDRVI
QLNSKEVFEL VAERVHSKIS SEVFSTDESS LTFRLKDLKD VVSADEKVIN LVKHSIVLHD
LRFSPHLLQF LKSLDLKKFE QDHFASSHIA AYFQRDGDHL GILVETENIT KAEDKLKELL
KEEVIHVTSD LTAVKTSENW LNFLKTLEAE VKFSHNAHRV TITPSEKEIV ICGFAPVVAD
LSHKVRDYLE NKTPETAEIQ LKSLRELEFV DSCVNLSEVP EIRDLGVTVL ACRTDVTPCL
KVTAAKENIQ DAKSVVMKHV SSIAVETLAY SKAGESKVIH KHEANVKAKA KEWNCQAYLS
IEKASSTTPT KSYTHKISNC LSLTIADGDL LKHTAEAYVC PMNSKLIFDN PVAQKFLQVA
GPQIQAICSK VQKEKQSLLA GDTVISETGL LNAKTLIYAV LPQSDQSLST CYMESAIHDS
LQKAETSKSA SVAMPVIGCG PFGFSVKDSC MAIRKAILKF SSCHQHSPSS IKDILVVDSN
PDVVEEFNNL ISQLGFPNVS ASTSFAKTTS MSPLKPVKPK PGSDTEVTVH GVLVSLKKGD
ITKETVDVIV NSNNSALDLN TGVSGAILAA AGQSVVDECK KHGPQKADGV VLTGGGNLSC
KHIAQMVGPN NAADITLSIE KVLKLCEGQT AATVAIPAIG TGRGGIGTKD SIKAIITGLE
NHMAQVQTSC LNEITVVAFE QKVYDSYCDY FKERNKKPSL IVAQTAHTKM PDNQVKVAGV
RIEVKKGNIT NETVRGIVNT TNNQMNLTSG VSGAIFKAAG PSVQQECQNH GPLQSDTVAV
TSAGNMQCDF IIHMMGPHSA AEAQLRVRKV LERCEEKQIS TVSFPAVGTG GGGVKGAEAI
TAILQGFEDH LSQRTSTAIK LIYVVVDRDE VLNEFLQGLK QWTSKTKIEM QDSDEESEGS
VCGDDSDEWE DEESLIASGE DEEYEEEEEE EEEEEEEEED DHISGTTTEA IIGRIKVKVI
CGDITKDTTE AIVSSTNTNL NLSSGVSGAI LKAAGQTVVD ECKKLGPQPS DGVVLTKAGN
LPFKNIVHMV GQTSEKEITR CMYNVLKKCE ENKIQSVSFP ALGTGAGNLA AGQVAKAMLD
SVANFAIDSP AFLKTVHIVI FQAKMLPDFE GALKTFKKIS PKPSPVSKPK PVKQTLPVTK
PSKAPLCLST ETAGVTFPVM KVEVYGTSRA DLAKVKTFLD NLVNEECITT DISSEHLPSL
PEADKETIVS LSQSNEVQVH VLAVDKLTVS GKKDDVYEAV LKINSFLQAA KERELLKVEE
KRLSKTLRWE VADREKWVPL DSSISYQLEL AFYRKDQNYS YQEKGETYTV DFKDLKRVNS
KGQSCNVKRT LLGDAETAII HPPPTWTKMG GKDLEIVALS KSDEYKKIEQ DFINCSKHAA
VAPVQVVEIH RIQNKGLWQR YCVLKQEVDK KYPKQTNERV LYHGTTLEIC QKINKNGFNR
SFCGRNAVVH GEGTYFAKDA WYSCQDQYSN PDPNGLKYIY RARVVTGSPC KSRKGMKEPD
PLDPNNHQAG LHNCAVDNLQ NPFIFVVFCD AGAYPDYLIT FKSV
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