ID A0A3P8XXL4_ESOLU Unreviewed; 722 AA.
AC A0A3P8XXL4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 2.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Poly(ADP-ribose) polymerase family member 9 {ECO:0000313|Ensembl:ENSELUP00000009193.2};
OS Esox lucius (Northern pike).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Esociformes;
OC Esocidae; Esox.
OX NCBI_TaxID=8010 {ECO:0000313|Ensembl:ENSELUP00000009193.2, ECO:0000313|Proteomes:UP000265140};
RN [1] {ECO:0000313|Ensembl:ENSELUP00000009193.2, ECO:0000313|Proteomes:UP000265140}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25069045;
RA Rondeau E.B., Minkley D.R., Leong J.S., Messmer A.M., Jantzen J.R.,
RA von Schalburg K.R., Lemon C., Bird N.H., Koop B.F.;
RT "The genome and linkage map of the northern pike (Esox lucius): conserved
RT synteny revealed between the salmonid sister group and the Neoteleostei.";
RL PLoS ONE 9:e102089-e102089(2014).
RN [2] {ECO:0000313|Ensembl:ENSELUP00000009193.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the ARTD/PARP family.
CC {ECO:0000256|ARBA:ARBA00024347}.
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DR AlphaFoldDB; A0A3P8XXL4; -.
DR Ensembl; ENSELUT00000004276.2; ENSELUP00000009193.2; ENSELUG00000009784.2.
DR GeneTree; ENSGT00940000158837; -.
DR Proteomes; UP000265140; LG11.
DR Bgee; ENSELUG00000009784; Expressed in stomach and 14 other cell types or tissues.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:InterPro.
DR CDD; cd02907; Macro_Af1521_BAL-like; 1.
DR Gene3D; 3.90.228.10; -; 1.
DR Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 2.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR012317; Poly(ADP-ribose)pol_cat_dom.
DR PANTHER; PTHR14453; PARP/ZINC FINGER CCCH TYPE DOMAIN CONTAINING PROTEIN; 1.
DR PANTHER; PTHR14453:SF70; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP9; 1.
DR Pfam; PF01661; Macro; 2.
DR SMART; SM00506; A1pp; 1.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52949; Macro domain-like; 2.
DR PROSITE; PS51154; MACRO; 2.
DR PROSITE; PS51059; PARP_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000265140}.
FT DOMAIN 55..244
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 289..453
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 531..722
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
FT REGION 260..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 80435 MW; 59E15D1A3BD95B8F CRC64;
MAKTHAIPLD TEMVSILKQC GTTFTYVLQS KFGCKAVLHG VEAASTARYK KPSPDKRFSV
QLVSGISLSV WMDDLTTHNA EAVVNAANMD LQHCGGLALA LSNAGGPSIQ KESDEYTKAK
GRLETGDAII TNSGSLPCKK IIHAVGPCLP NNPTENEIKK AIPKLRRTIL SILKEVRKEN
LKSVAIPAIS SGLFHFPLDL CADVIVKTLI EYNSTYNGDP FEVRLVNHDE PSVRKMESAC
KNILSSLAAH MLSHPPAAQW QASSHSPLRM TQPSKSSYSN AVSHRTKSTP HQHSFKINNV
SLNVSTGYIE KQKTCSIVNT ISPDLDLSAG EISRSILKMA GLGIQEEIRN QFYPGIYGDV
IVTTGHNLSC SVVYHTICPK RTDQRSEKAF ENKLKSLRGA ASYPSSFNSF SFTEHESRTD
HYDSRDAVKS AQEYIELTTA CDEMLREALR WYNDMLTNKH GFSIHNNFIQ HFGQEEMDEL
LNIQTKWGVF IKVFFQDGYA GVNLQVVSGD IRPAVLEVEA MCCQVQEDFA KEEERDMCLK
TPISFSRKPL DANSAVYREK LKTFSGFQIV RVEKLENSSL RQLFDLKKKQ LQVSTTPKLM
YQRLPAQFCN LLSRVGFQRE FAPPYEQKQG AGIYFSSSVK QAEKLWKGLA DEEYMYFVEA
VVLTGKSTVG SPDLIVPPEI HSGDPFSLYD SVTGGIDTHV IFNGHQALPE YLIICTQKNT
LN
//
