ID A0A2K5M4M5_CERAT Unreviewed; 1800 AA.
AC A0A2K5M4M5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=PARP14 {ECO:0000313|Ensembl:ENSCATP00000020127.1};
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:ENSCATP00000020127.1, ECO:0000313|Proteomes:UP000233060};
RN [1] {ECO:0000313|Ensembl:ENSCATP00000020127.1}
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 RefSeq; XP_011923931.1; XM_012068541.1.
DR STRING; 9531.ENSCATP00000020127; -.
DR Ensembl; ENSCATT00000044313.1; ENSCATP00000020127.1; ENSCATG00000033839.1.
DR GeneID; 105589781; -.
DR KEGG; caty:105589781; -.
DR CTD; 54625; -.
DR GeneTree; ENSGT00940000154311; -.
DR OMA; KCFSRTA; -.
DR OrthoDB; 5471082at2759; -.
DR Proteomes; UP000233060; Unplaced.
DR Bgee; ENSCATG00000033839; Expressed in lung and 12 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; 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:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0060336; P:negative regulation of type II interferon-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:1902216; P:positive regulation of interleukin-4-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR CDD; cd02907; Macro_Af1521_BAL-like; 1.
DR CDD; cd02903; Macro_BAL-like; 2.
DR CDD; cd12300; RRM1_PAR14; 1.
DR CDD; cd12543; RRM2_PAR14; 1.
DR CDD; cd01439; TCCD_inducible_PARP_like; 1.
DR Gene3D; 3.30.70.330; -; 2.
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; 3.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR034517; PAR14_RRM2.
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:SF89; PROTEIN MONO-ADP-RIBOSYLTRANSFERASE PARP14; 1.
DR Pfam; PF01661; Macro; 3.
DR Pfam; PF00644; PARP; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00506; A1pp; 3.
DR SUPFAM; SSF56399; ADP-ribosylation; 1.
DR SUPFAM; SSF52949; Macro domain-like; 3.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS51154; MACRO; 3.
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:UP000233060};
KW Transferase {ECO:0000256|RuleBase:RU362114}.
FT DOMAIN 791..978
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1002..1189
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1215..1386
FT /note="Macro"
FT /evidence="ECO:0000259|PROSITE:PS51154"
FT DOMAIN 1522..1600
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1604..1800
FT /note="PARP catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51059"
SQ SEQUENCE 1800 AA; 202988 MW; FA290A83E9958A21 CRC64;
MAVPGSFPLL VEGSWGPDPP KNLSTKLQMY FQSRKKSGGG ECEVHQDPRS PSRFLVLFYP
EDVRQKVLER KNHELVLQGK GTFKLTVQLP ETTDEIHHVF EEELLTQESK TKEDVKEPDV
SEELEAKLPL DDGSDNIEDI PEECENISSL VAFENLKANV TDIILTLLVE NISGLSSDDF
QLEVIRDFDV AVVTFQKHVD TVRFVDDCTR HHSIKQLQLS PRLLEVTKTI RVENLPPGVD
DYSLKLFFEN PYSGGGRVAN VEYFPEESSA LIEFFDRKVL DTIMATKLDF NKMPLSVFPY
YASLGTALYG KEKPLIKLPA PFEESLDLPL WKFLQKKNHL IEEINDEMRR CHCELTWSQL
SGKVTIRPAA TLVNEGRPRI KTWQADTSTA LSSIRSKYKV TPIKVDPTMW DTIKNDVKDD
RILIEFDTLK EMIILAGKSE DVQSIEVQVK ELIESTTQKI KREEQSLKEK MVISPGRYFL
LCHSSLLDHL HTECPEIEIC YDGVTQHLCL KGPSVDVYKV KCAIQEKVYT MAQKNIQVSP
EIFQFLQQVN WKEFSKCLFI AQEILALYEL EGTTVLLTSC SSEALLEAEK HMLSALDYKR
IEVENKEVLH GKNWKGLTHN LRKRQNFSPN TVIINELSSE TTAEVIITGC VKKVNETYAL
LFNFIEQNMK IERLVEVKPS LVIDYLKTEK KLFLPKIKRT NVQVSFNPEN KQKGILLTGS
KTEVLKAMDI VKQARDSVCV KSVHIDKPGA KMFFRDKAWF YQREIKRLFG CYIELQENEE
VKEGGSPSGQ KCFSRTALAP GIVLIVQQGD LAQLPVDVVV NASNEDLKHY GGLAAALSKA
AGPELQADCD QIVKREGRLL PGNATISKAG KLPYHHVIHA VGPRWNGCEA PRCVYLLRRT
VQLSLRLAEK YKYRSIAIPA ISSGVFGFPL GRCVETIVSA IKENFQRKKD GHYLKEIYLV
DVSEKTVEAF AEAVKTVFKA TLPDTAAPPS LPAAAGPGKT SWKQGSLVSP GGLQMLLVKE
GVQNAKTDVI VNSVPSDLEL SRGPLSKALL EKAGPALQEE LDTVGQGMTV SVGTVLKTNS
WNLDCRYVLH VVAPEWRNGS TSSLKIMEDI IRECMEITDS LSLKSIAFPA IGTGNLGFPK
TIFAELIISE VFKFSSKNQL KTLQEVHFLL HPSDHENIKA FSDEFARRAN GNLISDKISK
AEDTQGFYGT VSSPDLGVHE MKIGSIIFQV ASGDITKEEA DVIVNSTSKS FNLKAGVSKA
ILECAGQNVE MECSQQAQQH KNDYIITGGG FLKCKNIIHV IGGNDVKSSV SSVLQECEKQ
NYSSICLPAI GTGNAKQDPE KVAEAIIDAI EDFVQKGSAK SVKKVKVVIF LPQVLDVFYA
IMKKREGTQV SSQQSMMSKL ASFLRISKQS PKKENHLVLE KKTESATFRV CGGNVTCVEQ
TISWLQDLIE KEQCPYTSED EYIKYFDEKE YQKLKELQEK LNINIFLDNK RPLIKVLGIS
RDVMQARDEI EAMIKRVRLA KEEESRADCI SEFIEWQYND NNIFYRFDKI TNLKLEDARR
EKKKTIDVKI NHQHYTVNLN TYTATDAKGL SSSVQRLVKS EVDIPAHWSD MKQQNFCVVE
LQPSDPEYNT VASKFNQTCA HFRIEKIERI QNPDLWNSYQ AKKKTMDAKN GQTMNEKQLF
HGTDAGSVPY VNRNGFNRSY AGKNAVAYGK GTYFAVNANY SANDTYSRPD ANGRKHMYYV
RVLTGIYTHG NQSLIVPPSK NPQNPTDLYD TVTDNVQYPN LFVVFYDYQA YPEYLITFRR
//
