ARHL1_MOUSE
ID ARHL1_MOUSE Reviewed; 353 AA.
AC Q8BGK2; Q8C4L0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Inactive ADP-ribosyltransferase ARH2 {ECO:0000305};
DE AltName: Full=ADP-ribosylhydrolase-like protein 1 {ECO:0000305};
DE AltName: Full=[Protein ADP-ribosylarginine] hydrolase-like protein 1;
GN Name=Adprhl1; Synonyms=Arh2;
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 [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=12070318; DOI=10.1110/ps.0200602;
RA Glowacki G., Braren R., Firner K., Nissen M., Kuehl M., Reche P.,
RA Bazan J.F., Cetkovic-Cvrlje M., Leiter E., Haag F., Koch-Nolte F.;
RT "The family of toxin-related ecto-ADP-ribosyltransferases in humans and the
RT mouse.";
RL Protein Sci. 11:1657-1670(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head, and Heart;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Jaw, and Limb;
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).
RN [4]
RP FUNCTION.
RX PubMed=17075046; DOI=10.1073/pnas.0607911103;
RA Ono T., Kasamatsu A., Oka S., Moss J.;
RT "The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-
RT ribose, a product of the Sir2 family of acetyl-histone deacetylases.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:16687-16691(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=27217161; DOI=10.1016/j.ydbio.2016.05.006;
RA Smith S.J., Towers N., Saldanha J.W., Shang C.A., Mahmood S.R.,
RA Taylor W.R., Mohun T.J.;
RT "The cardiac-restricted protein ADP-ribosylhydrolase-like 1 is essential
RT for heart chamber outgrowth and acts on muscle actin filament assembly.";
RL Dev. Biol. 416:373-388(2016).
CC -!- FUNCTION: Required for myofibril assembly and outgrowth of the cardiac
CC chambers in the developing heart (By similarity). Appears to be
CC catalytically inactive, showing no activity against O-acetyl-ADP-ribose
CC (PubMed:17075046). {ECO:0000250|UniProtKB:Q6AZR2,
CC ECO:0000269|PubMed:17075046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC {ECO:0000250|UniProtKB:Q6AZR2}.
CC -!- TISSUE SPECIFICITY: Expressed in the embryonic heart at E11.5.
CC {ECO:0000269|PubMed:27217161}.
CC -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family.
CC {ECO:0000305}.
CC -!- CAUTION: Although it belongs to the ADP-ribosylglycohydrolase family,
CC lacks the metal-binding and substrate-binding residues, suggesting that
CC it has no hydrolase activity. {ECO:0000250|UniProtKB:Q6AZR2}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38332.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ427360; CAD20462.1; -; mRNA.
DR EMBL; AK081786; BAC38332.1; ALT_INIT; mRNA.
DR EMBL; AK084501; BAC39199.1; -; mRNA.
DR EMBL; BC063759; AAH63759.1; -; mRNA.
DR CCDS; CCDS22108.1; -.
DR RefSeq; NP_766338.1; NM_172750.3.
DR AlphaFoldDB; Q8BGK2; -.
DR SMR; Q8BGK2; -.
DR BioGRID; 231490; 2.
DR IntAct; Q8BGK2; 1.
DR STRING; 10090.ENSMUSP00000033825; -.
DR iPTMnet; Q8BGK2; -.
DR PhosphoSitePlus; Q8BGK2; -.
DR MaxQB; Q8BGK2; -.
DR PaxDb; Q8BGK2; -.
DR PeptideAtlas; Q8BGK2; -.
DR PRIDE; Q8BGK2; -.
DR ProteomicsDB; 265092; -.
DR Antibodypedia; 25929; 64 antibodies from 18 providers.
DR DNASU; 234072; -.
DR Ensembl; ENSMUST00000033825; ENSMUSP00000033825; ENSMUSG00000031448.
DR GeneID; 234072; -.
DR KEGG; mmu:234072; -.
DR UCSC; uc009kxf.1; mouse.
DR CTD; 113622; -.
DR MGI; MGI:2442168; Adprhl1.
DR VEuPathDB; HostDB:ENSMUSG00000031448; -.
DR eggNOG; ENOG502QPMI; Eukaryota.
DR GeneTree; ENSGT00530000063627; -.
DR HOGENOM; CLU_047061_0_0_1; -.
DR InParanoid; Q8BGK2; -.
DR PhylomeDB; Q8BGK2; -.
DR TreeFam; TF329417; -.
DR BioGRID-ORCS; 234072; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ldlrap1; mouse.
DR PRO; PR:Q8BGK2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8BGK2; protein.
DR Bgee; ENSMUSG00000031448; Expressed in myocardium of ventricle and 50 other tissues.
DR ExpressionAtlas; Q8BGK2; baseline and differential.
DR Genevisible; Q8BGK2; MM.
DR GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR GO; GO:0003875; F:ADP-ribosylarginine hydrolase activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0003242; P:cardiac chamber ballooning; ISS:UniProtKB.
DR GO; GO:0055003; P:cardiac myofibril assembly; ISS:UniProtKB.
DR GO; GO:0051725; P:protein de-ADP-ribosylation; IEA:InterPro.
DR Gene3D; 1.10.4080.10; -; 1.
DR InterPro; IPR012108; ADP-ribosylarg_hydro.
DR InterPro; IPR005502; Ribosyl_crysJ1.
DR InterPro; IPR036705; Ribosyl_crysJ1_sf.
DR Pfam; PF03747; ADP_ribosyl_GH; 1.
DR PIRSF; PIRSF016939; ADP_ribslarg_hdr; 1.
DR SUPFAM; SSF101478; SSF101478; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..353
FT /note="Inactive ADP-ribosyltransferase ARH2"
FT /id="PRO_0000277607"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 353 AA; 39885 MW; 8FDDDECDE80F5D2A CRC64;
MEKFKAAMLL GSVGDALGYG NICRENSVLG SIQEELQKTG GLDSLVLSPG RWPVSDNTIM
HMATAEALTT DYWCLDDLYR EMVKRYVETV ETLSEHRPDP STIEGCSQLK PDNYLLAWHT
PFSEKGSGFG AATKAMCIGM RYWKPERLET LIEVSIECGR MTHNHPTGFL GSLCTALFAS
YALQGKPLVQ WGREMLKVLP LAEEYCRKTI RHMAEYQEHW FYFEAKWQFY LEERKIREDA
EDKVTFPDNY DAEERDKTYK KWSSEGRGGR RGHDAPMIAY DALLASGSNW TELCQRAMFH
GGESGATGTI AGCLFGLLHG LATVPRGLYQ ELEHKGRLED LGAALHRLST EEK
