ID   ARHL1_HUMAN             Reviewed;         354 AA.
AC   Q8NDY3; Q5JUG2; Q96GD1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 131.
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   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Ovary;
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).
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       (By similarity). {ECO:0000250|UniProtKB:Q6AZR2,
CC       ECO:0000250|UniProtKB:Q8BGK2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere
CC       {ECO:0000250|UniProtKB:Q6AZR2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8NDY3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NDY3-2; Sequence=VSP_023036;
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}.
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DR   EMBL; AJ313429; CAC86114.1; -; mRNA.
DR   EMBL; AL160251; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC009755; AAH09755.1; -; mRNA.
DR   CCDS; CCDS9535.1; -. [Q8NDY3-1]
DR   CCDS; CCDS9536.1; -. [Q8NDY3-2]
DR   RefSeq; NP_612439.2; NM_138430.4. [Q8NDY3-1]
DR   RefSeq; NP_954631.1; NM_199162.2. [Q8NDY3-2]
DR   AlphaFoldDB; Q8NDY3; -.
DR   SMR; Q8NDY3; -.
DR   STRING; 9606.ENSP00000364567; -.
DR   iPTMnet; Q8NDY3; -.
DR   PhosphoSitePlus; Q8NDY3; -.
DR   BioMuta; ADPRHL1; -.
DR   EPD; Q8NDY3; -.
DR   MassIVE; Q8NDY3; -.
DR   MaxQB; Q8NDY3; -.
DR   PaxDb; Q8NDY3; -.
DR   PeptideAtlas; Q8NDY3; -.
DR   PRIDE; Q8NDY3; -.
DR   ProteomicsDB; 73089; -. [Q8NDY3-1]
DR   ProteomicsDB; 73090; -. [Q8NDY3-2]
DR   Antibodypedia; 25929; 64 antibodies from 18 providers.
DR   DNASU; 113622; -.
DR   Ensembl; ENST00000356501.8; ENSP00000348894.4; ENSG00000153531.15. [Q8NDY3-2]
DR   Ensembl; ENST00000375418.8; ENSP00000364567.3; ENSG00000153531.15. [Q8NDY3-1]
DR   GeneID; 113622; -.
DR   KEGG; hsa:113622; -.
DR   UCSC; uc001vtp.2; human. [Q8NDY3-1]
DR   CTD; 113622; -.
DR   DisGeNET; 113622; -.
DR   GeneCards; ADPRHL1; -.
DR   HGNC; HGNC:21303; ADPRHL1.
DR   HPA; ENSG00000153531; Group enriched (heart muscle, skeletal muscle, tongue).
DR   MIM; 610620; gene.
DR   neXtProt; NX_Q8NDY3; -.
DR   OpenTargets; ENSG00000153531; -.
DR   PharmGKB; PA134870688; -.
DR   VEuPathDB; HostDB:ENSG00000153531; -.
DR   eggNOG; ENOG502QPMI; Eukaryota.
DR   GeneTree; ENSGT00530000063627; -.
DR   HOGENOM; CLU_047061_1_0_1; -.
DR   InParanoid; Q8NDY3; -.
DR   OrthoDB; 1112828at2759; -.
DR   PhylomeDB; Q8NDY3; -.
DR   TreeFam; TF329417; -.
DR   PathwayCommons; Q8NDY3; -.
DR   SignaLink; Q8NDY3; -.
DR   BioGRID-ORCS; 113622; 11 hits in 1068 CRISPR screens.
DR   ChiTaRS; ADPRHL1; human.
DR   GenomeRNAi; 113622; -.
DR   Pharos; Q8NDY3; Tdark.
DR   PRO; PR:Q8NDY3; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q8NDY3; protein.
DR   Bgee; ENSG00000153531; Expressed in left ventricle myocardium and 162 other tissues.
DR   ExpressionAtlas; Q8NDY3; baseline and differential.
DR   Genevisible; Q8NDY3; HS.
DR   GO; GO:0030017; C:sarcomere; ISS:UniProtKB.
DR   GO; GO:0003875; F:ADP-ribosylarginine hydrolase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..354
FT                   /note="Inactive ADP-ribosyltransferase ARH2"
FT                   /id="PRO_0000277606"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BGK2"
FT   VAR_SEQ         1..82
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023036"
FT   VARIANT         7
FT                   /note="A -> V (in dbSNP:rs9577273)"
FT                   /id="VAR_048890"
SQ   SEQUENCE   354 AA;  40105 MW;  B880003EB955EB78 CRC64;
     MEKFKAAMLL GSVGDALGYR NVCKENSTVG MKIQEELQRS GGLDHLVLSP GEWPVSDNTI
     MHIATAEALT TDYWCLDDLY REMVRCYVEI VEKLPERRPD PATIEGCAQL KPNNYLLAWH
     TPFNEKGSGF GAATKAMCIG LRYWKPERLE TLIEVSVECG RMTHNHPTGF LGSLCTALFV
     SFAAQGKPLV QWGRDMLRAV PLAEEYCRKT IRHTAEYQEH WFYFEAKWQF YLEERKISKD
     SENKAIFPDN YDAEEREKTY RKWSSEGRGG RRGHDAPMIA YDALLAAGNS WTELCHRAMF
     HGGESAATGT IAGCLFGLLY GLDLVPKGLY QDLEDKEKLE DLGAALYRLS TEEK