ID   ARHL1_BOVIN             Reviewed;         354 AA.
AC   Q3ZBM1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Heart ventricle;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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   -!- 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; BC103222; AAI03223.1; -; mRNA.
DR   RefSeq; NP_001029706.1; NM_001034534.1.
DR   AlphaFoldDB; Q3ZBM1; -.
DR   SMR; Q3ZBM1; -.
DR   STRING; 9913.ENSBTAP00000035177; -.
DR   PaxDb; Q3ZBM1; -.
DR   Ensembl; ENSBTAT00000035299; ENSBTAP00000035177; ENSBTAG00000020928.
DR   GeneID; 519627; -.
DR   KEGG; bta:519627; -.
DR   CTD; 113622; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020928; -.
DR   eggNOG; ENOG502QPMI; Eukaryota.
DR   GeneTree; ENSGT00530000063627; -.
DR   HOGENOM; CLU_047061_0_0_1; -.
DR   InParanoid; Q3ZBM1; -.
DR   OMA; DATLMHM; -.
DR   OrthoDB; 1112828at2759; -.
DR   TreeFam; TF329417; -.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000020928; Expressed in tongue muscle and 59 other tissues.
DR   GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR   GO; GO:0055037; C:recycling endosome; IBA:GO_Central.
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   GO; GO:2000785; P:regulation of autophagosome assembly; IBA:GO_Central.
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   Cytoplasm; Phosphoprotein; Reference proteome.
FT   CHAIN           1..354
FT                   /note="Inactive ADP-ribosyltransferase ARH2"
FT                   /id="PRO_0000277605"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8BGK2"
SQ   SEQUENCE   354 AA;  39937 MW;  E7E2DBA6BEE4F7CF CRC64;
     MEKFQAAMLL GAVGDALGFG HAARESSSLG ARVQEEMGKG GGLDHLVLSP ETWPVSDNTI
     MHMSTAGALI TDFWCLDDLY REMVRRYVDV LEKLPEQRAD PATLEGCSQL KPDNYLLAWH
     TPFNEKGSGF GAATKAMCVG MRYWQPERLE TLVEVSVECG RMTHNHPTGF LGSLCTALFA
     SYAVQGKRLE QWGRDMLRTV PLAEEYCKKT IRHLAEYQEH WFYFEAKWQF YLEERKIIED
     TENEASFPDR YDAEEREKTY RKWSSEGRGG RRGHDAPMIA YDALLGAKGS WTELCRRAMF
     HGGESGATGA IAGCLFGLLH GLDAVPAGLY RELEHQDELR RLGEALHRLS SQEK