ID   H7C2G2_HUMAN            Unreviewed;       273 AA.
AC   H7C2G2;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   16-JAN-2019, entry version 35.
DE   RecName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase {ECO:0000256|RuleBase:RU361228};
DE            EC=2.4.2.31 {ECO:0000256|RuleBase:RU361228};
DE   AltName: Full=Mono(ADP-ribosyl)transferase {ECO:0000256|RuleBase:RU361228};
DE   Flags: Fragment;
GN   Name=ART4 {ECO:0000313|Ensembl:ENSP00000405689};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000405689, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000405689, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RG   Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A., null.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [2] {ECO:0000313|Ensembl:ENSP00000405689}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC         ribosyl)-L-arginyl-[protein] + nicotinamide;
CC         Xref=Rhea:RHEA:19149, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC         COMP:15087, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154,
CC         ChEBI:CHEBI:29965, ChEBI:CHEBI:57540, ChEBI:CHEBI:142554;
CC         EC=2.4.2.31; Evidence={ECO:0000256|RuleBase:RU361228};
CC   -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase
CC       family. {ECO:0000256|RuleBase:RU361228}.
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DR   EMBL; AC007655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; H7C2G2; -.
DR   jPOST; H7C2G2; -.
DR   PeptideAtlas; H7C2G2; -.
DR   PRIDE; H7C2G2; -.
DR   Ensembl; ENST00000420600; ENSP00000405689; ENSG00000111339.
DR   UCSC; uc058lnd.1; human.
DR   EuPathDB; HostDB:ENSG00000111339.10; -.
DR   HGNC; HGNC:726; ART4.
DR   OpenTargets; ENSG00000111339; -.
DR   eggNOG; ENOG410IFER; Eukaryota.
DR   eggNOG; ENOG4111WZG; LUCA.
DR   GeneTree; ENSGT00940000153943; -.
DR   ChiTaRS; ART4; human.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000111339; Expressed in 92 organ(s), highest expression level in amniotic fluid.
DR   ExpressionAtlas; H7C2G2; baseline and differential.
DR   GO; GO:0003956; F:NAD(P)+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006471; P:protein ADP-ribosylation; IEA:InterPro.
DR   InterPro; IPR000768; ART.
DR   Pfam; PF01129; ART; 1.
DR   PRINTS; PR00970; RIBTRNSFRASE.
DR   PROSITE; PS01291; ART; 1.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361228};
KW   NAD {ECO:0000256|RuleBase:RU361228};
KW   NADP {ECO:0000256|RuleBase:RU361228};
KW   Proteomics identification {ECO:0000213|MaxQB:H7C2G2,
KW   ECO:0000213|PeptideAtlas:H7C2G2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   Signal {ECO:0000256|RuleBase:RU361228};
KW   Transferase {ECO:0000256|RuleBase:RU361228}.
FT   SIGNAL        1     29       {ECO:0000256|RuleBase:RU361228}.
FT   CHAIN        30    273       NAD(P)(+)--arginine ADP-
FT                                ribosyltransferase.
FT                                {ECO:0000256|RuleBase:RU361228}.
FT                                /FTId=PRO_5005134628.
FT   NON_TER       1      1       {ECO:0000313|Ensembl:ENSP00000405689}.
SQ   SEQUENCE   273 AA;  31511 MW;  EEE91E549DE0B927 CRC64;
     PPATMRIWLL GGLLPFLLLL SGLQRPTEGS EVAIKIDFDF APGSFDDQYQ GCSKQVMEKL
     TQGDYFTKDI EAQKNYFRMW QKAHLAWLNQ GKVLPQNMTT THAVAILFYT LNSNVHSDFT
     RAMASVARTP QQYERSFHFK YLHYYLTSAI QLLRKDSIME NGTLCYEVHY RTKDVHFNAY
     TGATIRFGQF LSTSLLKEEA QEFGNQTLFT IFTCLGAPVQ YFSLKKEVLI PPYELFKVIN
     MSYHPRGDWL QLRSTGNLST YNCQLLKGIL YLN
//