ID   NAR4_MOUSE              Reviewed;         300 AA.
AC   Q9CRA0; Q80VB5; Q80W56;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 128.
DE   RecName: Full=Ecto-ADP-ribosyltransferase 4;
DE            EC=2.4.2.31;
DE   AltName: Full=ADP-ribosyltransferase C2 and C3 toxin-like 4;
DE            Short=ARTC4;
DE   AltName: Full=Mono(ADP-ribosyl)transferase 4;
DE   AltName: Full=NAD(P)(+)--arginine ADP-ribosyltransferase 4;
DE   AltName: CD_antigen=CD297;
DE   Flags: Precursor;
GN   Name=Art4;
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 [GENOMIC DNA].
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=Liver, and Lung;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Spleen;
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginyl-[protein] + NAD(+) = H(+) + N(omega)-(ADP-D-
CC         ribosyl)-L-arginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:19149,
CC         Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:15087, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17154, ChEBI:CHEBI:29965, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:142554; EC=2.4.2.31;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Cell membrane {ECO:0000250}; Lipid-
CC       anchor, GPI-anchor {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the Arg-specific ADP-ribosyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ486881; CAD31119.1; -; Genomic_DNA.
DR   EMBL; Y08300; CAA69608.1; -; Genomic_DNA.
DR   EMBL; AK004744; BAB23525.1; -; mRNA.
DR   EMBL; AK019467; BAB31738.1; -; mRNA.
DR   EMBL; AC122804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC046306; AAH46306.1; -; mRNA.
DR   CCDS; CCDS20658.1; -.
DR   RefSeq; NP_080915.1; NM_026639.2.
DR   AlphaFoldDB; Q9CRA0; -.
DR   SMR; Q9CRA0; -.
DR   STRING; 10090.ENSMUSP00000032341; -.
DR   GlyCosmos; Q9CRA0; 4 sites, No reported glycans.
DR   GlyGen; Q9CRA0; 4 sites.
DR   PhosphoSitePlus; Q9CRA0; -.
DR   EPD; Q9CRA0; -.
DR   MaxQB; Q9CRA0; -.
DR   PaxDb; 10090-ENSMUSP00000032341; -.
DR   PeptideAtlas; Q9CRA0; -.
DR   ProteomicsDB; 252770; -.
DR   Antibodypedia; 23686; 173 antibodies from 22 providers.
DR   DNASU; 109978; -.
DR   Ensembl; ENSMUST00000032341.3; ENSMUSP00000032341.3; ENSMUSG00000030217.3.
DR   GeneID; 109978; -.
DR   KEGG; mmu:109978; -.
DR   UCSC; uc009emk.1; mouse.
DR   AGR; MGI:1202710; -.
DR   CTD; 420; -.
DR   MGI; MGI:1202710; Art4.
DR   VEuPathDB; HostDB:ENSMUSG00000030217; -.
DR   eggNOG; ENOG502SKQR; Eukaryota.
DR   GeneTree; ENSGT01030000234601; -.
DR   HOGENOM; CLU_059744_4_0_1; -.
DR   InParanoid; Q9CRA0; -.
DR   OMA; HSFHFKY; -.
DR   OrthoDB; 2897283at2759; -.
DR   PhylomeDB; Q9CRA0; -.
DR   TreeFam; TF335356; -.
DR   Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR   BioGRID-ORCS; 109978; 3 hits in 76 CRISPR screens.
DR   PRO; PR:Q9CRA0; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q9CRA0; Protein.
DR   Bgee; ENSMUSG00000030217; Expressed in fetal liver hematopoietic progenitor cell and 84 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IBA:GO_Central.
DR   GO; GO:0106274; F:NAD+-protein-arginine ADP-ribosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000768; ART.
DR   PANTHER; PTHR10339; ADP-RIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR10339:SF1; ECTO-ADP-RIBOSYLTRANSFERASE 4; 1.
DR   Pfam; PF01129; ART; 1.
DR   PRINTS; PR00970; RIBTRNSFRASE.
DR   SUPFAM; SSF56399; ADP-ribosylation; 1.
DR   PROSITE; PS01291; ART; 1.
DR   PROSITE; PS51996; TR_MART; 1.
DR   Genevisible; Q9CRA0; MM.
PE   1: Evidence at protein level;
KW   Blood group antigen; Cell membrane; Disulfide bond; Glycoprotein;
KW   Glycosyltransferase; GPI-anchor; Lipoprotein; Membrane; NAD; NADP;
KW   Nucleotidyltransferase; Reference proteome; Signal; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..264
FT                   /note="Ecto-ADP-ribosyltransferase 4"
FT                   /id="PRO_0000416110"
FT   PROPEP          265..300
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000416111"
FT   TOPO_DOM        24..269
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        287..300
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          70..255
FT                   /note="TR mART core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01340"
FT   BINDING         185
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   LIPID           264
FT                   /note="GPI-anchor amidated alanine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        110
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        157
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        201
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        48..259
FT                   /evidence="ECO:0000250"
FT   DISULFID        161..210
FT                   /evidence="ECO:0000250"
FT   CONFLICT        26
FT                   /note="T -> A (in Ref. 1; CAD31119)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        39
FT                   /note="D -> N (in Ref. 1; CAD31119)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="L -> R (in Ref. 1; CAD31119)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="G -> E (in Ref. 1; CAD31119)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        195
FT                   /note="E -> G (in Ref. 1; CAA69608)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="G -> V (in Ref. 1; CAD31119)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        292
FT                   /note="A -> E (in Ref. 1; CAD31119)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   300 AA;  33080 MW;  0BB0B42D6AAC3406 CRC64;
     MALWLPGGQL TLLLLLWVQQ TPAGSTEAPL KVDVDLTPDS FDDQYQGCSE QMVEELNQGD
     YFIKEVDTHK YYSRAWQKAH LTWLNQAKAL PESMTPVHAV AIVVFTLNLN VSSDLAKAMA
     RAAGSPGQYS QSFHFKYLHY YLTSAIQLLR KDSSTKNGSL CYKVYHGMKD VSIGANVGST
     IRFGQFLSAS LLKEETRVSG NQTLFTIFTC LGASVQDFSL RKEVLIPPYE LFEVVSKSGS
     PKGDLINLRS AGNMSTYNCQ LLKACSKKCA PAPVVIGCLF LVTVVISSKS RAQRNLLAPF
//