NAR4_MOUSE
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 03-AUG-2022, entry version 121.
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 GlyGen; Q9CRA0; 4 sites.
DR PhosphoSitePlus; Q9CRA0; -.
DR EPD; Q9CRA0; -.
DR MaxQB; Q9CRA0; -.
DR PaxDb; Q9CRA0; -.
DR PeptideAtlas; Q9CRA0; -.
DR PRIDE; Q9CRA0; -.
DR ProteomicsDB; 252770; -.
DR Antibodypedia; 23686; 157 antibodies from 22 providers.
DR DNASU; 109978; -.
DR Ensembl; ENSMUST00000032341; ENSMUSP00000032341; ENSMUSG00000030217.
DR GeneID; 109978; -.
DR KEGG; mmu:109978; -.
DR UCSC; uc009emk.1; mouse.
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; 963174at2759; -.
DR PhylomeDB; Q9CRA0; -.
DR TreeFam; TF335356; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 109978; 2 hits in 71 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 82 other tissues.
DR Genevisible; Q9CRA0; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0018120; P:peptidyl-arginine ADP-ribosylation; IBA:GO_Central.
DR InterPro; IPR000768; ART.
DR Pfam; PF01129; ART; 1.
DR PRINTS; PR00970; RIBTRNSFRASE.
DR PROSITE; PS01291; ART; 1.
DR PROSITE; PS51996; TR_MART; 1.
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
