ARAID_MOUSE
ID ARAID_MOUSE Reviewed; 223 AA.
AC Q6PGD0; Q3UAH4; Q810Q3; Q9DD14;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=All-trans retinoic acid-induced differentiation factor;
DE AltName: Full=Apoptosis-related protein 3;
DE Short=APR-3;
DE Flags: Precursor;
GN Name=Atraid; Synonyms=Apr3;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Heart, and Kidney;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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: Promotes osteoblast cell differentiation and terminal
CC mineralization. Plays a role in inducing the cell cycle arrest via
CC inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal
CC pathway (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with NELL1; the interaction promotes osteoblastic
CC differentiation and mineralization. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000250|UniProtKB:Q6UW56}.
CC Cell membrane {ECO:0000250}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q6UW56}. Note=Colocalizes with NELL1 on the
CC nuclear envelope and the perinuclear region.
CC {ECO:0000250|UniProtKB:Q6UW56}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6PGD0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PGD0-2; Sequence=VSP_039970;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49637.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AK002276; BAB21981.1; -; mRNA.
DR EMBL; AK151307; BAE30289.1; -; mRNA.
DR EMBL; AK151366; BAE30340.1; -; mRNA.
DR EMBL; AK169267; BAE41028.1; -; mRNA.
DR EMBL; BC049637; AAH49637.1; ALT_SEQ; mRNA.
DR EMBL; BC057097; AAH57097.2; -; mRNA.
DR CCDS; CCDS19170.1; -. [Q6PGD0-1]
DR RefSeq; NP_082131.2; NM_027855.4. [Q6PGD0-1]
DR RefSeq; NP_997635.1; NM_212470.3.
DR AlphaFoldDB; Q6PGD0; -.
DR BioGRID; 238018; 1.
DR STRING; 10090.ENSMUSP00000013766; -.
DR iPTMnet; Q6PGD0; -.
DR PhosphoSitePlus; Q6PGD0; -.
DR MaxQB; Q6PGD0; -.
DR PaxDb; Q6PGD0; -.
DR PRIDE; Q6PGD0; -.
DR ProteomicsDB; 282009; -. [Q6PGD0-1]
DR Antibodypedia; 28263; 106 antibodies from 24 providers.
DR DNASU; 381629; -.
DR Ensembl; ENSMUST00000013766; ENSMUSP00000013766; ENSMUSG00000013622. [Q6PGD0-1]
DR Ensembl; ENSMUST00000200942; ENSMUSP00000144431; ENSMUSG00000013622. [Q6PGD0-2]
DR GeneID; 381629; -.
DR KEGG; mmu:381629; -.
DR UCSC; uc008www.3; mouse. [Q6PGD0-1]
DR CTD; 51374; -.
DR MGI; MGI:1918918; Atraid.
DR VEuPathDB; HostDB:ENSMUSG00000013622; -.
DR eggNOG; ENOG502S1YR; Eukaryota.
DR GeneTree; ENSGT00390000017252; -.
DR InParanoid; Q6PGD0; -.
DR OMA; RCCLNQE; -.
DR PhylomeDB; Q6PGD0; -.
DR TreeFam; TF335766; -.
DR BioGRID-ORCS; 381629; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Atraid; mouse.
DR PRO; PR:Q6PGD0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6PGD0; protein.
DR Bgee; ENSMUSG00000013622; Expressed in placenta labyrinth and 256 other tissues.
DR ExpressionAtlas; Q6PGD0; baseline and differential.
DR Genevisible; Q6PGD0; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IDA:CACAO.
DR GO; GO:0005635; C:nuclear envelope; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; ISS:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; ISS:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR InterPro; IPR042350; ATRAID.
DR InterPro; IPR000742; EGF-like_dom.
DR PANTHER; PTHR15926; PTHR15926; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Differentiation; Disulfide bond;
KW EGF-like domain; Membrane; Nucleus; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..223
FT /note="All-trans retinoic acid-induced differentiation
FT factor"
FT /id="PRO_0000020753"
FT TOPO_DOM 26..193
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 215..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 146..187
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 150..165
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 159..175
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 177..186
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 37..223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039970"
FT CONFLICT 23
FT /note="A -> S (in Ref. 1; BAB21981)"
FT /evidence="ECO:0000305"
FT CONFLICT 28
FT /note="E -> K (in Ref. 1; BAB21981)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="T -> P (in Ref. 1; BAB21981)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="D -> N (in Ref. 1; BAB21981)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 23858 MW; 1CB921F5F6D3E595 CRC64;
MASRESGGSR AAALLLVLGV ERALALPEIC TLCPGGMHNL SRVAAYCEDT SKLMQARCCL
NQKGTILGLD LQNCSLKDPG PNFLQAYTAI IIDLQANPLK DDLANTFRGF TQLQTLILPQ
DVPCPGGSNA WDNVTSFKDK QICQGQRDLC NSTGSPEMCP ENGSCASDGP GLLQCVCADG
FHGYKCMRQG SFSLLMFFGI LGSTTLAISI LLWGTQRRKA KAS
