GenomeNet

Database: UniProt
Entry: Q6PGD0
LinkDB: Q6PGD0
Original site: Q6PGD0 
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   13-FEB-2019, entry version 115.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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
RT   project: 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)
CC       signal pathway (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NELL1; the interaction promotes
CC       osteoblastic differentiation and mineralization. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus envelope
CC       {ECO:0000250|UniProtKB:Q6UW56}. Cell membrane {ECO:0000250};
CC       Single-pass membrane protein {ECO:0000250|UniProtKB:Q6UW56}.
CC       Note=Colocalizes with NELL1 on the nuclear envelope and the
CC       perinuclear region. {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         Note=No experimental confirmation available. May be produced at
CC         very low levels due to a premature stop codon in the mRNA,
CC         leading to nonsense-mediated mRNA decay.;
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH49637.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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   UniGene; Mm.28144; -.
DR   ProteinModelPortal; Q6PGD0; -.
DR   STRING; 10090.ENSMUSP00000013766; -.
DR   iPTMnet; Q6PGD0; -.
DR   PhosphoSitePlus; Q6PGD0; -.
DR   PaxDb; Q6PGD0; -.
DR   PRIDE; Q6PGD0; -.
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   eggNOG; ENOG410IYNU; Eukaryota.
DR   eggNOG; ENOG4111PJW; LUCA.
DR   GeneTree; ENSGT00390000017252; -.
DR   HOGENOM; HOG000010110; -.
DR   HOVERGEN; HBG054041; -.
DR   InParanoid; Q6PGD0; -.
DR   OMA; PGGINAW; -.
DR   OrthoDB; 1027431at2759; -.
DR   PhylomeDB; Q6PGD0; -.
DR   TreeFam; TF335766; -.
DR   PRO; PR:Q6PGD0; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000013622; Expressed in 286 organ(s), highest expression level in pituitary gland.
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: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:1903363; P:negative regulation of cellular protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0033689; P:negative regulation of osteoblast proliferation; 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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
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; Complete proteome;
KW   Differentiation; Disulfide bond; EGF-like domain; Membrane; Nucleus;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL        1     25       {ECO:0000250}.
FT   CHAIN        26    223       All-trans retinoic acid-induced
FT                                differentiation factor.
FT                                /FTId=PRO_0000020753.
FT   TOPO_DOM     26    193       Extracellular. {ECO:0000255}.
FT   TRANSMEM    194    214       Helical. {ECO:0000255}.
FT   TOPO_DOM    215    223       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      146    187       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DISULFID    150    165       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    159    175       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    177    186       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ      37    223       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_039970.
FT   CONFLICT     23     23       A -> S (in Ref. 1; BAB21981).
FT                                {ECO:0000305}.
FT   CONFLICT     28     28       E -> K (in Ref. 1; BAB21981).
FT                                {ECO:0000305}.
FT   CONFLICT     65     65       T -> P (in Ref. 1; BAB21981).
FT                                {ECO:0000305}.
FT   CONFLICT     70     70       D -> N (in Ref. 1; BAB21981).
FT                                {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
//
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