ID   ARAID_DANRE             Reviewed;         230 AA.
AC   A3KNS9; Q502E7; Q5RID6;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 2.
DT   03-AUG-2022, entry version 72.
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; ORFNames=si:ch211-101l18.3;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo, and Liver;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in osteoblast cell differentiation. May play a role
CC       in inducing the cell cycle arrest (By similarity). {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH95730.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BX276101; CAI11536.1; -; Genomic_DNA.
DR   EMBL; BC095730; AAH95730.1; ALT_INIT; mRNA.
DR   EMBL; BC133993; AAI33994.1; -; mRNA.
DR   RefSeq; NP_001038238.1; NM_001044773.1.
DR   AlphaFoldDB; A3KNS9; -.
DR   STRING; 7955.ENSDARP00000063695; -.
DR   PaxDb; A3KNS9; -.
DR   Ensembl; ENSDART00000063696; ENSDARP00000063695; ENSDARG00000043388.
DR   GeneID; 553468; -.
DR   KEGG; dre:553468; -.
DR   CTD; 51374; -.
DR   ZFIN; ZDB-GENE-040724-177; atraid.
DR   eggNOG; ENOG502S1YR; Eukaryota.
DR   GeneTree; ENSGT00390000017252; -.
DR   HOGENOM; CLU_086391_0_0_1; -.
DR   InParanoid; A3KNS9; -.
DR   OMA; RCCLNQE; -.
DR   OrthoDB; 1027431at2759; -.
DR   PhylomeDB; A3KNS9; -.
DR   TreeFam; TF335766; -.
DR   PRO; PR:A3KNS9; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 20.
DR   Bgee; ENSDARG00000043388; Expressed in brain and 22 other tissues.
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: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:0048856; P:anatomical structure development; IEA:UniProt.
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   Gene3D; 3.80.10.10; -; 1.
DR   InterPro; IPR042350; ATRAID.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   PANTHER; PTHR15926; PTHR15926; 1.
DR   PROSITE; PS00022; EGF_1; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Differentiation; Disulfide bond; EGF-like domain; Membrane;
KW   Nucleus; Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..230
FT                   /note="All-trans retinoic acid-induced differentiation
FT                   factor"
FT                   /id="PRO_0000360984"
FT   TOPO_DOM        27..200
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        201..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        222..230
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          152..194
FT                   /note="EGF-like"
FT   DISULFID        156..172
FT                   /evidence="ECO:0000250"
FT   DISULFID        166..182
FT                   /evidence="ECO:0000250"
FT   DISULFID        184..193
FT                   /evidence="ECO:0000250"
FT   CONFLICT        187
FT                   /note="N -> H (in Ref. 2; AAI33994)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   230 AA;  25580 MW;  7E7774219D87B73E CRC64;
     MTANVTVSSM YLFTVLLLLF NVYVNSQDTD AQLCQMCEGT IRHDSPVWSF CITKGYVKGH
     CCFKNNTSDV DTIIGLDLSN CSISHVEHLY NSSTALIIDL SNNPISNLSD YVFQGFSQLT
     QLLLPSKLEC PGGRASWEKV EVKSITRICE GQKNACNQTV QMPLVCPENS LCSPYGPGFF
     ECSCLNNFHG YKCMRQGEFP LVKVLGILTA STVVVSSVLW FTQRRKVKNT