ID   HIF1N_MOUSE             Reviewed;         349 AA.
AC   Q8BLR9; Q3U3G4;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   16-JUN-2009, entry version 49.
DE   RecName: Full=Hypoxia-inducible factor 1-alpha inhibitor;
DE            EC=1.14.11.16;
DE   AltName: Full=Hypoxia-inducible factor asparagine hydroxylase;
GN   Name=Hif1an;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Brain cortex;
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).
CC   -!- FUNCTION: Hydroxylates HIF-1 alpha at 'Asp-799' in the C-terminal
CC       transactivation domain (CAD). Functions as an oxygen sensor and,
CC       under normoxic conditions, the hydroxylation prevents interaction
CC       of HIF-1 with transcriptional coactivators including Cbp/p300-
CC       interacting transactivator. Involved in transcriptional repression
CC       through interaction with HIF1A, VHL and histone deacetylases (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Peptide L-aspartate + 2-oxoglutarate + O(2) =
CC       peptide 3-hydroxy-L-aspartate + succinate + CO(2).
CC   -!- COFACTOR: Iron (By similarity).
CC   -!- SUBUNIT: Homodimer. Interacts with VHL and HIF1A (By similarity).
CC   -!- SUBCELLULAR LOCATION: Nucleus (Potential).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8BLR9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BLR9-2; Sequence=VSP_017537, VSP_017538;
CC         Note=No experimental confirmation available;
CC   -!- SIMILARITY: Contains 1 JmjC domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AK043636; BAC31602.1; -; mRNA.
DR   EMBL; AK154774; BAE32822.1; -; mRNA.
DR   IPI; IPI00652254; -.
DR   IPI; IPI00742317; -.
DR   RefSeq; NP_795932.2; -.
DR   UniGene; Mm.145278; -.
DR   HSSP; Q9NWT6; 1MZE.
DR   SMR; Q8BLR9; 15-349.
DR   Ensembl; ENSMUSG00000036450; Mus musculus.
DR   GeneID; 319594; -.
DR   KEGG; mmu:319594; -.
DR   MGI; MGI:2442345; Hif1an.
DR   HOGENOM; Q8BLR9; -.
DR   HOVERGEN; Q8BLR9; -.
DR   OMA; Q8BLR9; FAQIKGH.
DR   BRENDA; 1.14.11.16; 244.
DR   NextBio; 395052; -.
DR   ArrayExpress; Q8BLR9; -.
DR   Bgee; Q8BLR9; -.
DR   GermOnline; ENSMUSG00000036450; Mus musculus.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single d...; IEA:UniProtKB-KW.
DR   GO; GO:0004597; F:peptide-aspartate beta-dioxygenase activity; IEA:EC.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR   GO; GO:0006350; P:transcription; IEA:UniProtKB-KW.
DR   InterPro; IPR003347; TF_JmjC_AAH.
DR   SMART; SM00558; JmjC; 1.
DR   PROSITE; PS51184; JMJC; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Dioxygenase; Iron; Metal-binding; Nucleus;
KW   Oxidoreductase; Transcription; Transcription regulation.
FT   CHAIN         1    349       Hypoxia-inducible factor 1-alpha
FT                                inhibitor.
FT                                /FTId=PRO_0000083975.
FT   DOMAIN      142    307       JmjC.
FT   REGION        1    349       Interaction with VHL (By similarity).
FT   REGION      126    349       Interaction with HIF1A (By similarity).
FT   METAL       199    199       Iron; catalytic (By similarity).
FT   METAL       201    201       Iron; catalytic (By similarity).
FT   METAL       279    279       Iron; catalytic (By similarity).
FT   BINDING     145    145       2-oxoglutarate (By similarity).
FT   BINDING     196    196       2-oxoglutarate (By similarity).
FT   BINDING     214    214       2-oxoglutarate (By similarity).
FT   VAR_SEQ     241    263       QVDFDNPDYERFPNFRNVVGYET -> GVKRRDQAKRETIA
FT                                KEKYTKQNK (in isoform 2).
FT                                /FTId=VSP_017537.
FT   VAR_SEQ     264    349       Missing (in isoform 2).
FT                                /FTId=VSP_017538.
SQ   SEQUENCE   349 AA;  40241 MW;  ED5C2B875EBCE76E CRC64;
     MAATAAEVAA SGSGEAREEA EAPGPAWDES QLRSYSFPTR PIPRLSQSDP RAEELIENEE
     PVVLTDTNLV YPALKWDLEY LQENIGNGDF SVYSASTHKF LYYDEKKMGN FQNFKPRSNR
     EEIKFHEFVE KLQAIQQRGG EERLYLQQTL NDTVGRKIVM DFLGFNWNWI NKQQGKRGWG
     QLTSNLLLIG MEGNVTPAHY DEQQNFFAQI KGHKRCILFP PDQFECLYPY PVHHPCDRQS
     QVDFDNPDYE RFPNFRNVVG YETVVGPGDV LYIPMYWWHH IESLLNGGIT ITVNFWYKGA
     PTPKRIEYPL KAHQKVAIMR NIEKMLGEAL GNPQEVGPLL NTMIKGRYN
//