ASPH2_MOUSE
ID ASPH2_MOUSE Reviewed; 343 AA.
AC Q80VP9; Q9CUZ2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Aspartate beta-hydroxylase domain-containing protein 2;
DE EC=1.14.11.-;
GN Name=Asphd2;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 168-343.
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 -!- FUNCTION: May function as 2-oxoglutarate-dependent dioxygenase.
CC {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC family. {ECO:0000305}.
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DR EMBL; BC046606; AAH46606.1; -; mRNA.
DR EMBL; AK013495; BAB28881.1; -; mRNA.
DR CCDS; CCDS19542.1; -.
DR RefSeq; NP_082662.1; NM_028386.1.
DR RefSeq; XP_011247871.1; XM_011249569.2.
DR RefSeq; XP_011247872.1; XM_011249570.1.
DR RefSeq; XP_011247873.1; XM_011249571.2.
DR RefSeq; XP_011247874.1; XM_011249572.2.
DR RefSeq; XP_011247875.1; XM_011249573.1.
DR RefSeq; XP_011247876.1; XM_011249574.2.
DR RefSeq; XP_011247877.1; XM_011249575.1.
DR RefSeq; XP_011247878.1; XM_011249576.1.
DR RefSeq; XP_017176606.1; XM_017321117.1.
DR RefSeq; XP_017176607.1; XM_017321118.1.
DR AlphaFoldDB; Q80VP9; -.
DR SMR; Q80VP9; -.
DR STRING; 10090.ENSMUSP00000031291; -.
DR GlyGen; Q80VP9; 2 sites.
DR PhosphoSitePlus; Q80VP9; -.
DR SwissPalm; Q80VP9; -.
DR PaxDb; Q80VP9; -.
DR PeptideAtlas; Q80VP9; -.
DR PRIDE; Q80VP9; -.
DR ProteomicsDB; 281851; -.
DR Antibodypedia; 212; 108 antibodies from 18 providers.
DR DNASU; 72898; -.
DR Ensembl; ENSMUST00000031291; ENSMUSP00000031291; ENSMUSG00000029348.
DR GeneID; 72898; -.
DR KEGG; mmu:72898; -.
DR UCSC; uc008yth.2; mouse.
DR CTD; 57168; -.
DR MGI; MGI:1920148; Asphd2.
DR VEuPathDB; HostDB:ENSMUSG00000029348; -.
DR eggNOG; KOG3696; Eukaryota.
DR GeneTree; ENSGT00940000159252; -.
DR HOGENOM; CLU_059279_3_0_1; -.
DR InParanoid; Q80VP9; -.
DR OMA; MSLEWLM; -.
DR OrthoDB; 1324479at2759; -.
DR PhylomeDB; Q80VP9; -.
DR TreeFam; TF312799; -.
DR BioGRID-ORCS; 72898; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Asphd2; mouse.
DR PRO; PR:Q80VP9; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80VP9; protein.
DR Bgee; ENSMUSG00000029348; Expressed in dentate gyrus of hippocampal formation granule cell and 147 other tissues.
DR ExpressionAtlas; Q80VP9; baseline and differential.
DR Genevisible; Q80VP9; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0018193; P:peptidyl-amino acid modification; IEA:InterPro.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR007803; Asp/Arg/Pro-Hydrxlase.
DR InterPro; IPR027443; IPNS-like_sf.
DR Pfam; PF05118; Asp_Arg_Hydrox; 1.
PE 1: Evidence at protein level;
KW Dioxygenase; Glycoprotein; Iron; Membrane; Metal-binding; Oxidoreductase;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..343
FT /note="Aspartate beta-hydroxylase domain-containing protein
FT 2"
FT /id="PRO_0000254163"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..343
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 202
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 266..268
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT BINDING 302
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250"
FT BINDING 315
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250"
FT CARBOHYD 77
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 343 AA; 38731 MW; 34284066FD6E76B2 CRC64;
MWLEWLVAWS WSLDGLRDCI ATGIQSVRDC DGTAVITVAC LLILFVWYCY HVGREQPRPH
VSVNSLLQGV DANGLQNGSM YCQSPECARC THHEGLNQKL YHNLQEYAKR YSWSGMGRIH
KGIREQGRYL SSQPSIQKPE VFFLPDLPTT PYFSRDAQKH DVELLERNFQ AILCEFETLY
KAFSNCSLPQ GWKVNSTPSG EWFTFDFVSQ GVCVPRNCRK CPRTYRLLGS LRTCIGNNVF
GNACISVLSP GTVITEHYGP TNIRIRCHLG LKTPNGCELV VGGEPQCWAE GRCLLFDDSF
LHTAFHEGSA EDGPRVVFMV DLWHPNVAAA ERQALDFIFA PGR
