ID   ASPH2_RAT               Reviewed;         343 AA.
AC   Q5HZW3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Aspartate beta-hydroxylase domain-containing protein 2;
DE            EC=1.14.11.-;
GN   Name=Asphd2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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: 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; BC088863; AAH88863.1; -; mRNA.
DR   RefSeq; NP_001009716.1; NM_001009716.1.
DR   RefSeq; XP_008767573.1; XM_008769351.2.
DR   RefSeq; XP_017453903.1; XM_017598414.1.
DR   RefSeq; XP_017453904.1; XM_017598415.1.
DR   RefSeq; XP_017453905.1; XM_017598416.1.
DR   RefSeq; XP_017453906.1; XM_017598417.1.
DR   AlphaFoldDB; Q5HZW3; -.
DR   SMR; Q5HZW3; -.
DR   STRING; 10116.ENSRNOP00000000823; -.
DR   GlyGen; Q5HZW3; 2 sites.
DR   PhosphoSitePlus; Q5HZW3; -.
DR   PaxDb; Q5HZW3; -.
DR   PRIDE; Q5HZW3; -.
DR   Ensembl; ENSRNOT00000079190; ENSRNOP00000068694; ENSRNOG00000061004.
DR   GeneID; 364948; -.
DR   KEGG; rno:364948; -.
DR   CTD; 57168; -.
DR   RGD; 1306020; Asphd2.
DR   eggNOG; KOG3696; Eukaryota.
DR   GeneTree; ENSGT00940000159252; -.
DR   HOGENOM; CLU_059279_3_0_1; -.
DR   InParanoid; Q5HZW3; -.
DR   OMA; MSLEWLM; -.
DR   OrthoDB; 1324479at2759; -.
DR   PhylomeDB; Q5HZW3; -.
DR   TreeFam; TF312799; -.
DR   PRO; PR:Q5HZW3; -.
DR   Proteomes; UP000002494; Chromosome 12.
DR   Bgee; ENSRNOG00000061004; Expressed in frontal cortex and 2 other tissues.
DR   Genevisible; Q5HZW3; RN.
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   2: Evidence at transcript 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_0000254164"
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;  38727 MW;  78591E14AD8410E5 CRC64;
     MWLEWLVAWS WSLDGLRDCI ATGIQSVRDC DGTAVITVAC LLVLFVWYCY HVGREQPRPH
     VSVNSLLQGV DANGLQNGSM YCQSPECVRC THHDGLNQKL YHNLQEYAKR YSWSGMGRIH
     KGIREQGRYL SSQPSIQKPE VFFLPDLPTT PYFPRDAQKH DVELLERNFQ AILCEFEALY
     KAFSNCSLPQ GWKVNSTPSG EWFTFDFVSQ GVCVPRNCRK CPRTYRLLGS LRTCIGNNVF
     GNACISVLSP GTVITEHYGP TNIRIRCHLG LKTPNGCELV VGGEPQCWAE GRCLLFDDSF
     LHTSFHEGSA EDGPRVVFMV DLWHPNVAAA ERQALDFIFA PGR