ID   ASPH2_XENTR             Reviewed;         370 AA.
AC   B5DE73;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Aspartate beta-hydroxylase domain-containing protein 2;
DE            EC=1.14.11.-;
GN   Name=asphd2;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; BC168555; AAI68555.1; -; mRNA.
DR   RefSeq; NP_001135655.1; NM_001142183.1.
DR   AlphaFoldDB; B5DE73; -.
DR   SMR; B5DE73; -.
DR   STRING; 8364.ENSXETP00000063425; -.
DR   PaxDb; B5DE73; -.
DR   GeneID; 100216215; -.
DR   KEGG; xtr:100216215; -.
DR   CTD; 57168; -.
DR   Xenbase; XB-GENE-5998370; asphd2.
DR   eggNOG; KOG3696; Eukaryota.
DR   HOGENOM; CLU_059279_3_0_1; -.
DR   InParanoid; B5DE73; -.
DR   OMA; MSLEWLM; -.
DR   OrthoDB; 1324479at2759; -.
DR   TreeFam; TF312799; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Proteomes; UP000790000; Unplaced.
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..370
FT                   /note="Aspartate beta-hydroxylase domain-containing protein
FT                   2"
FT                   /id="PRO_0000394144"
FT   TOPO_DOM        1..57
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        79..370
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   BINDING         229
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         273
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         293..295
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   BINDING         329
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         342
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        212
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   370 AA;  41798 MW;  C26A27AD23029A62 CRC64;
     MVWALPRTSS PSCIAPSYKP DSGWIKMSAE WLIDWSCLLN GLRDLIAGCI QAVRDCNSFA
     LTTVICLLML FAWYCYRVGK DQPRSPFATV NLLIQSSEAK GLQNGFAYCH SRECVRCTHN
     DGLNQKLYHN LQEYAKRYSW SGMGRIHKGI REQGRYLNNR PSIQKPEVFF LPDLPTMPYF
     PRDAQKHDVE LLEQNFATIL SEFEAIYKAF SNCSLPQGWK VNSTPSGEWF TFYLVNQGVT
     IPSNCKKCPR TYRLLGNLRT FIGNNVFGNA CISVLTPGTV ITEHYGPTNI RIRCHLGLRI
     PGNCELVVGG EPQCWAEGHC LLFDDSFLHT AFHEGSAEEG PRVIFMVDLW HPNVAAAERQ
     ALDSIFAPGR