ASPH1_BOVIN
ID ASPH1_BOVIN Reviewed; 367 AA.
AC A1L515;
DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Aspartate beta-hydroxylase domain-containing protein 1;
DE EC=1.14.11.-;
GN Name=ASPHD1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; BT029802; ABM21541.1; -; mRNA.
DR EMBL; BC149115; AAI49116.1; -; mRNA.
DR RefSeq; NP_001075210.1; NM_001081741.1.
DR AlphaFoldDB; A1L515; -.
DR SMR; A1L515; -.
DR STRING; 9913.ENSBTAP00000037186; -.
DR PaxDb; A1L515; -.
DR Ensembl; ENSBTAT00000037353; ENSBTAP00000037186; ENSBTAG00000026319.
DR GeneID; 614735; -.
DR KEGG; bta:614735; -.
DR CTD; 253982; -.
DR VEuPathDB; HostDB:ENSBTAG00000026319; -.
DR VGNC; VGNC:26220; ASPHD1.
DR eggNOG; KOG3696; Eukaryota.
DR GeneTree; ENSGT00940000161676; -.
DR HOGENOM; CLU_059279_3_1_1; -.
DR InParanoid; A1L515; -.
DR OMA; GQGNWGL; -.
DR OrthoDB; 1324479at2759; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000026319; Expressed in temporal cortex and 25 other tissues.
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: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; Membrane; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..367
FT /note="Aspartate beta-hydroxylase domain-containing protein
FT 1"
FT /id="PRO_0000394141"
FT TOPO_DOM 1..49
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..367
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4P2"
SQ SEQUENCE 367 AA; 38661 MW; FA0FFFEDAD92C9CA CRC64;
MWRGSSAGGS QGAAMEGTGG ELGGQGNWGL EDAPGLLARA SLPIMPAWPL PLASSALTLL
LGALTSLFLW YCYRLGSQDM QALGTGSRAG AVGGRPGGCS EAGRPSPGRS GESGEGPRTE
GLMSRRLRAY ARRYSWAGMG RVRRAAQGGP SPGGGPGVLG IQRPGLLFLP DLPSAPFVPR
EAQRHDVELL ESSFPAILRD FGAVSWDFSG TTPPPRGWSP PLAPGCYQLL LYQAGRCQPS
NCRRCPGAYR ALRGLRSFMS ANTFGNAGFS VLLPGARLEG RCGPTNARVR CHLGLKIPPG
CELVVGGEPQ CWAEGHCLLV DDSFLYTVAH NGSPEDGPRV VFIVDLWHPN VAGAERQALD
FVFAPDP