ASPH_BOVIN
ID ASPH_BOVIN Reviewed; 754 AA.
AC Q28056;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Aspartyl/asparaginyl beta-hydroxylase;
DE EC=1.14.11.16 {ECO:0000269|PubMed:1856229};
DE AltName: Full=Aspartate beta-hydroxylase;
DE Short=ASP beta-hydroxylase;
DE AltName: Full=Peptide-aspartate beta-dioxygenase;
GN Name=ASPH;
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 [MRNA], CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC TISSUE=Brain, and Liver;
RX PubMed=1378441; DOI=10.1016/s0021-9258(19)49715-9;
RA Jia S., Vandusen W.J., Diehl R.E., Kohl N.E., Dixon R.A.F., Elliston K.O.,
RA Stern A.M., Friedman P.A.;
RT "cDNA cloning and expression of bovine aspartyl (asparaginyl) beta-
RT hydroxylase.";
RL J. Biol. Chem. 267:14322-14327(1992).
RN [2]
RP PROTEIN SEQUENCE OF 289-385 AND 615-641, CATALYTIC ACTIVITY, FUNCTION,
RP COFACTOR, AND SUBUNIT.
RC TISSUE=Liver;
RX PubMed=1856229; DOI=10.1016/s0021-9258(18)92802-4;
RA Wang Q., Vandusen W.J., Petroski C.J., Garsky V.M., Stern A.M.,
RA Friedman P.A.;
RT "Bovine liver aspartyl beta-hydroxylase. Purification and
RT characterization.";
RL J. Biol. Chem. 266:14004-14010(1991).
CC -!- FUNCTION: Specifically hydroxylates an Asp or Asn residue in certain
CC epidermal growth factor-like (EGF) domains of a number of proteins.
CC {ECO:0000269|PubMed:1856229}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-aspartyl-[protein] + O2 = 3-hydroxy-L-
CC aspartyl-[protein] + CO2 + succinate; Xref=Rhea:RHEA:11508,
CC Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:14951, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17427,
CC ChEBI:CHEBI:29961, ChEBI:CHEBI:30031; EC=1.14.11.16;
CC Evidence={ECO:0000269|PubMed:1378441, ECO:0000269|PubMed:1856229};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:1856229};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1856229}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein {ECO:0000303|PubMed:1378441}.
CC -!- PTM: Might be processed to the 56 kDa (AA 289-754) or 52 kDa (AA 311-
CC 754) forms in the lumen of the endoplasmic reticulum.
CC {ECO:0000303|PubMed:1856229}.
CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC family. {ECO:0000305}.
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DR EMBL; M91213; AAA03563.1; -; mRNA.
DR PIR; A42969; BABOH.
DR RefSeq; NP_777182.1; NM_174757.2.
DR AlphaFoldDB; Q28056; -.
DR SMR; Q28056; -.
DR STRING; 9913.ENSBTAP00000021267; -.
DR PaxDb; Q28056; -.
DR PeptideAtlas; Q28056; -.
DR PRIDE; Q28056; -.
DR Ensembl; ENSBTAT00000021267; ENSBTAP00000021267; ENSBTAG00000026283.
DR GeneID; 286771; -.
DR KEGG; bta:286771; -.
DR CTD; 444; -.
DR VEuPathDB; HostDB:ENSBTAG00000026283; -.
DR VGNC; VGNC:26219; ASPH.
DR eggNOG; KOG3696; Eukaryota.
DR GeneTree; ENSGT00940000156304; -.
DR HOGENOM; CLU_023717_0_0_1; -.
DR InParanoid; Q28056; -.
DR OMA; YTELVKX; -.
DR OrthoDB; 1324479at2759; -.
DR TreeFam; TF312799; -.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000026283; Expressed in omental fat pad and 108 other tissues.
DR ExpressionAtlas; Q28056; baseline and differential.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0062101; F:peptidyl-aspartic acid 3-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0042264; P:peptidyl-aspartic acid hydroxylation; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 2.60.120.330; -; 1.
DR InterPro; IPR007943; Asp-B-hydro/Triadin_dom.
DR InterPro; IPR007803; Asp/Arg/Pro-Hydrxlase.
DR InterPro; IPR039038; ASPH.
DR InterPro; IPR027443; IPNS-like_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR12366; PTHR12366; 1.
DR Pfam; PF05279; Asp-B-Hydro_N; 1.
DR Pfam; PF05118; Asp_Arg_Hydrox; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Calcium; Dioxygenase; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Signal-anchor;
KW TPR repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..754
FT /note="Aspartyl/asparaginyl beta-hydroxylase"
FT /id="PRO_0000064705"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..754
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REPEAT 337..370
FT /note="TPR 1"
FT REPEAT 378..411
FT /note="TPR 2"
FT REPEAT 450..483
FT /note="TPR 3"
FT REPEAT 485..517
FT /note="TPR 4"
FT REPEAT 521..553
FT /note="TPR 5"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 111
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 113
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 115
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 120
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 621
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 664
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 675
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 684..686
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 721
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT BINDING 731
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12797"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 637..644
FT /evidence="ECO:0000250|UniProtKB:Q12797"
SQ SEQUENCE 754 AA; 84999 MW; 369593A1F0B558C8 CRC64;
MAPRKNAKGG GGNSSSSSSG SPTGCTSGGS SSPGARRETK QGGLKNGRKG GLSGSSFFTW
FMVIALLGVW TSVAVVWFDL VDYEEVLAKA KDFRYNLSEV LQGKLGIYDA DGDGDFDVDD
AKVLLGLKEK PAPKPTVPPE EADMYPWLED QVLESPGRQN IEDEVYEQVQ SLDETVYSEP
GENLPQEPEG PAEELQPDDH VFVGSDADDR YEPMGTGAVH EETEDSYHIE ETASPAYSQD
MEDMMYEQEN PDSSEPVVVD DAERTYQETD DVTYRDYDEQ DHAVDNSNTI LEEPHMPPAE
EQQEVPPETN KKADEPGKKG KVKKKKPKLL NKFDKTIKAE LDAAEKLRKR GKIEEAVNAF
EELVRKYPQS PGARYGKAQC EDDLAEKRRS NEILRRAIET YQEAASLPDA PTDLVKLSLK
RRSDRQQFLG HMRGSLLTLQ KLVQLFPDDT ALKNDLGVGY LLIGDNDSAK KVYEEVLSVT
PNDGFAKVHY GFILKAQNKI AESIPYLKEG IESGDPGTDD GRFYFHLGDA MQRVGNKEAY
RWYELGHQRG HFASVWQRSL YNVQGLKAQP WWTPKETGYT ELVKSLERNW KLIRDEGLAA
MDRTHGLFLP EDENLREKGD WSQFTLWQQG RKNENACKGA PKTCSLLDKF PETTGCRRGQ
IKYSIMHPGT HVWPHTGPTN CRLRMHLGLV IPKEGCKIRC ANETRTWEEG KVLIFDDSFE
HEVWQDAASF RLIFIVDVWH PELTPHQRRS LPAI
