ID A0A455C615_PHYMC Unreviewed; 754 AA.
AC A0A455C615;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Aspartyl/asparaginyl beta-hydroxylase isoform X12 {ECO:0000313|RefSeq:XP_028356502.1};
GN Name=ASPH {ECO:0000313|RefSeq:XP_028356502.1};
OS Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Physeteridae; Physeter.
OX NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028356502.1};
RN [1] {ECO:0000313|RefSeq:XP_028356502.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_028356502.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-
CC pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC family. {ECO:0000256|ARBA:ARBA00007730}.
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DR RefSeq; XP_028356502.1; XM_028500701.2.
DR AlphaFoldDB; A0A455C615; -.
DR Ensembl; ENSPCTT00005008894; ENSPCTP00005008074; ENSPCTG00005005499.
DR Proteomes; UP000248484; Chromosome 15.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0062101; F:peptidyl-aspartic acid 3-dioxygenase activity; IEA:InterPro.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; ASPARTYL/ASPARAGINYL BETA-HYDROXYLASE; 1.
DR PANTHER; PTHR12366:SF33; ASPARTYL_ASPARAGINYL BETA-HYDROXYLASE; 1.
DR Pfam; PF05279; Asp-B-Hydro_N; 1.
DR Pfam; PF05118; Asp_Arg_Hydrox; 1.
DR Pfam; PF13174; TPR_6; 1.
DR SMART; SM00028; TPR; 2.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022964};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248484};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 59..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 48..113
FT /note="Aspartyl beta-hydroxylase/Triadin"
FT /evidence="ECO:0000259|Pfam:PF05279"
FT REPEAT 450..483
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 587..741
FT /note="Aspartyl/asparaginy/proline hydroxylase"
FT /evidence="ECO:0000259|Pfam:PF05118"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 377..404
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 84486 MW; 6AE56E7274D7DD45 CRC64;
MAPRKNAKGG GGNSSSSSSS SSSPSSCTSG GSSSPGARRE TKHGGHKNGR KGGLSGSSFF
TWFMVIALLG VWTSVAVVWF DLVDYEEVLG KLGIYDADGD GDFDVDDAKV LLGLKERSAP
KPTVPPEETE PYPWLEDQVL EGPGPQNIED EVQEQVQSLL DETIYAEHGE DLHQEQDGPA
GELQPEDGIF AGGVTDDRYE PVGTGAVHEE TEDSYHVEET ASPAYSQDME DMIYEQENPD
SSEPVVDDAG RTYQEADDIT YQEYDEQAFE PSENEGTESS DNAVDDSNTI LEEVHVPPAE
EQREVPPETN KKTDDPEKKG KVKKKKPKLL NKLDKTIKAE LDAAEKLRKQ GKIEEAVHAF
EELVQKYPQS PGARYGKAKC EDDLAEKRRS NEILRRAIKS YQEAASLPDV PADLVKLSLK
RQSDRQQFLG HMRGSLLTLQ KLVQLFPDDT SLKNDLGVGY LLIGDNDSAK KVYEEVLNVT
PNDGFAKVHY GFILKAQNKI AESIPYLKEG IESGDPGTDD GRFYFHLGDA MQRVGNKEAY
KWYELGHQRG HFASVWQRSL YNVHGLKAQP WWTPKETGYT ELVKSLERNW KLIRDEGLAV
MDRAQGLFLP EDENLREKGD WSQFTLWQQG RKNENACKGA PKTCSLLDKF PETTGCRRGQ
IKYSVMHPGT HVWPHTGPTN CRLRMHLGLV IPKEGCKIRC ANETKTWEEG KVLIFDDSFE
HEVWQDATSF RLIFIVDVWH PELTPHQRRS LPAI
//
