ID F6YKA0_CALJA Unreviewed; 742 AA.
AC F6YKA0;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 4.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Aspartate beta-hydroxylase {ECO:0000313|Ensembl:ENSCJAP00000016812.5};
GN Name=ASPH {ECO:0000313|Ensembl:ENSCJAP00000016812.5};
OS Callithrix jacchus (White-tufted-ear marmoset).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Callitrichinae; Callithrix; Callithrix.
OX NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000016812.5, ECO:0000313|Proteomes:UP000008225};
RN [1] {ECO:0000313|Ensembl:ENSCJAP00000016812.5}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCJAP00000016812.5}
RP IDENTIFICATION.
RG Ensembl;
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 Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004157};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004157}.
CC -!- SIMILARITY: Belongs to the aspartyl/asparaginyl beta-hydroxylase
CC family. {ECO:0000256|ARBA:ARBA00007730}.
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DR AlphaFoldDB; F6YKA0; -.
DR Ensembl; ENSCJAT00000017774.5; ENSCJAP00000016812.5; ENSCJAG00000009122.5.
DR GeneTree; ENSGT00940000156304; -.
DR HOGENOM; CLU_023717_0_0_1; -.
DR Proteomes; UP000008225; Chromosome 16.
DR Bgee; ENSCJAG00000009122; Expressed in testis and 6 other cell types or tissues.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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; PF13432; TPR_16; 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:UP000008225};
KW Sarcoplasmic reticulum {ECO:0000256|ARBA:ARBA00022951};
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 25..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..79
FT /note="Aspartyl beta-hydroxylase/Triadin"
FT /evidence="ECO:0000259|Pfam:PF05279"
FT REPEAT 438..471
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 575..729
FT /note="Aspartyl/asparaginy/proline hydroxylase"
FT /evidence="ECO:0000259|Pfam:PF05118"
FT REGION 87..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 365..392
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 94..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 742 AA; 84669 MW; A08F75289781FF4D CRC64;
MAEDKETKHG GHKNGRKGGL SGTSFFTWFM VIALLGVWTS VAVVWFDLVD YEEVLGKLGV
YDADGDGDFD VDDAKVLLEG SSGVAKRKTK AKGLKERSTS EPAVPPEEAE PHAEPEEQAP
MEAEPQNIED EAKEQIQSLL HEMMHAEHGE DLQQEEDGPA GEPQPEDADF LTATDVSDRF
EILEPEVFHE ETEHSYHLEE TVSQDYNQDM EEMMSEQENP DSSEPVVEDE RLHHDTDDVT
YQIYEERAVY EPPENEGIEI AEVTVPPEDN AVEDSKVIVE EVSIPPVEEK QEVPPETNRK
TEDPEQKAKV KKKKPKLLNK FDKTIKAELD AAEKLRKRGK IEEAVNAFKE LVRKYPQSPR
ARYGKAQCED DLAEKRRSNE VLREAIETYQ EVASLPDVPE DLLKLSLKRR SDRQQFLGHM
RGSLLTLQRL VHLFPNDTSL KNDLGVGYLL IGDNDNAKKV YEEVLSMTPN DGFAKVHYGF
ILKAQNKIAE SISYLKEGIE SGDPGTDDGR FYFHLGDAMQ RVGNKEAYKW YELGHKRGHF
ASVWQRSLYN VNGLKAQPWW TPKETGYTDL VKSLERNWKL IRDEGLAVMD KAKGLFLPED
ENLREKGDWS QFTLWQQGRR NENACKGAPK TCTLLEKFPE TTGCRRGQIK YSIMHPGTHV
WPHTGPTNCR LRMHLGLVIP KEGCKIRCAD ETKTWEEGKV LIFDDSFEHE VWQDASSFRL
IFIVDVWHPE LTPQQRRSLP AI
//
