ID A0A096MKE0_RAT Unreviewed; 737 AA.
AC A0A096MKE0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Aspartate-beta-hydroxylase {ECO:0000313|Ensembl:ENSRNOP00000068479.1};
GN Name=Asph {ECO:0000313|Ensembl:ENSRNOP00000068479.1,
GN ECO:0000313|RGD:1312000};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000068479.1, ECO:0000313|Proteomes:UP000002494};
RN [1] {ECO:0000313|Ensembl:ENSRNOP00000068479.1, ECO:0000313|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068479.1,
RC ECO:0000313|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RG Rat Genome Sequencing Project Consortium;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000313|Ensembl:ENSRNOP00000068479.1}
RP IDENTIFICATION.
RC STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000068479.1};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006225255.1; XM_006225193.3.
DR RefSeq; XP_006237920.1; XM_006237858.3.
DR AlphaFoldDB; A0A096MKE0; -.
DR SMR; A0A096MKE0; -.
DR jPOST; A0A096MKE0; -.
DR Ensembl; ENSRNOT00000076426.3; ENSRNOP00000068479.1; ENSRNOG00000007445.9.
DR AGR; RGD:1312000; -.
DR CTD; 444; -.
DR RGD; 1312000; Asph.
DR GeneTree; ENSGT00940000156304; -.
DR OrthoDB; 37221at2759; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007445; Expressed in skeletal muscle tissue and 20 other cell types or tissues.
DR ExpressionAtlas; A0A096MKE0; baseline and differential.
DR GO; GO:0032541; C:cortical endoplasmic reticulum; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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 GO; GO:0008283; P:cell population proliferation; ISO:RGD.
DR GO; GO:0060325; P:face morphogenesis; ISO:RGD.
DR GO; GO:0035108; P:limb morphogenesis; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0007389; P:pattern specification process; ISO:RGD.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISO:RGD.
DR GO; GO:0051480; P:regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:1901879; P:regulation of protein depolymerization; ISO:RGD.
DR GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
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 Pfam; PF13181; TPR_8; 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 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|PeptideAtlas:A0A096MKE0};
KW Reference proteome {ECO:0000313|Proteomes:UP000002494};
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 61..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..115
FT /note="Aspartyl beta-hydroxylase/Triadin"
FT /evidence="ECO:0000259|Pfam:PF05279"
FT REPEAT 433..466
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 570..724
FT /note="Aspartyl/asparaginy/proline hydroxylase"
FT /evidence="ECO:0000259|Pfam:PF05118"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 360..387
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 9..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 737 AA; 82662 MW; A345DEF7BC5B6A1A CRC64;
MAPRKNAKGG GGNSSSSGSG SGSGSPSTGS SGSSSSPGAR REAKHGGHKN GRRGGISGGS
FFTWFMVIAL LGVWTSVAVV WFDLVDYEEV LGKLGVYDAD GDGDFDVDDA KVLLGLKERS
TSERTFPPEE AETQAELEEQ APEGAEAQNV EDEVKEQIQS LLQESVHTDH DLEADGPAGE
PQSEVEDFLT ATDSDDRFEA LEPGTVHEDT EDSYHVEETA SQNHPNDAEE VMSEQESSDH
GEAVTDDGLQ QHAEEVRHED YDEPVYEPSE NERIEISDNA IDDSNIISEE INVASVEEQQ
DTPPVKKKKP KLLNKFDKTI KAELDAAEKL RKRGKIEEAV SAFEELVRRY PQSPRARYGK
AQCEDDLAEK QRSNEVLRRA IETYQEAASL PDAPTDLVKL SLKRRSERQQ FLGHMRGSLL
TLQRLVQLFP SDTTLKNDLG VGYLLMGDND SAKKVYEEVL NVTPNDGFAK VHYGFILKAQ
NRIAESIPYL KEGIESGDPG TDDGRFYFHL GDAMQRVGNK EAYKWYELGH KRGHFASVWQ
RSLYNVNGLK AQPWWTPRET GYTELVKSLE RNWKLIRDEG LMVMDKAKGL FLPEDENLRE
KGDWSQFTLW QQGRKNENAC KGAPKTCTLL EKFSETTGCR RGQIKYSIMH PGTHVWPHTG
PTNCRLRMHL GLVIPKEGCK IRCANETRSW EEGKVLIFDD SFEHEVWQDA SSFRLIFIVD
VWHPELTPQQ RRSLPAI
//
