JMJD8_RAT
ID JMJD8_RAT Reviewed; 271 AA.
AC Q6AY40;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 3.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=JmjC domain-containing protein 8 {ECO:0000305};
DE AltName: Full=Jumonji domain-containing protein 8;
DE Flags: Precursor;
GN Name=Jmjd8 {ECO:0000312|RGD:1307381};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Functions as a positive regulator of TNF-induced NF-kappaB
CC signaling. Regulates angiogenesis and cellular metabolism through
CC interaction with PKM. {ECO:0000250|UniProtKB:Q96S16}.
CC -!- SUBUNIT: Oligomer. Dimer. Interacts with PKM; regulates angiogenesis
CC and metabolism. {ECO:0000250|UniProtKB:Q96S16}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q96S16}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q96S16}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q96S16}.
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DR EMBL; AABR03073234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC079205; AAH79205.1; -; mRNA.
DR RefSeq; NP_001014138.1; NM_001014116.1.
DR AlphaFoldDB; Q6AY40; -.
DR SMR; Q6AY40; -.
DR STRING; 10116.ENSRNOP00000026789; -.
DR GlyGen; Q6AY40; 3 sites.
DR PhosphoSitePlus; Q6AY40; -.
DR PaxDb; Q6AY40; -.
DR GeneID; 360498; -.
DR KEGG; rno:360498; -.
DR UCSC; RGD:1307381; rat.
DR CTD; 339123; -.
DR RGD; 1307381; Jmjd8.
DR VEuPathDB; HostDB:ENSRNOG00000019729; -.
DR eggNOG; KOG2131; Eukaryota.
DR HOGENOM; CLU_074983_0_0_1; -.
DR InParanoid; Q6AY40; -.
DR OrthoDB; 1029368at2759; -.
DR PhylomeDB; Q6AY40; -.
DR PRO; PR:Q6AY40; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000019729; Expressed in pancreas and 20 other tissues.
DR ExpressionAtlas; Q6AY40; baseline and differential.
DR Genevisible; Q6AY40; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; ISS:UniProtKB.
DR GO; GO:0006110; P:regulation of glycolytic process; ISS:UniProtKB.
DR GO; GO:1903302; P:regulation of pyruvate kinase activity; ISS:UniProtKB.
DR InterPro; IPR041667; Cupin_8.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF13621; Cupin_8; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endoplasmic reticulum; Glycoprotein; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..271
FT /note="JmjC domain-containing protein 8"
FT /evidence="ECO:0000255"
FT /id="PRO_0000344533"
FT DOMAIN 149..271
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT CARBOHYD 137
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 271 AA; 30751 MW; 62153649A1E9FCFB CRC64;
MLMAAAGRFG LLLLIVLWTM VTVVLPASGE GGWKQSRLGT EAAVMEEERC TVERRAHLTY
SEFMQHYAFL KPVILQGLTD NSKFRALCSR ENLLASFGDN VVRLSTANTY SYQKVDLPFQ
EYVEQLLHPQ DPESLGNDTL YFFGDNNFTE WAPLFQHYRP PPFRLLGTTP AYSFGIAGAG
SGVPFHWHGP GFSEVIYGRK RWFLYPPEKT PEFHPNKTTL AWLLEIYPSL APSARPLECT
IQAGEALYFP DRWWHATLNL DTSVFISTFL G
