MED1_MOUSE
ID MED1_MOUSE Reviewed; 1575 AA.
AC Q925J9; A2A526; A2A528; O88323; Q3UHV0; Q6AXD5; Q8BW37; Q8BX19; Q8VDQ7;
AC Q925K0;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 1;
DE AltName: Full=Mediator complex subunit 1;
DE AltName: Full=Peroxisome proliferator-activated receptor-binding protein;
DE Short=PBP;
DE Short=PPAR-binding protein;
DE AltName: Full=Thyroid hormone receptor-associated protein complex 220 kDa component;
DE Short=Trap220;
DE AltName: Full=Thyroid receptor-interacting protein 2;
DE Short=TR-interacting protein 2;
DE Short=TRIP-2;
GN Name=Med1; Synonyms=Crsp210, Drip205, Pbp, Pparbp, Trap220, Trip2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC31118.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH PPARA; PPARG; RARA; RXRA AND THRB.
RC TISSUE=Liver {ECO:0000269|PubMed:9325263};
RX PubMed=9325263; DOI=10.1074/jbc.272.41.25500;
RA Zhu Y., Qi C., Jain S., Rao M.S., Reddy J.K.;
RT "Isolation and characterization of PBP, a protein that interacts with
RT peroxisome proliferator-activated receptor.";
RL J. Biol. Chem. 272:25500-25506(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK56102.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND VARIANTS SER-960 AND MET-1348.
RC STRAIN=ILS {ECO:0000312|EMBL:AAK56102.1}, and
RC ISS {ECO:0000312|EMBL:AAK56101.1};
RX PubMed=11471062; DOI=10.1007/s00335-001-1001-x;
RA Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J.,
RA Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.;
RT "High-throughput sequence identification of gene coding variants within
RT alcohol-related QTLs.";
RL Mamm. Genome 12:657-663(2001).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAN75014.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND VARIANTS SER-960 AND MET-1348.
RC STRAIN=129/Ola {ECO:0000312|EMBL:AAN75014.1};
RX PubMed=14500757; DOI=10.1210/me.2003-0097;
RA Landles C., Chalk S., Steel J.H., Rosewell I., Spencer-Dene B.,
RA Lalani E.-N., Parker M.G.;
RT "The thyroid hormone receptor-associated protein TRAP220 is required at
RT distinct embryonic stages in placental, cardiac, and hepatic development.";
RL Mol. Endocrinol. 17:2418-2435(2003).
RN [4] {ECO:0000305, ECO:0000312|EMBL:BAC35779.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-389 (ISOFORMS 1/4), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1-964 (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC35779.2};
RC TISSUE=Embryonic stem cell {ECO:0000269|PubMed:16141072}, and
RC Ovary {ECO:0000312|EMBL:BAC35779.2};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAH79636.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH79636.1}, and
RC Czech II {ECO:0000312|EMBL:AAH21440.1};
RC TISSUE=Brain {ECO:0000269|PubMed:15489334}, and
RC Mammary gland {ECO:0000269|PubMed:15489334};
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).
RN [7]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=10882104; DOI=10.1016/s1097-2765(00)80247-6;
RA Ito M., Yuan C.-X., Okano H.J., Darnell R.B., Roeder R.G.;
RT "Involvement of the TRAP220 component of the TRAP/SMCC coactivator complex
RT in embryonic development and thyroid hormone action.";
RL Mol. Cell 5:683-693(2000).
RN [8] {ECO:0000305}
RP INTERACTION WITH YWHAH.
RX PubMed=11266503; DOI=10.1210/mend.15.4.0624;
RA Zilliacus J., Holter E., Wakui H., Tazawa H., Treuter E., Gustafsson J.-A.;
RT "Regulation of glucocorticoid receptor activity by 14-3-3-dependent
RT intracellular relocalization of the corepressor RIP140.";
RL Mol. Endocrinol. 15:501-511(2001).
RN [9]
RP FUNCTION.
RX PubMed=12037571; DOI=10.1038/417563a;
RA Ge K., Guermah M., Yuan C.-X., Ito M., Wallberg A.E., Spiegelman B.M.,
RA Roeder R.G.;
RT "Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated
RT adipogenesis.";
RL Nature 417:563-567(2002).
RN [10]
RP FUNCTION, AND INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
RX PubMed=11867769; DOI=10.1073/pnas.261715899;
RA Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.;
RT "The TRAP/Mediator coactivator complex interacts directly with estrogen
RT receptors alpha and beta through the TRAP220 subunit and directly enhances
RT estrogen receptor function in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002).
RN [11]
RP INTERACTION WITH NR4A3.
RX PubMed=12709428; DOI=10.1074/jbc.m300088200;
RA Wansa K.D., Harris J.M., Yan G., Ordentlich P., Muscat G.E.;
RT "The AF-1 domain of the orphan nuclear receptor NOR-1 mediates trans-
RT activation, coactivator recruitment, and activation by the purine anti-
RT metabolite 6-mercaptopurine.";
RL J. Biol. Chem. 278:24776-24790(2003).
RN [12]
RP FUNCTION, AND INTERACTION WITH PPARGC1A.
RX PubMed=14636573; DOI=10.1016/s1097-2765(03)00391-5;
RA Wallberg A.E., Yamamura S., Malik S., Spiegelman B.M., Roeder R.G.;
RT "Coordination of p300-mediated chromatin remodeling and TRAP/mediator
RT function through coactivator PGC-1alpha.";
RL Mol. Cell 12:1137-1149(2003).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15150259; DOI=10.1074/jbc.m402391200;
RA Jia Y., Qi C., Kashireddy P., Surapureddi S., Zhu Y.-J., Rao M.S.,
RA Le Roith D., Chambon P., Gonzalez F.J., Reddy J.K.;
RT "Transcription coactivator PBP, the peroxisome proliferator-activated
RT receptor (PPAR)-binding protein, is required for PPARalpha-regulated gene
RT expression in liver.";
RL J. Biol. Chem. 279:24427-24434(2004).
RN [14]
RP ERRATUM OF PUBMED:15150259.
RA Jia Y., Qi C., Kashireddy P., Surapureddi S., Zhu Y.-J., Rao M.S.,
RA Le Roith D., Chambon P., Gonzalez F.J., Reddy J.K.;
RL J. Biol. Chem. 279:29870-29870(2004).
RN [15]
RP FUNCTION, AND INTERACTION OF THE MEDIATOR COMPLEX WITH THRA.
RX PubMed=15340084; DOI=10.1128/mcb.24.18.8244-8254.2004;
RA Malik S., Guermah M., Yuan C.-X., Wu W., Yamamura S., Roeder R.G.;
RT "Structural and functional organization of TRAP220, the TRAP/mediator
RT subunit that is targeted by nuclear receptors.";
RL Mol. Cell. Biol. 24:8244-8254(2004).
RN [16]
RP FUNCTION, AND ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=16137621; DOI=10.1016/j.molcel.2005.08.008;
RA Park S.W., Li G., Lin Y.-P., Barrero M.J., Ge K., Roeder R.G., Wei L.-N.;
RT "Thyroid hormone-induced juxtaposition of regulatory elements/factors and
RT chromatin remodeling of Crabp1 dependent on MED1/TRAP220.";
RL Mol. Cell 19:643-653(2005).
RN [17]
RP FUNCTION, INTERACTION WITH GATA1, AND ASSOCIATION WITH PROMOTER REGIONS.
RX PubMed=17132730; DOI=10.1073/pnas.0604494103;
RA Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P., Zhang X.,
RA Guyot B., Roeder R.G., Borggrefe T.;
RT "The mediator complex functions as a coactivator for GATA-1 in
RT erythropoiesis via subunit Med1/TRAP220.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18504-18509(2006).
RN [18]
RP ERRATUM OF PUBMED:17132730.
RA Stumpf M., Waskow C., Kroetschel M., van Essen D., Rodriguez P., Zhang X.,
RA Guyot B., Roeder R.G., Borggrefe T.;
RL Proc. Natl. Acad. Sci. U.S.A. 104:1442-1442(2007).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-953 AND SER-955, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-664; THR-805; SER-955;
RP THR-1051; THR-1057; SER-1158; SER-1209; SER-1435; THR-1442; SER-1465;
RP SER-1467; SER-1481 AND SER-1484, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [21]
RP INTERACTION WITH CLOCK.
RX PubMed=24043798; DOI=10.1073/pnas.1305980110;
RA Lande-Diner L., Boyault C., Kim J.Y., Weitz C.J.;
RT "A positive feedback loop links circadian clock factor CLOCK-BMAL1 to the
RT basic transcriptional machinery.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:16021-16026(2013).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 641-654 IN COMPLEX WITH RARB AND
RP RXRA.
RX PubMed=15528208; DOI=10.1074/jbc.m409302200;
RA Pogenberg V., Guichou J.F., Vivat-Hannah V., Kammerer S., Perez E.,
RA Germain P., de Lera A.R., Gronemeyer H., Royer C.A., Bourguet W.;
RT "Characterization of the interaction between retinoic acid
RT receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional
RT coactivators through structural and fluorescence anisotropy studies.";
RL J. Biol. Chem. 280:1625-1633(2005).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors. Essential for embryogenesis,
CC including development of the central nervous system, heart, liver and
CC placenta and for erythropoiesis. Also required for normal
CC transcriptional control of thyroid-stimulating hormone beta (TSHB) in
CC the pituitary. Acts as a coactivator for GATA1-mediated transcriptional
CC activation during erythroid differentiation of K562 erythroleukemia
CC cells (By similarity). {ECO:0000250|UniProtKB:Q15648,
CC ECO:0000269|PubMed:10882104, ECO:0000269|PubMed:11867769,
CC ECO:0000269|PubMed:12037571, ECO:0000269|PubMed:14500757,
CC ECO:0000269|PubMed:14636573, ECO:0000269|PubMed:15150259,
CC ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:16137621,
CC ECO:0000269|PubMed:17132730, ECO:0000269|PubMed:9325263}.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC module termed the CDK8 module. Mediator containing the CDK8 module is
CC less active than Mediator lacking this module in supporting
CC transcriptional activation. Individual preparations of the Mediator
CC complex lacking one or more distinct subunits have been variously
CC termed ARC, CRSP, DRIP, PC2, SMCC and TRAP. This subunit specifically
CC interacts with a number of nuclear receptors in a ligand-dependent
CC fashion including AR, ESR1, ESR2, PPARA, PPARG, RORA, RXRA, RXRG, THRA,
CC THRB and VDR. Interacts with CTNNB1, GABPA, GLI3, PPARGC1A and TP53.
CC Interacts with GATA1 and YWHAH. Interacts with CLOCK; this interaction
CC requires the presence of THRAP3. Interacts with CCAR1 (By similarity).
CC Interacts with NR4A3 (PubMed:12709428). Interacts (via IBM motif) with
CC PSIP1 (via IBD domain); phosphorylation increases its affinity for
CC PSIP1 (By similarity). {ECO:0000250|UniProtKB:Q15648,
CC ECO:0000269|PubMed:11266503, ECO:0000269|PubMed:11867769,
CC ECO:0000269|PubMed:12709428, ECO:0000269|PubMed:14636573,
CC ECO:0000269|PubMed:15340084, ECO:0000269|PubMed:15528208,
CC ECO:0000269|PubMed:17132730, ECO:0000269|PubMed:24043798,
CC ECO:0000269|PubMed:9325263}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15150259}. Note=A
CC subset of the protein may enter the nucleolus subsequent to
CC phosphorylation by MAPK1 or MAPK3. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1 {ECO:0000303|PubMed:16141072};
CC IsoId=Q925J9-1; Sequence=Displayed;
CC Name=2 {ECO:0000303|PubMed:15489334};
CC IsoId=Q925J9-2; Sequence=VSP_051893, VSP_051896;
CC Name=3 {ECO:0000303|PubMed:16141072};
CC IsoId=Q925J9-3; Sequence=VSP_051894, VSP_051895;
CC Name=4 {ECO:0000269|PubMed:11471062, ECO:0000269|PubMed:9325263};
CC IsoId=Q925J9-4; Sequence=VSP_051892;
CC -!- TISSUE SPECIFICITY: Widely expressed in the adult, with high levels of
CC expression in the liver, lung, intestinal mucosa, kidney cortex, thymic
CC cortex, splenic follicle and seminiferous epithelium in testis. Also
CC expressed in the adult heart, brain, spleen and skeletal muscle.
CC {ECO:0000269|PubMed:14500757, ECO:0000269|PubMed:9325263}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed during embryonic development; at
CC stages 9.5 dpc-10.5 dpc, expression is strongest in neural tissues. At
CC 11.5 dpc-12.5 dpc, expression is abundant throughout embryonic tissues,
CC being strongest in the developing liver, primitive gut, nasopharynx,
CC and developing limb buds. Moderately expressed at this stage in the
CC brain and optic stalk, branchial arch and urogential ridge. Expressed
CC at a low level in the heart. By stage 13.5 dpc-14.5 dpc, expression is
CC abundant in the forebrain, vagus nerve, dorsal root ganglia,
CC nasopharynx, kidney, liver, pancreas, intestine, gut, thymus, lung,
CC genital tubercle, tongue and lower jaw. Moderately expressed in the
CC midbrain and expressed at a low level in the heart and large blood
CC vessels. In the developing placenta, expression is moderate in the
CC giant and spongiotrophoblast cell layers and strongest in the
CC labyrinthine portion throughout 9.5 dpc-13.5 dpc.
CC {ECO:0000269|PubMed:10882104, ECO:0000269|PubMed:14500757}.
CC -!- PTM: Phosphorylated by MAPK1 or MAPK3 during G2/M phase which may
CC enhance protein stability and promote entry into the nucleolus (By
CC similarity). Phosphorylation increases its interaction with PSIP1 (By
CC similarity). {ECO:0000250|UniProtKB:Q15648}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH21440.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF000294; AAC31118.1; -; mRNA.
DR EMBL; AF332073; AAK56101.1; -; mRNA.
DR EMBL; AF332074; AAK56102.1; -; mRNA.
DR EMBL; AY176046; AAN75014.1; -; Genomic_DNA.
DR EMBL; AK049203; BAC33607.2; -; mRNA.
DR EMBL; AK054437; BAC35779.2; -; mRNA.
DR EMBL; AK147199; BAE27757.1; -; mRNA.
DR EMBL; AL591205; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021440; AAH21440.1; ALT_INIT; mRNA.
DR EMBL; BC079636; AAH79636.1; -; mRNA.
DR CCDS; CCDS25341.1; -. [Q925J9-4]
DR CCDS; CCDS36300.1; -. [Q925J9-1]
DR PIR; T02885; T02885.
DR RefSeq; NP_001073587.1; NM_001080118.1. [Q925J9-1]
DR RefSeq; NP_038662.2; NM_013634.2. [Q925J9-4]
DR RefSeq; NP_598788.2; NM_134027.2. [Q925J9-3]
DR PDB; 1XDK; X-ray; 2.90 A; C/D/G/H=641-654.
DR PDBsum; 1XDK; -.
DR AlphaFoldDB; Q925J9; -.
DR SMR; Q925J9; -.
DR BioGRID; 202318; 14.
DR ComplexPortal; CPX-3264; Core mediator complex.
DR CORUM; Q925J9; -.
DR DIP; DIP-59232N; -.
DR ELM; Q925J9; -.
DR IntAct; Q925J9; 10.
DR MINT; Q925J9; -.
DR STRING; 10090.ENSMUSP00000103169; -.
DR iPTMnet; Q925J9; -.
DR PhosphoSitePlus; Q925J9; -.
DR EPD; Q925J9; -.
DR jPOST; Q925J9; -.
DR MaxQB; Q925J9; -.
DR PaxDb; Q925J9; -.
DR PeptideAtlas; Q925J9; -.
DR PRIDE; Q925J9; -.
DR ProteomicsDB; 292184; -. [Q925J9-1]
DR ProteomicsDB; 292185; -. [Q925J9-2]
DR ProteomicsDB; 292186; -. [Q925J9-3]
DR ProteomicsDB; 292187; -. [Q925J9-4]
DR Antibodypedia; 4326; 531 antibodies from 39 providers.
DR DNASU; 19014; -.
DR Ensembl; ENSMUST00000018304; ENSMUSP00000018304; ENSMUSG00000018160. [Q925J9-4]
DR Ensembl; ENSMUST00000107545; ENSMUSP00000103169; ENSMUSG00000018160. [Q925J9-1]
DR GeneID; 19014; -.
DR KEGG; mmu:19014; -.
DR UCSC; uc007lfo.1; mouse. [Q925J9-3]
DR UCSC; uc007lfp.1; mouse. [Q925J9-1]
DR CTD; 5469; -.
DR MGI; MGI:1100846; Med1.
DR VEuPathDB; HostDB:ENSMUSG00000018160; -.
DR eggNOG; ENOG502QPZ7; Eukaryota.
DR GeneTree; ENSGT00660000095569; -.
DR HOGENOM; CLU_245015_0_0_1; -.
DR InParanoid; Q925J9; -.
DR OMA; HAMKLTY; -.
DR OrthoDB; 57581at2759; -.
DR PhylomeDB; Q925J9; -.
DR TreeFam; TF324954; -.
DR Reactome; R-MMU-212436; Generic Transcription Pathway.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR Reactome; R-MMU-9707564; Cytoprotection by HMOX1.
DR BioGRID-ORCS; 19014; 18 hits in 78 CRISPR screens.
DR ChiTaRS; Med1; mouse.
DR EvolutionaryTrace; Q925J9; -.
DR PRO; PR:Q925J9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q925J9; protein.
DR Bgee; ENSMUSG00000018160; Expressed in rostral migratory stream and 270 other tissues.
DR ExpressionAtlas; Q925J9; baseline and differential.
DR Genevisible; Q925J9; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0070847; C:core mediator complex; ISO:MGI.
DR GO; GO:0016592; C:mediator complex; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0050693; F:LBD domain binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0042974; F:nuclear retinoic acid receptor binding; ISO:MGI.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISS:UniProtKB.
DR GO; GO:0042809; F:nuclear vitamin D receptor binding; ISO:MGI.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; ISS:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0006702; P:androgen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:BHF-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
DR GO; GO:0031100; P:animal organ regeneration; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0000902; P:cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IMP:MGI.
DR GO; GO:0071383; P:cellular response to steroid hormone stimulus; ISO:MGI.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISO:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0001892; P:embryonic placenta development; IMP:MGI.
DR GO; GO:0048822; P:enucleate erythrocyte development; IMP:MGI.
DR GO; GO:0060750; P:epithelial cell proliferation involved in mammary gland duct elongation; IMP:MGI.
DR GO; GO:0048821; P:erythrocyte development; IMP:BHF-UCL.
DR GO; GO:0045444; P:fat cell differentiation; IMP:MGI.
DR GO; GO:0045023; P:G0 to G1 transition; IMP:MGI.
DR GO; GO:0007507; P:heart development; IMP:MGI.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030216; P:keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0007595; P:lactation; IMP:MGI.
DR GO; GO:0002088; P:lens development in camera-type eye; IMP:BHF-UCL.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0060745; P:mammary gland branching involved in pregnancy; IMP:MGI.
DR GO; GO:0060744; P:mammary gland branching involved in thelarche; IMP:MGI.
DR GO; GO:0033598; P:mammary gland epithelial cell proliferation; IMP:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:BHF-UCL.
DR GO; GO:0030224; P:monocyte differentiation; IMP:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0035357; P:peroxisome proliferator activated receptor signaling pathway; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0070318; P:positive regulation of G0 to G1 transition; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISS:UniProtKB.
DR GO; GO:2000347; P:positive regulation of hepatocyte proliferation; IMP:MGI.
DR GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; IMP:MGI.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:MGI.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR GO; GO:2001141; P:regulation of RNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0070562; P:regulation of vitamin D receptor signaling pathway; IMP:MGI.
DR GO; GO:0003406; P:retinal pigment epithelium development; IMP:BHF-UCL.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0006590; P:thyroid hormone generation; IMP:MGI.
DR GO; GO:0002154; P:thyroid hormone mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:MGI.
DR GO; GO:0003222; P:ventricular trabecula myocardium morphogenesis; IMP:BHF-UCL.
DR DisProt; DP02151; -.
DR InterPro; IPR019680; Mediator_Med1.
DR Pfam; PF10744; Med1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..1575
FT /note="Mediator of RNA polymerase II transcription subunit
FT 1"
FT /id="PRO_0000058553"
FT REGION 1..670
FT /note="Interaction with the Mediator complex and THRA"
FT /evidence="ECO:0000250"
FT REGION 16..590
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT REGION 108..212
FT /note="Interaction with the Mediator complex"
FT /evidence="ECO:0000250"
FT REGION 215..390
FT /note="Interaction with the Mediator complex"
FT /evidence="ECO:0000250"
FT REGION 405..644
FT /note="Interaction with THRA"
FT /evidence="ECO:0000250"
FT REGION 542..789
FT /note="Interaction with VDR"
FT /evidence="ECO:0000250"
FT REGION 609..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..701
FT /note="Interaction with GATA1"
FT /evidence="ECO:0000269|PubMed:17132730"
FT REGION 622..701
FT /note="Interaction with PPARGC1A and THRA"
FT /evidence="ECO:0000250"
FT REGION 656..1066
FT /note="Interaction with ESR1"
FT /evidence="ECO:0000250"
FT REGION 737..760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1564
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1423
FT /note="Interaction with TP53"
FT /evidence="ECO:0000250"
FT MOTIF 604..608
FT /note="LXXLL motif 1"
FT MOTIF 645..649
FT /note="LXXLL motif 2"
FT MOTIF 875..902
FT /note="Integrase domain-binding motif (IBM)"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT COMPBIAS 652..680
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 742..756
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..994
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1020
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1053
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1075..1199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1351..1368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1500..1514
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1525..1549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 588
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 795
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 805
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 953
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1032
FT /note="Phosphothreonine; by MAPK1 or MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1051
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1057
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1158
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1217
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1405
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1442
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1459
FT /note="Phosphothreonine; by MAPK1 or MAPK3"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1467
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1481
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT MOD_RES 1484
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1523
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q15648"
FT VAR_SEQ 1..15
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11471062,
FT ECO:0000303|PubMed:9325263"
FT /id="VSP_051892"
FT VAR_SEQ 548..632
FT /note="YGMTTGNNPMSGTTTPTNTFPGGPITTLFNMSMSIKDRHESVGHGEDFSKVS
FT QNPILTSLLQITGNGGSTIGSSPTPPHHTPPPV -> VEEKRQDKPSLGHLPPIQVCSP
FT SCLKDGKDMKSTCTYLLLLLLLLEFMVFCFFFFFLTYSSVFGLHVKGLWTKICSDVQEY
FT FSVS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051893"
FT VAR_SEQ 548..556
FT /note="YGMTTGNNP -> SKNPELGSG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_051894"
FT VAR_SEQ 557..1575
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_051895"
FT VAR_SEQ 633..1575
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051896"
FT VARIANT 960
FT /note="T -> S (in strain: ISS and 129/Ola)"
FT /evidence="ECO:0000269|PubMed:11471062,
FT ECO:0000269|PubMed:14500757"
FT VARIANT 1348
FT /note="T -> M (in strain: ISS and 129/Ola)"
FT /evidence="ECO:0000269|PubMed:11471062,
FT ECO:0000269|PubMed:14500757"
FT CONFLICT 84
FT /note="I -> L (in Ref. 1; AAC31118)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="A -> T (in Ref. 6; AAH21440)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="L -> H (in Ref. 4; BAE27757)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="F -> S (in Ref. 1; AAC31118)"
FT /evidence="ECO:0000305"
FT CONFLICT 382..389
FT /note="LPDGQSLQ -> VLPNKAVS (in Ref. 4; BAC35779)"
FT /evidence="ECO:0000305"
FT CONFLICT 948
FT /note="E -> K (in Ref. 4; BAC33607)"
FT /evidence="ECO:0000305"
FT CONFLICT 964
FT /note="G -> A (in Ref. 4; BAC33607)"
FT /evidence="ECO:0000305"
FT CONFLICT 1323
FT /note="G -> S (in Ref. 1; AAC31118)"
FT /evidence="ECO:0000305"
FT CONFLICT 1387
FT /note="G -> R (in Ref. 1; AAC31118)"
FT /evidence="ECO:0000305"
FT HELIX 643..649
FT /evidence="ECO:0007829|PDB:1XDK"
SQ SEQUENCE 1575 AA; 167141 MW; C3B8121A26003A22 CRC64;
MKAQGETEDS ERLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS
CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL
CDVKVAHHGE NPVSCPELVQ QLREKNFEEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL
EQDLSKMAIM YWKATNAAPL DKILHGSVGY LTPRSGGHLM NMKYYASPSD LLDDKTASPI
ILHEKNVPRS LGMNASVTIE GTSAMYKLPI APLIMGSHPA DNKWTPSFSA VTSANSVDLP
ACFFLKFPQP IPVSKAFVQK LQNCTGIPLF ETPPTYLPLY ELITQFELSK DPDPLPLNHN
MRFYAALPGQ QHCYFLNKDA PLPDGQSLQG TLVSKITFQH PGRVPLILNM IRHQVAYNTL
IGSCVKRTIL KEDSPGLLQF EVCPLSESRF SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY
KGLSDALICT DDFIAKVVQR CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL
PPASSPGYGM TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ
NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK DNPAQDFSTL
YGSSPLERQN SSSGSPRMEM CSGSNKAKKK KSSRVPPDKP KHQTEDDFQR ELFSMDVDSQ
NPMFDVSMTA DALDTPHITP APSQCSTPPA TYPQPVSHPQ PSIQRMVRLS SSDSIGPDVT
DILSDIAEEA SKLPSTSDDC PPIGTPVRDS SSSGHSQSAL FDSDVFQTNN NENPYTDPAD
LIADAAGSPN SDSPTNHFFP DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS
QALNTLGMPM LGGDNGEPKF KGSSQADTVD FSIISVAGKA LGAADLMEHH SGSQSPLLTT
GELGKEKTQK RVKEGNGTGA SSGSGPGSDS KPGKRSRTPS NDGKSKDKPP KRKKADTEGK
SPSHSSSNRP FTPPTSTGGS KSPGSSGRSQ TPPGVATPPI PKITIQIPKG TVMVGKPSSH
SQYTSSGSVS SSGSKSHHSH SSSSSSLASA STSGKVKSSK SEGSSSSKLS GSMYASQGSS
GSSQSKNSSQ TGGKPGSSPI TKHGLSSGSS STKMKPQGKP SSLMNPSISK PNISPSHSRP
PGGSDKLASP MKPVPGTPPS SKAKSPISSG SSGSHVSGTS SSSGMKSSSG SASSGSVSQK
TPPASNSCTP SSSSFSSSGS SMSSSQNQHG SSKGKSPSRN KKPSLTAVID KLKHGVVTSG
PGGEDPIDSQ MGASTNSSNH PMSSKHNTSG GEFQSKREKS DKDKSKVSAS GGSVDSSKKT
SESKNVGSTG VAKIIISKHD GGSPSIKAKV TLQKPGESGG DGLRPQIASS KNYGSPLISG
STPKHERGSP SHSKSPAYTP QNVDSESESG SSIAERSYQN SPSSEDGIRP LPEYSTEKHK
KHKKEKKKVR DKDRDKKKSH SMKPENWSKS PISSDPTASV TNNPILSADR PSRLSPDFMI
GEEDDDLMDV ALIGN
