EVI2A_MOUSE
ID EVI2A_MOUSE Reviewed; 223 AA.
AC P20934; Q6DKP1;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein EVI2A;
DE AltName: Full=Ecotropic viral integration site 2A protein;
DE Short=EVI-2A;
DE Flags: Precursor;
GN Name=Evi2a; Synonyms=Evi-2, Evi-2a, Evi2;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN MYELOGENOUS LEUKEMIA.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=2167436; DOI=10.1128/mcb.10.9.4658-4666.1990;
RA Buchberg A.M., Bedigian H.G., Jenkins N.A., Copeland N.G.;
RT "Evi-2, a common integration site involved in murine myeloid
RT leukemogenesis.";
RL Mol. Cell. Biol. 10:4658-4666(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Brain cortex, Corpora quadrigemina, Medulla oblongata, and
RC Spinal cord;
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197 AND SER-203, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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).
CC -!- FUNCTION: May complex with itself or/and other proteins within the
CC membrane, to function as part of a cell-surface receptor.
CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
CC -!- DISEASE: Note=Expression of this gene is altered by viral integration
CC and this altered expression may predispose cells to myeloid disease
CC (PubMed:2167436). {ECO:0000269|PubMed:2167436}.
CC -!- SIMILARITY: Belongs to the EVI2A family. {ECO:0000305}.
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DR EMBL; M34896; AAA37583.1; -; mRNA.
DR EMBL; M34897; AAA37584.1; -; mRNA.
DR EMBL; AK044098; BAC31775.1; -; mRNA.
DR EMBL; AK046407; BAC32711.1; -; mRNA.
DR EMBL; AK160302; BAE35731.1; -; mRNA.
DR EMBL; AK162958; BAE37135.1; -; mRNA.
DR EMBL; AK170527; BAE41859.1; -; mRNA.
DR EMBL; AK171594; BAE42550.1; -; mRNA.
DR EMBL; AL591174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466556; EDL15609.1; -; Genomic_DNA.
DR EMBL; BC038124; AAH38124.1; -; mRNA.
DR CCDS; CCDS25122.1; -.
DR PIR; A36462; A36462.
DR RefSeq; NP_001028883.1; NM_001033711.1.
DR RefSeq; NP_034291.1; NM_010161.3.
DR AlphaFoldDB; P20934; -.
DR SMR; P20934; -.
DR STRING; 10090.ENSMUSP00000125936; -.
DR GlyConnect; 2626; 2 N-Linked glycans (1 site).
DR GlyGen; P20934; 4 sites, 2 N-linked glycans (1 site).
DR iPTMnet; P20934; -.
DR PhosphoSitePlus; P20934; -.
DR PaxDb; P20934; -.
DR PeptideAtlas; P20934; -.
DR PRIDE; P20934; -.
DR ProteomicsDB; 275697; -.
DR DNASU; 14017; -.
DR Ensembl; ENSMUST00000103236; ENSMUSP00000099526; ENSMUSG00000078771.
DR Ensembl; ENSMUST00000170799; ENSMUSP00000125936; ENSMUSG00000078771.
DR GeneID; 14017; -.
DR KEGG; mmu:14017; -.
DR UCSC; uc007kkq.1; mouse.
DR CTD; 2123; -.
DR MGI; MGI:95458; Evi2a.
DR VEuPathDB; HostDB:ENSMUSG00000078771; -.
DR eggNOG; ENOG502S3SG; Eukaryota.
DR GeneTree; ENSGT00390000003004; -.
DR HOGENOM; CLU_073339_0_0_1; -.
DR InParanoid; P20934; -.
DR OMA; KCAVRTR; -.
DR OrthoDB; 1364705at2759; -.
DR PhylomeDB; P20934; -.
DR TreeFam; TF336075; -.
DR BioGRID-ORCS; 14017; 2 hits in 72 CRISPR screens.
DR PRO; PR:P20934; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P20934; protein.
DR Bgee; ENSMUSG00000078771; Expressed in granulocyte and 199 other tissues.
DR ExpressionAtlas; P20934; baseline and differential.
DR Genevisible; P20934; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR008608; Ectropic_vir_integratn_site_2A.
DR PANTHER; PTHR15568; PTHR15568; 1.
DR Pfam; PF05399; EVI2A; 1.
DR PIRSF; PIRSF019625; EVI_S2A; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..223
FT /note="Protein EVI2A"
FT /id="PRO_0000021212"
FT TOPO_DOM 20..125
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..151
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..223
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 40..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 135
FT /note="V -> A (in Ref. 1; AAA37583)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 223 AA; 24087 MW; B49013A0F5C7CFBD CRC64;
MEHKGQYLHL VFLMTTVWAS SSSGTRPNYT HLWASSVTAS GSSNQNGSSR HPSDNNTNLV
TPAVGHKVSA TDKPASSPPV PLASTSTLKS STPHAFRNSS PTAEIKSQGE TFKKEVCEEN
TSNTAMLICL IVIAVLFLIC TFLFLSTVVL ANKVSSLKRS KQVGKRQPRS NGDFLASSGL
WTAESDTWKR AKELTGSNLL LQSPGVLTAA RERKHEEGTE KLN
