EMAL1_MOUSE
ID EMAL1_MOUSE Reviewed; 814 AA.
AC Q05BC3; Q05AF8; Q0P5V3;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Echinoderm microtubule-associated protein-like 1;
DE Short=EMAP-1;
GN Name=Eml1;
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 [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, and 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).
RN [3]
RP FUNCTION, ROLE IN DISEASE, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY,
RP SUBCELLULAR LOCATION, MUTAGENESIS OF THR-242, AND SUBUNIT.
RX PubMed=24859200; DOI=10.1038/nn.3729;
RA Kielar M., Tuy F.P., Bizzotto S., Lebrand C., de Juan Romero C.,
RA Poirier K., Oegema R., Mancini G.M., Bahi-Buisson N., Olaso R.,
RA Le Moing A.G., Boutourlinsky K., Boucher D., Carpentier W., Berquin P.,
RA Deleuze J.F., Belvindrah R., Borrell V., Welker E., Chelly J.,
RA Croquelois A., Francis F.;
RT "Mutations in Eml1 lead to ectopic progenitors and neuronal heterotopia in
RT mouse and human.";
RL Nat. Neurosci. 17:923-933(2014).
RN [4]
RP INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA Prochazka J., Sedlacek R.;
RT "Fam208a orchestrates interaction protein network essential for early
RT embryonic development and cell division.";
RL Exp. Cell Res. 382:111437-111437(2019).
CC -!- FUNCTION: Modulates the assembly and organization of the microtubule
CC cytoskeleton, and probably plays a role in regulating the orientation
CC of the mitotic spindle and the orientation of the plane of cell
CC division. Required for normal proliferation of neuronal progenitor
CC cells in the developing brain and for normal brain development. Does
CC not affect neuron migration per se. {ECO:0000269|PubMed:24859200}.
CC -!- SUBUNIT: Homotrimer; self-association is mediated by the N-terminal
CC coiled coil (By similarity). Does not interact with EML3 (By
CC similarity). Binds unpolymerized tubulins via its WD repeat region (By
CC similarity). Binds repolymerizing microtubules (PubMed:24859200).
CC Interacts with TASOR (PubMed:31112734). {ECO:0000250|UniProtKB:O00423,
CC ECO:0000250|UniProtKB:Q9HC35, ECO:0000269|PubMed:24859200,
CC ECO:0000269|PubMed:31112734}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24859200}.
CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:24859200}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:24859200}. Note=Detected in
CC cytoplasmic punctae. Co-localizes with microtubules. Enriched in
CC perinuclear regions during interphase and in the region of spindle
CC microtubules during metaphase. Enriched at the midzone during telophase
CC and cytokinesis. Detected at growth cones in neurons.
CC {ECO:0000269|PubMed:24859200}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q05BC3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q05BC3-2; Sequence=VSP_024477;
CC Name=3;
CC IsoId=Q05BC3-3; Sequence=VSP_024478;
CC -!- TISSUE SPECIFICITY: Detected in adult brain cortex, hippocampus and
CC thalamus (PubMed:24859200). Expressed in the stomach, lungs and in
CC Sertoli cells of the testis (PubMed:31112734).
CC {ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:31112734}.
CC -!- DEVELOPMENTAL STAGE: Detected from 13.5 dpc to the first day after
CC birth in cortical neuron progenitor cells in the ventricular zone and
CC in postmitotic neurons in the cortical plate.
CC {ECO:0000269|PubMed:24859200}.
CC -!- DOMAIN: Contains a tandem atypical propeller in EMLs (TAPE) domain. The
CC N-terminal beta-propeller is formed by canonical WD repeats; in
CC contrast, the second beta-propeller contains one blade that is formed
CC by discontinuous parts of the polypeptide chain.
CC {ECO:0000250|UniProtKB:O00423}.
CC -!- DOMAIN: The N-terminal coiled coil is required for association with
CC microtubules. {ECO:0000250|UniProtKB:O00423}.
CC -!- DISEASE: Note=Defects in Eml1 are the cause of the neuronal heterotopia
CC observed in HeCo mice. These mice display heterotopic neurons in the
CC rostro-medial part of the neocortex, together with epilepsy and subtle
CC learning deficits in adults. At 17 dpc both Tbr1(+) and Cux1(+) neurons
CC contribute to the heterotopia. Three days after birth, most Tbr1(+)
CC have reached their final destination, but many Cux1(+) neurons remain
CC in the heterotopia and fail to reach cortical layers II to IV, contrary
CC to the situation in wild-type. Besides, progenitor cells continue to
CC proliferate, resulting in large numbers of abnormally positioned
CC actively proliferating cells during both early and late stages of
CC corticogenesis. In HeCo mice, insertion of a retrotransposon into Eml1
CC leads to the absence of full-length Eml1 transcripts.
CC -!- SIMILARITY: Belongs to the WD repeat EMAP family. {ECO:0000305}.
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DR EMBL; BC053094; AAH53094.2; -; mRNA.
DR EMBL; BC059839; AAH59839.1; -; mRNA.
DR EMBL; BC079582; AAH79582.1; -; mRNA.
DR EMBL; BC125289; AAI25290.1; -; mRNA.
DR CCDS; CCDS36555.1; -. [Q05BC3-1]
DR CCDS; CCDS36556.1; -. [Q05BC3-2]
DR RefSeq; NP_001036800.1; NM_001043335.1. [Q05BC3-1]
DR RefSeq; NP_001036801.1; NM_001043336.2. [Q05BC3-2]
DR RefSeq; NP_001273275.1; NM_001286346.1.
DR RefSeq; NP_001273276.1; NM_001286347.1.
DR RefSeq; XP_017170659.1; XM_017315170.1.
DR RefSeq; XP_017170661.1; XM_017315172.1.
DR AlphaFoldDB; Q05BC3; -.
DR SMR; Q05BC3; -.
DR BioGRID; 212902; 3.
DR IntAct; Q05BC3; 1.
DR STRING; 10090.ENSMUSP00000105486; -.
DR iPTMnet; Q05BC3; -.
DR PhosphoSitePlus; Q05BC3; -.
DR MaxQB; Q05BC3; -.
DR PaxDb; Q05BC3; -.
DR PRIDE; Q05BC3; -.
DR ProteomicsDB; 275603; -. [Q05BC3-1]
DR ProteomicsDB; 275604; -. [Q05BC3-2]
DR ProteomicsDB; 275605; -. [Q05BC3-3]
DR Antibodypedia; 27460; 87 antibodies from 25 providers.
DR Ensembl; ENSMUST00000054955; ENSMUSP00000057209; ENSMUSG00000058070. [Q05BC3-2]
DR Ensembl; ENSMUST00000109860; ENSMUSP00000105486; ENSMUSG00000058070. [Q05BC3-1]
DR GeneID; 68519; -.
DR KEGG; mmu:68519; -.
DR UCSC; uc007ozq.2; mouse. [Q05BC3-1]
DR CTD; 2009; -.
DR MGI; MGI:1915769; Eml1.
DR VEuPathDB; HostDB:ENSMUSG00000058070; -.
DR eggNOG; KOG2106; Eukaryota.
DR GeneTree; ENSGT00940000153887; -.
DR HOGENOM; CLU_011754_2_0_1; -.
DR InParanoid; Q05BC3; -.
DR OMA; TTRDIQW; -.
DR OrthoDB; 271572at2759; -.
DR PhylomeDB; Q05BC3; -.
DR TreeFam; TF317832; -.
DR BioGRID-ORCS; 68519; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Eml1; mouse.
DR PRO; PR:Q05BC3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q05BC3; protein.
DR Bgee; ENSMUSG00000058070; Expressed in interventricular septum and 168 other tissues.
DR ExpressionAtlas; Q05BC3; baseline and differential.
DR Genevisible; Q05BC3; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR005108; HELP.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR Pfam; PF03451; HELP; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 10.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Microtubule; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..814
FT /note="Echinoderm microtubule-associated protein-like 1"
FT /id="PRO_0000284386"
FT REPEAT 260..309
FT /note="WD 1"
FT REPEAT 314..357
FT /note="WD 2"
FT REPEAT 362..399
FT /note="WD 3"
FT REPEAT 408..445
FT /note="WD 4"
FT REPEAT 449..488
FT /note="WD 5"
FT REPEAT 492..529
FT /note="WD 6"
FT REPEAT 534..571
FT /note="WD 7"
FT REPEAT 577..612
FT /note="WD 8"
FT REPEAT 616..654
FT /note="WD 9"
FT REPEAT 663..700
FT /note="WD 10"
FT REPEAT 708..767
FT /note="WD 11"
FT REPEAT 774..813
FT /note="WD 12"
FT REGION 77..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..814
FT /note="Tandem atypical propeller in EMLs"
FT /evidence="ECO:0000250"
FT COILED 31..72
FT /evidence="ECO:0000255"
FT COMPBIAS 89..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024477"
FT VAR_SEQ 181
FT /note="P -> PALQSPKPQGKRRVTHCK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024478"
FT MUTAGEN 242
FT /note="T->A: Impairs tubulin binding."
FT /evidence="ECO:0000269|PubMed:24859200"
FT CONFLICT 113
FT /note="A -> S (in Ref. 1; AAI25290)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="G -> C (in Ref. 1; AAH59839)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 814 AA; 89680 MW; 9881D29F4C2899D5 CRC64;
MEDGFSSYSS LYDTSSLLQF CNDDSASAAS SMEVSDRIAS LEQRVQMQED DIQLLKSALA
DVVRRLNITE EQQAVLNRKG PTKARPLGQT LPLRTTVNNG TVLPKKPSAS LPAPSGARKE
VVVPVTKSIN RTSSSERVSP GGRRESSGDS KGSRNRTGST SSSSSGKKNS ESKPKEPAFS
PEEGYVKMFL RGRPVTMYMP KDQVDSYSLE AKAELPTKRL KLEWVYGYRG RDCRNNLYLL
PTGETVYFIA SVVVLYNVEE QLQRHYAGHN DDVKCLAVHP DRITIATGQV AGTSKDGKQL
PPHVRIWDSV TLNTLHVIGI GFFDRAVTCI AFSKSNGGGH LCAVDDSNDH VLSVWDWQKE
ERLADVKCSN EAVFAADFHP TDTNIIVTCG KSHLYFWTLE GNSLNKKQGL FEKQEKPKFV
LCVTFSENGD TITGDSSGNI LVWGKGTNRI SYAVQGAHEG GIFALCMLRD GTLVSGGGKD
RRLISWNGNY QKLHKAEIPE QFGPIRTVAE GKGNVILIGT TRNFVLQGTL SGDFTPITQG
HTDELWGLAI HASKPQFLTC GHDKHATLWD AVGHRPVWDK IIEDPAQSSG FHPSGSVVAV
GTLTGRWFVF DTETKDLVTV HTDGNEQLSV MRYSPDGNFL AIGSHDNCIY IYGVTDNGRK
YTRVGKCSGH SSFITHLDWS VNSQFLVSNS GDYEILYWVP SACKQVVSVE TTRDIEWATY
TCTLGFHVFG VWPEGSDGTD INAVCRAHER KLLCTGDDFG KVHLFSYPCS QFRAPSHIYS
GHSSHVTNVD FLCEDSHLIS TGGKDTSIMQ WRVI
