EMAL4_MOUSE
ID EMAL4_MOUSE Reviewed; 988 AA.
AC Q3UMY5; Q6NS73; Q6NXL8; Q6NZJ8; Q6P1A7;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Echinoderm microtubule-associated protein-like 4;
DE Short=EMAP-4;
GN Name=Eml4;
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] (ISOFORM 1).
RC TISSUE=Lung;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
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 [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17196341; DOI=10.1016/j.neuroscience.2006.11.015;
RA Houtman S.H., Rutteman M., De Zeeuw C.I., French P.J.;
RT "Echinoderm microtubule-associated protein like protein 4, a member of the
RT echinoderm microtubule-associated protein family, stabilizes
RT microtubules.";
RL Neuroscience 144:1373-1382(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79; SER-144; SER-146 AND
RP SER-908, AND IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Essential for the stability of microtubules (MTs)
CC (PubMed:17196341). Essential for the formation of MTs (By similarity).
CC Required for the organization of the mitotic spindle and for the proper
CC attachment of kinetochores to MTs (By similarity). Promotes the
CC recruitment of NUDC to the mitotic spindle for mitotic progression (By
CC similarity). {ECO:0000250|UniProtKB:Q9HC35,
CC ECO:0000269|PubMed:17196341}.
CC -!- SUBUNIT: Homotrimer; self-association is mediated by the N-terminal
CC coiled coil (By similarity). Interacts (via WD repeats) with NUDC (By
CC similarity). Interacts with alpha- and beta-tubulin during mitosis (By
CC similarity). {ECO:0000250|UniProtKB:Q9HC35}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:17196341, ECO:0000305}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:17196341}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9HC35}. Cytoplasm, cytoskeleton, microtubule
CC organizing center {ECO:0000250|UniProtKB:Q9HC35}. Midbody
CC {ECO:0000250|UniProtKB:Q9HC35}. Note=Localizes to microtubules (MTs)
CC during interphase with a significantly reduced affinity for MTs during
CC mitosis. {ECO:0000250|UniProtKB:Q9HC35}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q3UMY5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3UMY5-2; Sequence=VSP_024486, VSP_024487;
CC Name=3;
CC IsoId=Q3UMY5-3; Sequence=VSP_024484, VSP_024486;
CC Name=4;
CC IsoId=Q3UMY5-4; Sequence=VSP_024485, VSP_024487;
CC -!- PTM: Phosphorylated during mitosis (By similarity). Phosphorylation at
CC Ser-144 and Ser-146 promotes its dissociation from microtubules during
CC mitosis which is required for efficient chromosome congression (By
CC similarity). {ECO:0000250|UniProtKB:Q9HC35}.
CC -!- SIMILARITY: Belongs to the WD repeat EMAP family. {ECO:0000305}.
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DR EMBL; AK144604; BAE25963.1; -; mRNA.
DR EMBL; BC065178; AAH65178.1; -; mRNA.
DR EMBL; BC066099; AAH66099.1; -; mRNA.
DR EMBL; BC067011; AAH67011.1; -; mRNA.
DR EMBL; BC070427; AAH70427.1; -; mRNA.
DR EMBL; BC079619; AAH79619.1; -; mRNA.
DR CCDS; CCDS37708.1; -. [Q3UMY5-4]
DR CCDS; CCDS50192.1; -. [Q3UMY5-1]
DR CCDS; CCDS50193.1; -. [Q3UMY5-2]
DR RefSeq; NP_001107834.1; NM_001114362.1.
DR RefSeq; NP_001273496.1; NM_001286567.1.
DR RefSeq; NP_955760.3; NM_199466.3.
DR AlphaFoldDB; Q3UMY5; -.
DR SMR; Q3UMY5; -.
DR BioGRID; 219641; 3.
DR STRING; 10090.ENSMUSP00000094528; -.
DR iPTMnet; Q3UMY5; -.
DR PhosphoSitePlus; Q3UMY5; -.
DR EPD; Q3UMY5; -.
DR jPOST; Q3UMY5; -.
DR MaxQB; Q3UMY5; -.
DR PaxDb; Q3UMY5; -.
DR PeptideAtlas; Q3UMY5; -.
DR PRIDE; Q3UMY5; -.
DR ProteomicsDB; 277827; -. [Q3UMY5-1]
DR ProteomicsDB; 277828; -. [Q3UMY5-2]
DR ProteomicsDB; 277829; -. [Q3UMY5-3]
DR ProteomicsDB; 277830; -. [Q3UMY5-4]
DR DNASU; 78798; -.
DR GeneID; 78798; -.
DR KEGG; mmu:78798; -.
DR UCSC; uc008drx.2; mouse. [Q3UMY5-4]
DR UCSC; uc008dry.2; mouse. [Q3UMY5-3]
DR UCSC; uc008dsb.2; mouse. [Q3UMY5-2]
DR CTD; 27436; -.
DR MGI; MGI:1926048; Eml4.
DR eggNOG; KOG2106; Eukaryota.
DR InParanoid; Q3UMY5; -.
DR OrthoDB; 271572at2759; -.
DR PhylomeDB; Q3UMY5; -.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 78798; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Eml4; mouse.
DR PRO; PR:Q3UMY5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UMY5; protein.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB.
DR GO; GO:0048487; F:beta-tubulin binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase plate congression; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:MGI.
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 InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF03451; HELP; 1.
DR Pfam; PF00400; WD40; 5.
DR SMART; SM00320; WD40; 9.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..988
FT /note="Echinoderm microtubule-associated protein-like 4"
FT /id="PRO_0000284392"
FT REPEAT 270..308
FT /note="WD 1"
FT REPEAT 312..359
FT /note="WD 2"
FT REPEAT 367..407
FT /note="WD 3"
FT REPEAT 414..449
FT /note="WD 4"
FT REPEAT 456..495
FT /note="WD 5"
FT REPEAT 511..549
FT /note="WD 6"
FT REPEAT 554..590
FT /note="WD 7"
FT REPEAT 593..632
FT /note="WD 8"
FT REPEAT 636..673
FT /note="WD 9"
FT REPEAT 679..715
FT /note="WD 10"
FT REPEAT 722..761
FT /note="WD 11"
FT REPEAT 771..829
FT /note="WD 12"
FT REPEAT 836..875
FT /note="WD 13"
FT REGION 1..260
FT /note="Microtubule-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT REGION 106..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 14..63
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT COMPBIAS 110..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 134
FT /note="Phosphoserine; by NEK7"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 144
FT /note="Phosphoserine; by NEK6"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 146
FT /note="Phosphoserine; by NEK7"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 201
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 237
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 248
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 620
FT /note="Phosphothreonine; by NEK6 and NEK7"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 914
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HC35"
FT VAR_SEQ 1..8
FT /note="MDGFAGSL -> MNRVSSDPVAIP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024484"
FT VAR_SEQ 113..214
FT /note="SGTEKKKEKPQGQREKKEDSHSNDQSPQIRASPSPQPSSQPLQINRQTPESK
FT SSAPIKSIKRPPTAEKSHNSWENSDDSRNKLMKTVSTSKLISKVIKNADK -> R (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024485"
FT VAR_SEQ 114..171
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024486"
FT VAR_SEQ 223..233
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024487"
FT CONFLICT 603
FT /note="R -> T (in Ref. 2; AAH67011/AAH66099/AAH79619/
FT AAH65178/AAH70427)"
FT /evidence="ECO:0000305"
FT CONFLICT 804
FT /note="N -> I (in Ref. 2; AAH67011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 988 AA; 110027 MW; 950336CFC1C178D5 CRC64;
MDGFAGSLDD SISAASTSDV QDRLSALESR VQQQEDEITV LKAALADVLR RLAISEDHVA
SVKKSMPSKG QPSLREAISM SCITNGSGIS RKQNHTSSVS IARKETLSSA AKSGTEKKKE
KPQGQREKKE DSHSNDQSPQ IRASPSPQPS SQPLQINRQT PESKSSAPIK SIKRPPTAEK
SHNSWENSDD SRNKLMKTVS TSKLISKVIK NADKHKDVIV NQAKMSTREK NSQEGEYIKM
FMRGRPITMF IPSDVDNYDD IRTELPPEKL KLEWVYGYRG KDCRANVYLL PTGEIVYFIA
SVVVLFNYEE RTQRHYLGHT DCVRCLAVHP DKIRIATGQI AGVDKDGRPL QPHVRVWDSV
SLTTLHVIGL GTFERGVGCL DFSKADSGVH LCVIDDSNEH MLTVWDWQKK SKIAEIKTTN
EVVLAVEFHP TDANTIITCG KSHIFFWTWS GNSLTRKQGI FGKYEKPKFV QCLAFLGNGD
VLTGDSGGVM LIWSKTMVEP PPGKGPKGVY QINRQIKAHD GSVFTLCQMR NGMLLTGGGK
DRKIILWDHD LNLEREIEVP DQYGTIRAVA EGRAEQFLVG TSRNFILRGT FNDGFQIEVQ
GHRDELWGLA THPFKDLLLT CAQDRQVCMW NSVEHRLEWT RLVDEPGHCA DFHPSGTVVA
IGTHSGRWFV LDAETRDLVS IHTDGNEQLS VMRYSVDGTL LAVGSHDNFI YLYTVLENGR
KYSRYGKCTG HSSYITHLDW SPDNKHIMSN SGDYEILYWD IENGCKLIRN RSDCKDIDWT
TYTCVLGFQV FGVWPEGSDG TDINALVRSH NRRVIAVADD FCKVHLFQYP CSKAKAPSHK
YSAHSSHVTN VSFTHNDSHL ISTGGKDMSI IQWKLVEKLP VPQNEVITDA SVTKTPASSS
ETARPSNSPP LPPSLPLTGT AEEESRMGSS PTLVENSLEQ IAEPSEEQSE WGSEDLGVVI
DEEPASELSE TQGATELPEE ERGITPLC
