EMAL3_MOUSE
ID EMAL3_MOUSE Reviewed; 897 AA.
AC Q8VC03; Q8R1S1;
DT 17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Echinoderm microtubule-associated protein-like 3;
DE Short=EMAP-3;
GN Name=Eml3;
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].
RC STRAIN=FVB/N; TISSUE=Liver, and Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Kidney;
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: Regulates mitotic spindle assembly, microtubule (MT)-
CC kinetochore attachment and chromosome separation via recruitment of
CC HAUS augmin-like complex and TUBG1 to the existing MTs and promoting
CC MT-based MT nucleation (By similarity). Required for proper alignnment
CC of chromosomes during metaphase (By similarity).
CC {ECO:0000250|UniProtKB:Q32P44}.
CC -!- SUBUNIT: Homotrimer; self-association is mediated by the N-terminal
CC coiled coil (By similarity). Interacts with EML2 but not with EML1 (By
CC similarity). Interacts (phosphorylated at Thr-882) with TUBG1, HAUS1,
CC HAUS2, HAUS3, HAUS4, HAUS5, HAUS6, HAUS7 and HAUS8.
CC {ECO:0000250|UniProtKB:Q32P44, ECO:0000250|UniProtKB:Q9HC35}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q32P44}. Nucleus {ECO:0000250|UniProtKB:Q32P44}.
CC Midbody {ECO:0000250|UniProtKB:Q32P44}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000250|UniProtKB:Q32P44}. Note=Localizes to microtubules
CC throughout all mitotic stages and localizes to the midbody during
CC cytokinesis. {ECO:0000250|UniProtKB:Q32P44}.
CC -!- PTM: Phosphorylation at Thr-882 during mitosis is required for
CC interaction with TUBG1, HAUS1, HAUS2, HAUS3, HAUS4, HAUS5, HAUS6, HAUS7
CC and HAUS8 and their recruitment to spindle microtubules.
CC {ECO:0000250|UniProtKB:Q32P44}.
CC -!- SIMILARITY: Belongs to the WD repeat EMAP family. {ECO:0000305}.
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DR EMBL; BC022146; AAH22146.1; -; mRNA.
DR EMBL; BC023878; AAH23878.1; -; mRNA.
DR EMBL; BC024134; AAH24134.1; -; mRNA.
DR CCDS; CCDS29560.1; -.
DR RefSeq; NP_659121.1; NM_144872.1.
DR AlphaFoldDB; Q8VC03; -.
DR SMR; Q8VC03; -.
DR BioGRID; 230444; 9.
DR STRING; 10090.ENSMUSP00000093960; -.
DR iPTMnet; Q8VC03; -.
DR PhosphoSitePlus; Q8VC03; -.
DR EPD; Q8VC03; -.
DR jPOST; Q8VC03; -.
DR MaxQB; Q8VC03; -.
DR PaxDb; Q8VC03; -.
DR PeptideAtlas; Q8VC03; -.
DR PRIDE; Q8VC03; -.
DR ProteomicsDB; 277826; -.
DR Antibodypedia; 28533; 54 antibodies from 13 providers.
DR DNASU; 225898; -.
DR Ensembl; ENSMUST00000096241; ENSMUSP00000093960; ENSMUSG00000071647.
DR GeneID; 225898; -.
DR KEGG; mmu:225898; -.
DR UCSC; uc008god.1; mouse.
DR CTD; 256364; -.
DR MGI; MGI:2387612; Eml3.
DR VEuPathDB; HostDB:ENSMUSG00000071647; -.
DR eggNOG; KOG2106; Eukaryota.
DR GeneTree; ENSGT00940000159589; -.
DR HOGENOM; CLU_011754_0_1_1; -.
DR InParanoid; Q8VC03; -.
DR OMA; LCTHPAQ; -.
DR OrthoDB; 271572at2759; -.
DR PhylomeDB; Q8VC03; -.
DR TreeFam; TF317832; -.
DR BioGRID-ORCS; 225898; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Eml3; mouse.
DR PRO; PR:Q8VC03; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q8VC03; protein.
DR Bgee; ENSMUSG00000071647; Expressed in retinal neural layer and 213 other tissues.
DR ExpressionAtlas; Q8VC03; baseline and differential.
DR Genevisible; Q8VC03; MM.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0030496; C:midbody; ISS:UniProtKB.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005819; C:spindle; ISS:UniProtKB.
DR GO; GO:0005876; C:spindle microtubule; 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: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:1901673; P:regulation of mitotic spindle assembly; ISS: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 InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF03451; HELP; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..897
FT /note="Echinoderm microtubule-associated protein-like 3"
FT /id="PRO_0000284391"
FT REPEAT 235..287
FT /note="WD 1"
FT REPEAT 296..345
FT /note="WD 2"
FT REPEAT 351..393
FT /note="WD 3"
FT REPEAT 399..435
FT /note="WD 4"
FT REPEAT 449..488
FT /note="WD 5"
FT REPEAT 505..544
FT /note="WD 6"
FT REPEAT 550..585
FT /note="WD 7"
FT REPEAT 590..627
FT /note="WD 8"
FT REPEAT 630..668
FT /note="WD 9"
FT REPEAT 675..710
FT /note="WD 10"
FT REPEAT 717..756
FT /note="WD 11"
FT REPEAT 766..824
FT /note="WD 12"
FT REPEAT 831..870
FT /note="WD 13"
FT REGION 51..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 875..897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 16..43
FT /evidence="ECO:0000255"
FT COMPBIAS 51..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 879..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q32P44"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32P44"
FT MOD_RES 205
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32P44"
FT MOD_RES 882
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q32P44"
FT MOD_RES 884
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q32P44"
SQ SEQUENCE 897 AA; 95695 MW; F0D1390F323BD5B1 CRC64;
MDGAAGPGEG PAHETLQTLS QRLRVQEEEM ELVKAALAEA LRLLRLHGST TTLQGSGISA
PTRNSSITVP PGLPPTCSPS LVTRGTQTEE ELEIVPSSGP PGLSNGPPAL QGGSEEPSGT
QSEGGCSSSS GAGSPGPPGI LRPVQPLQRS DTPRRNSSSS SSPSERPRQK LSRKAASSAN
LLLRSGSTES RGNKDPLSSP GGPGSRRSNY NLEGISVKMF LRGRPITMYI PSGIRSLEEL
PSGPPPETLS LDWVYGYRGR DSRSNLFVLR SGEVVYFIAC VVVLYRPGGG PGGPGGGGQR
HYRGHTDCVR CLAVHPDGVR VASGQTAGVD KDGKPLQPVV HIWDSETLLK LQEIGLGAFE
RGVGALAFSA ADQGAFLCVV DDSNEHMLSV WDCSRGVKLA EIKSTNDSVL AVGFSPRDSS
CIVTSGKSHV HFWNWSGGTG APGNGLLARK QGVFGKYKKP KFIPCFVFLP DGDILTGDSE
GNILTWGRSV SDSKTPGRGG AKETYTIVAQ AHAHEGSIFA LCLRRDGTVL SGGGRDRRLV
QWGPGLVALQ EAEIPEHFGA VRAIAEGLGS ELLVGTTKNA LLRGDLAQGF SPVIQGHTDE
LWGLCTHPSQ NRFLTCGHDR QLCLWDGEGH ALAWSMDLKE TGLCADFHPS GAVVVVGLNT
GRWLVLDTET REIVSDVTDG NEQLSVVRYS PDGLYLAIGS HDNMIYIYSV SSCGTKSSRF
GRCMGHSSFI THLDWSKDGN FIMSNSGDYE ILYWDVAGGC KLLRNRYESR DREWATYTCV
LGFHVYGVWP DGSDGTDINS LCRSHNERVV AVADDFCKVH LFQYPCARAK APSRMYSGHG
SHVTSVRFTH DDSYLVSLGG KDASIFQWRV LGAGSSGPAP ATPSRTPSLS PASSLDV
