ID EFHC1_MOUSE Reviewed; 648 AA. AC Q9D9T8; DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 12-AUG-2020, entry version 126. DE RecName: Full=EF-hand domain-containing protein 1; DE AltName: Full=Myoclonin-1; GN Name=Efhc1; 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=C57BL/6J; TISSUE=Testis; 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 FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=15258581; DOI=10.1038/ng1393; RA Suzuki T., Delgado-Escueta A.V., Aguan K., Alonso M.E., Shi J., Hara Y., RA Nishida M., Numata T., Medina M.T., Takeuchi T., Morita R., Bai D., RA Ganesh S., Sugimoto Y., Inazawa J., Bailey J.N., Ochoa A., Jara-Prado A., RA Rasmussen A., Ramos-Peek J., Cordova S., Rubio-Donnadieu F., Inoue Y., RA Osawa M., Kaneko S., Oguni H., Mori Y., Yamakawa K.; RT "Mutations in EFHC1 cause juvenile myoclonic epilepsy."; RL Nat. Genet. 36:842-849(2004). RN [3] RP TISSUE SPECIFICITY. RX PubMed=15670853; DOI=10.1016/j.febslet.2004.12.070; RA Ikeda T., Ikeda K., Enomoto M., Park M.K., Hirono M., Kamiya R.; RT "The mouse ortholog of EFHC1 implicated in juvenile myoclonic epilepsy is RT an axonemal protein widely conserved among organisms with motile cilia and RT flagella."; RL FEBS Lett. 579:819-822(2005). RN [4] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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: Microtubule-associated protein which regulates cell division CC and neuronal migration during cortical development. Necessary for CC mitotic spindle organization. Necessary for radial and tangential cell CC migration during brain development, possibly acting as a regulator of CC cell morphology and process formation during migration (By similarity). CC May enhance calcium influx through CACNA1E and stimulate programmed CC cell death. Overexpression of EFHC1 in hippocampal primary culture CC neurons induced apoptosis. {ECO:0000250|UniProtKB:Q5JVL4, CC ECO:0000269|PubMed:15258581}. CC -!- SUBUNIT: Interacts with the C-terminus of CACNA1E. InteractS with CC alpha-tubulin. {ECO:0000250|UniProtKB:Q5JVL4}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing CC center, centrosome {ECO:0000250|UniProtKB:Q5JVL4}. Cytoplasm, CC cytoskeleton, spindle {ECO:0000250|UniProtKB:Q5JVL4}. Cytoplasm, CC cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q5JVL4}. CC -!- TISSUE SPECIFICITY: Expressed in adult brain including hippocampus, CC cerebellum, cerebral cortex, thalamus, hypothalamus, amygdala and upper CC brainstem. Expressed in soma and dentrites of pyramidal neurons of the CC hippocampal CA1 region, pyramidal neurons of the cerebral cortex and CC Purkinje cells of cerebellum. Highly expressed in testis, trachea, and CC oviduct, moderately in lung, and slightly in brain. Highly expressed in CC sperm flagella and tracheal cilia (at protein level). CC {ECO:0000269|PubMed:15258581, ECO:0000269|PubMed:15670853}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK006489; BAB24614.1; -; mRNA. DR CCDS; CCDS48227.1; -. DR RefSeq; NP_082250.1; NM_027974.1. DR SMR; Q9D9T8; -. DR STRING; 10090.ENSMUSP00000042343; -. DR iPTMnet; Q9D9T8; -. DR PhosphoSitePlus; Q9D9T8; -. DR MaxQB; Q9D9T8; -. DR PaxDb; Q9D9T8; -. DR PRIDE; Q9D9T8; -. DR GeneID; 71877; -. DR KEGG; mmu:71877; -. DR CTD; 114327; -. DR MGI; MGI:1919127; Efhc1. DR eggNOG; KOG0043; Eukaryota. DR InParanoid; Q9D9T8; -. DR KO; K23029; -. DR OrthoDB; 236088at2759; -. DR PhylomeDB; Q9D9T8; -. DR BioGRID-ORCS; 71877; 0 hits in 18 CRISPR screens. DR PRO; PR:Q9D9T8; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q9D9T8; protein. DR GO; GO:0005930; C:axoneme; IDA:UniProtKB. DR GO; GO:0005813; C:centrosome; ISO:MGI. DR GO; GO:0005929; C:cilium; IDA:MGI. DR GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB. DR GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB. DR GO; GO:0000922; C:spindle pole; ISS:UniProtKB. DR GO; GO:0043014; F:alpha-tubulin binding; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB. DR GO; GO:0006874; P:cellular calcium ion homeostasis; NAS:UniProtKB. DR GO; GO:0021795; P:cerebral cortex cell migration; ISO:MGI. DR GO; GO:0060285; P:cilium-dependent cell motility; IBA:GO_Central. DR GO; GO:0000281; P:mitotic cytokinesis; ISS:UniProtKB. DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; NAS:UniProtKB. DR GO; GO:0051302; P:regulation of cell division; ISS:UniProtKB. DR CDD; cd00051; EFh; 1. DR InterPro; IPR010554; DUF1126. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR040193; EFHC1/EFHC2/EFHB. DR InterPro; IPR006602; Uncharacterised_DM10. DR PANTHER; PTHR12086; PTHR12086; 1. DR Pfam; PF06565; DUF1126; 3. DR SMART; SM00676; DM10; 3. DR SMART; SM00054; EFh; 1. DR SUPFAM; SSF47473; SSF47473; 1. DR PROSITE; PS51336; DM10; 3. DR PROSITE; PS50222; EF_HAND_2; 1. PE 1: Evidence at protein level; KW Cytoplasm; Cytoskeleton; Reference proteome; Repeat. FT CHAIN 1..648 FT /note="EF-hand domain-containing protein 1" FT /id="PRO_0000073878" FT DOMAIN 93..198 FT /note="DM10 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00665" FT DOMAIN 239..359 FT /note="DM10 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00665" FT DOMAIN 416..520 FT /note="DM10 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00665" FT DOMAIN 582..617 FT /note="EF-hand" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 1..45 FT /note="Required for its localization in the mitotic spindle FT and interaction with alpha-tubulin" FT /evidence="ECO:0000250|UniProtKB:Q5JVL4" SQ SEQUENCE 648 AA; 75142 MW; BBA3377AADB9D373 CRC64; MGTNPVHGLP FLPGSSFTDS TKTAFHRSQT LNYRNGYAVV RRPTMGIGGD RLHYNQLSQA ELDELANKAP ILTYGPLKQA PLAEFVPAHV AFDKKVLKFS AYFQEDVPIS MEEHYRIRHV NIYYYLEDDS MSVIEPVVEN SGIPQGKLIK RQRFTKNDMG DHYHWKDLNR GINLTVYGKT FRIVDCDRFT QDFLESQGIE LNPSEKIPLD PYTQLRKEPV RKYVTPSDFD QLKQFLTFDK QVLRFYAIWD DTDSLFGECR HYIIHYYLMD DTVEIREVHE RNNGRDPFPL LMNRQRMPKV LVENAKNFPK CVLEISDQEV LEWYTAKDFI VGKPLTILGR TFFIYDCDPF TRQFYKDKFG MPDLPPVDVT KKEPPPVKQE LPPYNGYGLI EDSAQNCFAL IPKAPRKDVV KMLMNDNKVL RYLAALESPI PEDKDRRFVF SYFLATDMIS IFEPPVRNSG IIGGKFLGRT KVVKSFSPVD NPIYYSPSDF FIGAVIEVFG HRFVILDTDE YVLKYMESNA SQYSPEALAS IQNRIQKPEL PAPELESKQA TGEPMVQGTE ESKVQDLDAL IDQIHMHLKY NSYKENLRET FQMYDKDESG YVDRETFFKI CETLNVPVDD SLIKELIRLC THGEGRINYY NFVRAFSN //