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 05-JUN-2019, entry version 121. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA Hara Y., Nishida M., Numata T., Medina M.T., Takeuchi T., Morita R., RA Bai D., Ganesh S., Sugimoto Y., Inazawa J., Bailey J.N., Ochoa A., RA Jara-Prado A., Rasmussen A., Ramos-Peek J., Cordova S., RA Rubio-Donnadieu F., Inoue Y., Osawa M., Kaneko S., Oguni H., Mori Y., RA 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 RT is an axonemal protein widely conserved among organisms with motile RT cilia and 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 RT expression."; RL Cell 143:1174-1189(2010). CC -!- FUNCTION: Microtubule-associated protein which regulates cell CC division and neuronal migration during cortical development. CC Necessary for mitotic spindle organization. Necessary for radial CC and tangential cell migration during brain development, possibly CC acting as a regulator of cell morphology and process formation CC during migration (By similarity). May enhance calcium influx CC through CACNA1E and stimulate programmed cell death. CC Overexpression of EFHC1 in hippocampal primary culture neurons CC 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 CC organizing center, centrosome {ECO:0000250|UniProtKB:Q5JVL4}. CC Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q5JVL4}. CC Cytoplasm, cytoskeleton, spindle pole CC {ECO:0000250|UniProtKB:Q5JVL4}. CC -!- TISSUE SPECIFICITY: Expressed in adult brain including CC hippocampus, cerebellum, cerebral cortex, thalamus, hypothalamus, CC amygdala and upper brainstem. Expressed in soma and dentrites of CC pyramidal neurons of the hippocampal CA1 region, pyramidal neurons CC of the cerebral cortex and Purkinje cells of cerebellum. Highly CC expressed in testis, trachea, and oviduct, moderately in lung, and CC slightly in brain. Highly expressed in sperm flagella and tracheal CC cilia (at protein level). {ECO:0000269|PubMed:15258581, CC 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 eggNOG; ENOG410XQCQ; LUCA. DR HOGENOM; HOG000265451; -. DR InParanoid; Q9D9T8; -. DR KO; K23029; -. DR OrthoDB; 236088at2759; -. DR PhylomeDB; Q9D9T8; -. DR PRO; PR:Q9D9T8; -. DR Proteomes; UP000000589; Unplaced. 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 Complete proteome; Cytoplasm; Cytoskeleton; Reference proteome; KW Repeat. FT CHAIN 1 648 EF-hand domain-containing protein 1. FT /FTId=PRO_0000073878. FT DOMAIN 93 198 DM10 1. {ECO:0000255|PROSITE- FT ProRule:PRU00665}. FT DOMAIN 239 359 DM10 2. {ECO:0000255|PROSITE- FT ProRule:PRU00665}. FT DOMAIN 416 520 DM10 3. {ECO:0000255|PROSITE- FT ProRule:PRU00665}. FT DOMAIN 582 617 EF-hand. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT REGION 1 45 Required for its localization in the FT mitotic spindle and interaction with FT alpha-tubulin. FT {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 //