Q9WTI7 (MYO1C_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Unconventional myosin-Ic

Alternative name(s):
Myosin I beta
Short name=MMI-beta
Short name=MMIb

Gene names

Name:

Myo1c

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1063 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails are presumed to bind to membranous compartments, which would be moved relative to actin filaments By similarity. Involved in glucose transporter recycling in response to insulin by regulating movement of intracellular GLUT4-containing vesicles to the plasma membrane. Component of the hair cell's (the sensory cells of the inner ear) adaptation-motor complex. Acts as a mediator of adaptation of mechanoelectrical transduction in stereocilia of vestibular hair cells. Binds phosphoinositides and links the actin cytoskeleton to cellular membranes. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19 Isoform 3 is involved in regulation of transcription. Associated with transcriptional active ribosomal genes. Appears to cooperate with the WICH chromatin-remodeling complex to facilitate transcription. Necessary for the formation of the first phosphodiester bond during transcription initiation. Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.17 Ref.18 Ref.19
Subunit structure	Interacts (via its IQ motifs) with calmodulin. Interacts with RPS6 and actin By similarity. Interacts (via its IQ motifs) with CABP1 and CIB1; the interaction with CABP1 and CIB1 is calcium-dependent. Interacts (via tail domain) with PLEKHB1 (via PH domain); the interaction is not affected by the presence or absence of calcium and calmodulin. Interacts with POLR1A and POLR2A. Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Ref.2 Ref.14 Ref.16 Ref.17 Ref.21
Subcellular location	Cytoplasm. Cell membrane. Cell projection › stereocilium membrane. Note: Colocalizes with CABP1 and CIB1 at cell margin, membrane ruffles and punctate regions on the cell membrane. Colocalizes in adipocytes with GLUT4 in actin-based membranes. Localizes transiently at cell membrane to region known to be enriched in PIP2. Activation of phospholipase C results in its redistribution to the cytoplasm. Ref.2 Ref.11 Ref.16 Ref.19 Ref.20 Ref.21 Isoform 3: Nucleus › nucleolus. Nucleus › nucleoplasm By similarity. Nucleus › nuclear pore complex By similarity. Note: In the nucleolus, is localized predominantly in dense fibrillar component (DFC) and in granular component (GC). Accumulates strongly in DFC and GC during activation of transcription. Colocalizes with transcription sites. Colocalizes in the granular cortex at the periphery of the nucleolus with RPS6. Colocalizes in nucleoplasm with RPS6 and actin that are in contact with RNP particles. Colocalizes with RPS6 at the nuclear pore level By similarity. Colocalizes with RNA polymerase II in the nucleus. Colocalizes with RNA polymerase I in nucleoli. Ref.2 Ref.11 Ref.16 Ref.19 Ref.20 Ref.21
Tissue specificity	Isoform 3 is expressed in small intestine, pancreas, brain, kidney, skin, heart muscle, testis, striated muscle, spleen, liver and lung (at protein level). Expressed in brain, testis, adrenal glands, thymus, spleen, kidney, lung, heart, cochlea and vestibule. Expressed in sensory hair cells of the inner ear. Expressed in adipocytes. Ref.7 Ref.11 Ref.15 Ref.20
Induction	Up-regulated by serum. Ref.20
Domain	Binds directly to large unilamellar vesicles (LUVs) containing phosphatidylinositol 4,5-bisphosphate (PIP2) or inositol 1,4,5-trisphosphate (InsP3). The PIP2-binding site corresponds to a putative PH domain present in its tail domain.
Post-translational modification	Isoform 2 contains a N-acetylmethionine at position 1 By similarity.
Sequence similarities	Contains 2 IQ domains. Contains 1 myosin head-like domain.
Caution	Represents a unconventional myosin. This protein should not be confused with the conventional myosin-1 (MYH1).

Ontologies

Keywords
Biological process	Protein transport Translocation Transport mRNA transport
Cellular component	Cell membrane Cell projection Cytoplasm Membrane Nuclear pore complex Nucleus
Coding sequence diversity	Alternative splicing
Domain	Repeat
Ligand	ATP-binding Actin-binding Calmodulin-binding Nucleotide-binding
Molecular function	Motor protein Myosin
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW protein transport Inferred from electronic annotation. Source: UniProtKB-KW transport Inferred from direct assay Ref.11. Source: MGI
Cellular_component	basal plasma membrane Inferred from electronic annotation. Source: Compara brush border Inferred from direct assay PubMed 15758024. Source: MGI cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell filamentous actin Inferred from electronic annotation. Source: Compara lateral plasma membrane Inferred from electronic annotation. Source: Compara membrane Traceable author statement Ref.14. Source: UniProtKB myosin I complex Inferred from direct assay Ref.11. Source: MGI nuclear pore Inferred from electronic annotation. Source: UniProtKB-SubCell nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell stereocilium Inferred from direct assay PubMed 17050716. Source: MGI stereocilium membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Non-traceable author statement Ref.14. Source: UniProtKB actin binding Non-traceable author statement Ref.14. Source: UniProtKB calmodulin binding Non-traceable author statement Ref.14. Source: UniProtKB motor activity Inferred from electronic annotation. Source: InterPro phospholipid binding Traceable author statement Ref.14. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Plekhb1	Q9QYE9-1	4	EBI-777558,EBI-1127141
Plekhb1	Q9QYE9-2	2	EBI-777558,EBI-1127145

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9WTI7-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Gene prediction based on EST data.

Isoform 2 (identifier: Q9WTI7-2)

Also known as: A;

The sequence of this isoform differs from the canonical sequence as follows:
     1-35: Missing.

Note: Contains a N-acetylmethionine at position 1 (By similarity).

Isoform 3 (identifier: Q9WTI7-3)

Also known as: Nuclear myosin 1; NM1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MALQVELIPTGEIIRVVHPHRPCKL → MRYRAS

Isoform 4 (identifier: Q9WTI7-4)

Also known as: B;

The sequence of this isoform differs from the canonical sequence as follows:
     932-1063: GYKPRPRQLL...AVVAPRLNSR → VTSLAPGSCCSRPVLWSLWRMLKSSRELIMPT

Note: No experimental confirmation available. May be due to a frameshift.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1063	1063	Unconventional myosin-Ic		PRO_0000123446
Regions
	Domain	36 – 718	683	Myosin head-like
	Domain	734 – 757	24	IQ 1
	Domain	758 – 786	29	IQ 2
	Nucleotide binding	140 – 147	8	ATP Potential
	Region	927 – 938	12	PIP2-binding motif
Amino acid modifications
	Modified residue	383	1	N6-methyllysine By similarity
	Modified residue	408	1	Phosphoserine Ref.22
Natural variations
	Alternative sequence	1 – 35	35	Missing in isoform 2.		VSP_036863
	Alternative sequence	1 – 25	25	MALQV…RPCKL → MRYRAS in isoform 3.		VSP_036864
	Alternative sequence	932 – 1063	132	GYKPR…RLNSR → VTSLAPGSCCSRPVLWSLWR MLKSSRELIMPT in isoform 4.		VSP_003350
Experimental info
	Mutagenesis	927	1	K → A: Inhibits binding to PIP2 and disrupts membrane binding. Ref.18
	Mutagenesis	938	1	R → A: Inhibits binding to PIP2 and disrupts membrane binding. Ref.18
	Sequence conflict	69 – 70	2	RR → GG in CAA67956. Ref.7
	Sequence conflict	97 – 99	3	SRQ → RRK in CAA67956. Ref.7
	Sequence conflict	102	1	E → G in BAE33311. Ref.3
	Sequence conflict	107	1	V → I in BAE33311. Ref.3
	Sequence conflict	251	1	T → A Ref.9
	Sequence conflict	272	1	C → F Ref.9
	Sequence conflict	286 – 287	2	VM → LL Ref.9
	Sequence conflict	388	1	R → A Ref.9
	Sequence conflict	401 – 403	3	LAS → VPA Ref.9
	Sequence conflict	446	1	Q → R Ref.9
	Sequence conflict	517 – 519	3	VKP → IKH Ref.9
	Sequence conflict	578	1	M → T Ref.9
	Sequence conflict	607	1	S → G Ref.9
	Sequence conflict	735	1	Q → R in CAA67956. Ref.7
	Sequence conflict	821	1	R → G in CAA67956. Ref.7
	Sequence conflict	842	1	E → D in CAA67956. Ref.7
	Sequence conflict	1024	1	T → A in BAE33311. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 14, 2009. Version 2. Checksum: 494A31B8634A1AF9	FASTA	1,063	121,944
	10 20 30 40 50 60 MALQVELIPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD FVLLENFTSE 70 80 90 100 110 120 AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH MERYRGVSFY EVPPHLFAVA 130 140 150 160 170 180 DTVYRALRTE RRDQAVMISG ESGAGKTEAT KRLLQFYAET CPAPERGGAV RDRLLQSNPV 190 200 210 220 230 240 LEAFGNAKTL RNDNSSRFGK YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHVF 250 260 270 280 290 300 YQLLEGGEEE TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVMRKA LSVIDFTEDE 310 320 330 340 350 360 VEDLLSIVAS VLHLGNIHFA ADEDSNAQVT TENQLKYLTR LLGVEGTTLR EALTHRKIIA 370 380 390 400 410 420 KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVRKINRS LASKDAESPS WRSTTVLGLL 430 440 450 460 470 480 DIYGFEVFQH NSFEQFCINY CNEKLQQLFI ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC 490 500 510 520 530 540 DLVEEKFKGI ISILDEECLR PGEATDLTFL EKLEDTVKPH PHFLTHKLAD QKTRKSLDRG 550 560 570 580 590 600 EFRLLHYAGE VTYSVTGFLD KNNDLLFRNL KETMCSSMNP IMAQCFDKSE LSDKKRPETV 610 620 630 640 650 660 ATQFKMSLLQ LVEILRSKEP AYIRCIKPND AKQPGRFDEV LIRHQVKYLG LMENLRVRRA 670 680 690 700 710 720 GFAYRRKYEA FLQRYKSLCP ETWPMWAGRP QDGVAVLVRH LGYKPEEYKM GRTKIFIRFP 730 740 750 760 770 780 KTLFATEDSL EVRRQSLATK IQAAWRGFHW RQKFLRVKRS AICIQSWWRG TLGRRKAAKR 790 800 810 820 830 840 KWAAQTIRRL IRGFILRHSP RCPENAFFLD HVRASFLLNL RRQLPRNVLD TSWPTPPPAL 850 860 870 880 890 900 REASELLREL CMKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR 910 920 930 940 950 960 LGTEEISPRV LQSLGSEPIQ YAVPVVKYDR KGYKPRPRQL LLTPSAVVIV EDAKVKQRID 970 980 990 1000 1010 1020 YANLTGISVS SLSDSLFVLH VQREDNKQKG DVVLQSDHVI ETLTKTALSA DRVNNININQ 1030 1040 1050 1060 GSITFAGGPG RDGIIDFTSG SELLITKAKN GHLAVVAPRL NSR
	Isoform 2 (A) [UniParc]. Checksum: 2CF5535D816884DF	FASTA	1,028	118,156
	10 20 30 40 50 60 MESALTARDR VGVQDFVLLE NFTSEAAFIE NLRRRFRENL IYTYIGPVLV SVNPYRDLQI 70 80 90 100 110 120 YSRQHMERYR GVSFYEVPPH LFAVADTVYR ALRTERRDQA VMISGESGAG KTEATKRLLQ 130 140 150 160 170 180 FYAETCPAPE RGGAVRDRLL QSNPVLEAFG NAKTLRNDNS SRFGKYMDVQ FDFKGAPVGG 190 200 210 220 230 240 HILSYLLEKS RVVHQNHGER NFHVFYQLLE GGEEETLRRL GLERNPQSYL YLVKGQCAKV 250 260 270 280 290 300 SSINDKSDWK VMRKALSVID FTEDEVEDLL SIVASVLHLG NIHFAADEDS NAQVTTENQL 310 320 330 340 350 360 KYLTRLLGVE GTTLREALTH RKIIAKGEEL LSPLNLEQAA YARDALAKAV YSRTFTWLVR 370 380 390 400 410 420 KINRSLASKD AESPSWRSTT VLGLLDIYGF EVFQHNSFEQ FCINYCNEKL QQLFIELTLK 430 440 450 460 470 480 SEQEEYEAEG IAWEPVQYFN NKIICDLVEE KFKGIISILD EECLRPGEAT DLTFLEKLED 490 500 510 520 530 540 TVKPHPHFLT HKLADQKTRK SLDRGEFRLL HYAGEVTYSV TGFLDKNNDL LFRNLKETMC 550 560 570 580 590 600 SSMNPIMAQC FDKSELSDKK RPETVATQFK MSLLQLVEIL RSKEPAYIRC IKPNDAKQPG 610 620 630 640 650 660 RFDEVLIRHQ VKYLGLMENL RVRRAGFAYR RKYEAFLQRY KSLCPETWPM WAGRPQDGVA 670 680 690 700 710 720 VLVRHLGYKP EEYKMGRTKI FIRFPKTLFA TEDSLEVRRQ SLATKIQAAW RGFHWRQKFL 730 740 750 760 770 780 RVKRSAICIQ SWWRGTLGRR KAAKRKWAAQ TIRRLIRGFI LRHSPRCPEN AFFLDHVRAS 790 800 810 820 830 840 FLLNLRRQLP RNVLDTSWPT PPPALREASE LLRELCMKNM VWKYCRSISP EWKQQLQQKA 850 860 870 880 890 900 VASEIFKGKK DNYPQSVPRL FISTRLGTEE ISPRVLQSLG SEPIQYAVPV VKYDRKGYKP 910 920 930 940 950 960 RPRQLLLTPS AVVIVEDAKV KQRIDYANLT GISVSSLSDS LFVLHVQRED NKQKGDVVLQ 970 980 990 1000 1010 1020 SDHVIETLTK TALSADRVNN ININQGSITF AGGPGRDGII DFTSGSELLI TKAKNGHLAV VAPRLNSR
	Isoform 3 (Nuclear myosin 1) (NM1) [UniParc]. Checksum: CDAB0FF699D041C9	FASTA	1,044	119,877
	10 20 30 40 50 60 MRYRASALGS DGVRVTMESA LTARDRVGVQ DFVLLENFTS EAAFIENLRR RFRENLIYTY 70 80 90 100 110 120 IGPVLVSVNP YRDLQIYSRQ HMERYRGVSF YEVPPHLFAV ADTVYRALRT ERRDQAVMIS 130 140 150 160 170 180 GESGAGKTEA TKRLLQFYAE TCPAPERGGA VRDRLLQSNP VLEAFGNAKT LRNDNSSRFG 190 200 210 220 230 240 KYMDVQFDFK GAPVGGHILS YLLEKSRVVH QNHGERNFHV FYQLLEGGEE ETLRRLGLER 250 260 270 280 290 300 NPQSYLYLVK GQCAKVSSIN DKSDWKVMRK ALSVIDFTED EVEDLLSIVA SVLHLGNIHF 310 320 330 340 350 360 AADEDSNAQV TTENQLKYLT RLLGVEGTTL REALTHRKII AKGEELLSPL NLEQAAYARD 370 380 390 400 410 420 ALAKAVYSRT FTWLVRKINR SLASKDAESP SWRSTTVLGL LDIYGFEVFQ HNSFEQFCIN 430 440 450 460 470 480 YCNEKLQQLF IELTLKSEQE EYEAEGIAWE PVQYFNNKII CDLVEEKFKG IISILDEECL 490 500 510 520 530 540 RPGEATDLTF LEKLEDTVKP HPHFLTHKLA DQKTRKSLDR GEFRLLHYAG EVTYSVTGFL 550 560 570 580 590 600 DKNNDLLFRN LKETMCSSMN PIMAQCFDKS ELSDKKRPET VATQFKMSLL QLVEILRSKE 610 620 630 640 650 660 PAYIRCIKPN DAKQPGRFDE VLIRHQVKYL GLMENLRVRR AGFAYRRKYE AFLQRYKSLC 670 680 690 700 710 720 PETWPMWAGR PQDGVAVLVR HLGYKPEEYK MGRTKIFIRF PKTLFATEDS LEVRRQSLAT 730 740 750 760 770 780 KIQAAWRGFH WRQKFLRVKR SAICIQSWWR GTLGRRKAAK RKWAAQTIRR LIRGFILRHS 790 800 810 820 830 840 PRCPENAFFL DHVRASFLLN LRRQLPRNVL DTSWPTPPPA LREASELLRE LCMKNMVWKY 850 860 870 880 890 900 CRSISPEWKQ QLQQKAVASE IFKGKKDNYP QSVPRLFIST RLGTEEISPR VLQSLGSEPI 910 920 930 940 950 960 QYAVPVVKYD RKGYKPRPRQ LLLTPSAVVI VEDAKVKQRI DYANLTGISV SSLSDSLFVL 970 980 990 1000 1010 1020 HVQREDNKQK GDVVLQSDHV IETLTKTALS ADRVNNININ QGSITFAGGP GRDGIIDFTS 1030 1040 GSELLITKAK NGHLAVVAPR LNSR
	Isoform 4 (B) [UniParc]. Checksum: C8CEFAE7FADE5B41	FASTA	963	111,290
	10 20 30 40 50 60 MALQVELIPT GEIIRVVHPH RPCKLALGSD GVRVTMESAL TARDRVGVQD FVLLENFTSE 70 80 90 100 110 120 AAFIENLRRR FRENLIYTYI GPVLVSVNPY RDLQIYSRQH MERYRGVSFY EVPPHLFAVA 130 140 150 160 170 180 DTVYRALRTE RRDQAVMISG ESGAGKTEAT KRLLQFYAET CPAPERGGAV RDRLLQSNPV 190 200 210 220 230 240 LEAFGNAKTL RNDNSSRFGK YMDVQFDFKG APVGGHILSY LLEKSRVVHQ NHGERNFHVF 250 260 270 280 290 300 YQLLEGGEEE TLRRLGLERN PQSYLYLVKG QCAKVSSIND KSDWKVMRKA LSVIDFTEDE 310 320 330 340 350 360 VEDLLSIVAS VLHLGNIHFA ADEDSNAQVT TENQLKYLTR LLGVEGTTLR EALTHRKIIA 370 380 390 400 410 420 KGEELLSPLN LEQAAYARDA LAKAVYSRTF TWLVRKINRS LASKDAESPS WRSTTVLGLL 430 440 450 460 470 480 DIYGFEVFQH NSFEQFCINY CNEKLQQLFI ELTLKSEQEE YEAEGIAWEP VQYFNNKIIC 490 500 510 520 530 540 DLVEEKFKGI ISILDEECLR PGEATDLTFL EKLEDTVKPH PHFLTHKLAD QKTRKSLDRG 550 560 570 580 590 600 EFRLLHYAGE VTYSVTGFLD KNNDLLFRNL KETMCSSMNP IMAQCFDKSE LSDKKRPETV 610 620 630 640 650 660 ATQFKMSLLQ LVEILRSKEP AYIRCIKPND AKQPGRFDEV LIRHQVKYLG LMENLRVRRA 670 680 690 700 710 720 GFAYRRKYEA FLQRYKSLCP ETWPMWAGRP QDGVAVLVRH LGYKPEEYKM GRTKIFIRFP 730 740 750 760 770 780 KTLFATEDSL EVRRQSLATK IQAAWRGFHW RQKFLRVKRS AICIQSWWRG TLGRRKAAKR 790 800 810 820 830 840 KWAAQTIRRL IRGFILRHSP RCPENAFFLD HVRASFLLNL RRQLPRNVLD TSWPTPPPAL 850 860 870 880 890 900 REASELLREL CMKNMVWKYC RSISPEWKQQ LQQKAVASEI FKGKKDNYPQ SVPRLFISTR 910 920 930 940 950 960 LGTEEISPRV LQSLGSEPIQ YAVPVVKYDR KVTSLAPGSC CSRPVLWSLW RMLKSSRELI MPT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The vibrator mutation causes neurodegeneration via reduced expression of PITP alpha: positional complementation cloning and extragenic suppression." Hamilton B.A., Smith D.J., Mueller K.L., Kerrebrock A.W., Bronson R.T., van Berkel V., Daly M.J., Kruglyak L., Reeve M.P., Nemhauser J.L., Hawkins T.L., Rubin E.M., Lander E.S. Neuron 18:711-722(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 4). Strain: DBA/2J. Tissue: Brain.
[2]	"A myosin I isoform in the nucleus." Pestic-Dragovich L., Stojiljkovic L., Philimonenko A.A., Nowak G., Ke Y., Settlage R.E., Shabanowitz J., Hunt D.F., Hozak P., de Lanerolle P. Science 290:337-341(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH POLR2A, SUBCELLULAR LOCATION. Tissue: Embryo.
[3]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Strain: C57BL/6J and NOD. Tissue: Lung.
[4]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[5]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: FVB/N. Tissue: Mammary gland.
[7]	"Cloning of the genes encoding two murine and human cochlear unconventional type I myosins." Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P., Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G., Weil D., Pujol R., Petit C. Genomics 40:332-341(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-842 (ISOFORM 2), TISSUE SPECIFICITY. Strain: BALB/c. Tissue: Cochlea.
[8]	Gerhard D.S. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-34 (ISOFORM 1). Tissue: Placenta.
[9]	"Mammalian myosin I alpha, I beta, and I gamma: new widely expressed genes of the myosin I family." Sherr E.H., Joyce M.P., Greene L.A. J. Cell Biol. 120:1405-1416(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 181-628 (ISOFORM 1/2/3/4).
[10]	"A chemical-genetic strategy implicates myosin-1c in adaptation by hair cells." Holt J.R., Gillespie S.K., Provance D.W., Shah K., Shokat K.M., Corey D.P., Mercer J.A., Gillespie P.G. Cell 108:371-381(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[11]	"Glucose transporter recycling in response to insulin is facilitated by myosin Myo1c." Bose A., Guilherme A., Robida S.I., Nicoloro S.M., Zhou Q.L., Jiang Z.Y., Pomerleau D.P., Czech M.P. Nature 420:821-824(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[12]	"Myo1c is designed for the adaptation response in the inner ear." Batters C., Arthur C.P., Lin A., Porter J., Geeves M.A., Milligan R.A., Molloy J.E., Coluccio L.M. EMBO J. 23:1433-1440(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"An actin-myosin complex on actively transcribing genes." Fomproix N., Percipalle P. Exp. Cell Res. 294:140-148(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[14]	"PHR1, an integral membrane protein of the inner ear sensory cells, directly interacts with myosin 1c and myosin VIIa." Etournay R., El-Amraoui A., Bahloul A., Blanchard S., Roux I., Pezeron G., Michalski N., Daviet L., Hardelin J.-P., Legrain P., Petit C. J. Cell Sci. 118:2891-2899(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PLEKHB1.
[15]	"Fast adaptation in vestibular hair cells requires myosin-1c activity." Stauffer E.A., Scarborough J.D., Hirono M., Miller E.D., Shah K., Mercer J.A., Holt J.R., Gillespie P.G. Neuron 47:541-553(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[16]	"The chromatin remodelling complex WSTF-SNF2h interacts with nuclear myosin 1 and has a role in RNA polymerase I transcription." Percipalle P., Fomproix N., Cavellan E., Voit R., Reimer G., Krueger T., Thyberg J., Scheer U., Grummt I., Oestlund Farrants A.-K.O. EMBO Rep. 7:525-530(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BAZ1B, POLR1A AND SMARCA5, SUBCELLULAR LOCATION.
[17]	"Nuclear myosin I is necessary for the formation of the first phosphodiester bond during transcription initiation by RNA polymerase II." Hofmann W.A., Vargas G.M., Ramchandran R., Stojiljkovic L., Goodrich J.A., de Lanerolle P. J. Cell. Biochem. 99:1001-1009(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH POLR2A.
[18]	"Myo1c binds phosphoinositides through a putative pleckstrin homology domain." Hokanson D.E., Laakso J.M., Lin T., Sept D., Ostap E.M. Mol. Biol. Cell 17:4856-4865(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF LYS-927 AND ARG-938.
[19]	"Myo1c binds tightly and specifically to phosphatidylinositol 4,5-bisphosphate and inositol 1,4,5-trisphosphate." Hokanson D.E., Ostap E.M. Proc. Natl. Acad. Sci. U.S.A. 103:3118-3123(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[20]	"Nuclear myosin is ubiquitously expressed and evolutionary conserved in vertebrates." Kahle M., Pridalova J., Spacek M., Dzijak R., Hozak P. Histochem. Cell Biol. 127:139-148(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[21]	"CIB1 and CaBP1 bind to the myo1c regulatory domain." Tang N., Lin T., Yang J., Foskett J.K., Ostap E.M. J. Muscle Res. Cell Motil. 28:285-291(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CABP1 AND CIB1, SUBCELLULAR LOCATION.
[22]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, MASS SPECTROMETRY. Tissue: Macrophage.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U96723 mRNA. Translation: AAC53264.1. U96726 Genomic DNA. Translation: AAC60758.1. AY007255 mRNA. Translation: AAG02570.1. AK004743 mRNA. Translation: BAB23524.1. AK154294 mRNA. Translation: BAE32495.1. AK155530 mRNA. Translation: BAE33311.1. AK171107 mRNA. Translation: BAE42253.1. AL591440 Genomic DNA. Translation: CAI24085.1. AL591440 Genomic DNA. Translation: CAI24086.2. AL591440 Genomic DNA. Translation: CAI24088.2. CH466596 Genomic DNA. Translation: EDL12832.1. CH466596 Genomic DNA. Translation: EDL12833.1. BC021481 mRNA. Translation: AAH21481.1. X99638 mRNA. Translation: CAA67956.1. CF615767 mRNA. No translation available.
IPI	IPI00467172. IPI00620222. IPI00754649. IPI00928288.
PIR	B45438. H75634.
RefSeq	NP_001074243.1. NM_001080774.1. NP_001074244.1. NM_001080775.1. NP_032685.1. NM_008659.3.
UniGene	Mm.234502.
3D structure databases
ProteinModelPortal	Q9WTI7.
SMR	Q9WTI7. Positions 47-732.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9WTI7. 5 interactions.
PTM databases
PhosphoSite	Q9WTI7.
Proteomic databases
PaxDb	Q9WTI7.
PRIDE	Q9WTI7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000069057; ENSMUSP00000070388; ENSMUSG00000017774. ENSMUST00000102504; ENSMUSP00000099562; ENSMUSG00000017774. ENSMUST00000102505; ENSMUSP00000099563; ENSMUSG00000017774. ENSMUST00000108431; ENSMUSP00000104069; ENSMUSG00000017774.
GeneID	17913.
KEGG	mmu:17913.
UCSC	uc007kem.1. mouse. uc007keo.1. mouse.
Organism-specific databases
CTD	4641.
MGI	MGI:106612. Myo1c.
Phylogenomic databases
eggNOG	COG5022.
GeneTree	ENSGT00690000101926.
HOVERGEN	HBG062373.
InParanoid	Q3U231.
KO	K10356.
OMA	WAGRPQD.
OrthoDB	EOG4C5CHM.
Enzyme and pathway databases
Reactome	REACT_147847. Translocation of Glut4 to the Plasma Membrane. REACT_88307. Membrane Trafficking.
Gene expression databases
ArrayExpress	Q9WTI7.
Bgee	Q9WTI7.
CleanEx	MM_MYO1C.
Genevestigator	Q9WTI7.
GermOnline	ENSMUSG00000017774. Mus musculus.
Family and domain databases
InterPro	IPR000048. IQ_motif_EF-hand-BS. IPR001609. Myosin_head_motor_dom. IPR010926. Myosin_tail_2. [Graphical view]
Pfam	PF00612. IQ. 2 hits. PF00063. Myosin_head. 1 hit. PF06017. Myosin_TH1. 1 hit. [Graphical view]
PRINTS	PR00193. MYOSINHEAVY.
SMART	SM00015. IQ. 2 hits. SM00242. MYSc. 1 hit. [Graphical view]
PROSITE	PS50096. IQ. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MYO1C. mouse.
NextBio	292757.
SOURCE	Search...

Entry information

Entry name

MYO1C_MOUSE

Accession

Primary (citable) accession number: Q9WTI7
Secondary accession number(s): O08571 , O08834, Q3TBQ4, Q3U231, Q5ND46, Q5ND48, Q5ND49, Q9ERB6, Q9QW54

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	April 14, 2009
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program