ID MYO1C_AQUCT Reviewed; 1028 AA.
AC Q92002;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=Unconventional myosin-Ic;
DE AltName: Full=Myosin I beta;
DE Short=MMI-beta;
DE Short=MMIb;
DE Short=aMIb;
GN Name=Myo1c;
OS Aquarana catesbeiana (American bullfrog) (Rana catesbeiana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Neobatrachia; Ranoidea; Ranidae; Rana; Aquarana.
OX NCBI_TaxID=8400;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RA Solc C.F., Derfler B.H., Duyk G.M., Corey D.P.;
RT "Molecular cloning of myosins from the bullfrog saccular macula: A
RT candidate for the hair-cell adaptation motor.";
RL Aud. Neurosci. 1:63-75(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7991542; DOI=10.1073/pnas.91.25.11821;
RA Metcalf A.B., Chelliah Y., Hudspeth A.J.;
RT "Molecular cloning of a myosin I beta isozyme that may mediate adaptation
RT by hair cells of the bullfrog's internal ear.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11821-11825(1994).
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=9786971; DOI=10.1523/jneurosci.18-21-08637.1998;
RA Garcia J.A., Yee A.G., Gillespie P.G., Corey D.P.;
RT "Localization of myosin-Ibeta near both ends of tip links in frog saccular
RT hair cells.";
RL J. Neurosci. 18:8637-8647(1998).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails are presumed to bind to membranous compartments, which
CC would be moved relative to actin filaments (By similarity).
CC {ECO:0000250|UniProtKB:Q9WTI7}.
CC -!- SUBUNIT: Interacts (via its IQ motifs) with calmodulin.
CC {ECO:0000250|UniProtKB:O00159}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9786971}. Cell
CC membrane {ECO:0000269|PubMed:9786971}; Peripheral membrane protein
CC {ECO:0000269|PubMed:9786971}; Cytoplasmic side
CC {ECO:0000269|PubMed:9786971}. Cell projection, ruffle membrane
CC {ECO:0000250|UniProtKB:Q9WTI7}. Cytoplasmic vesicle
CC {ECO:0000250|UniProtKB:Q9WTI7}. Cell projection, stereocilium membrane
CC {ECO:0000269|PubMed:9786971}. Note=Detected in stereocilia at the
CC insertions of stereocilia into the apical surface of the cell, near the
CC side plaques of tip links and near the tops of the tip links.
CC {ECO:0000269|PubMed:9786971}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and the sacculus of the internal
CC ear. {ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-1 (MYH1). {ECO:0000305}.
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DR EMBL; U14382; AAA65091.1; -; mRNA.
DR EMBL; U14549; AAA57192.1; -; mRNA.
DR PIR; I51173; I51173.
DR AlphaFoldDB; Q92002; -.
DR SMR; Q92002; -.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060171; C:stereocilium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR PANTHER; PTHR13140:SF255; UNCONVENTIONAL MYOSIN-IC; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50096; IQ; 2.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; ATP-binding; Cell membrane; Cell projection;
KW Cytoplasm; Cytoplasmic vesicle; Membrane; Methylation; Motor protein;
KW Myosin; Nucleotide-binding; Repeat.
FT CHAIN 1..1028
FT /note="Unconventional myosin-Ic"
FT /id="PRO_0000369412"
FT DOMAIN 12..696
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 699..728
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 722..751
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 850..1024
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 573..595
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 104..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 157..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250"
FT MOD_RES 348
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1028 AA; 118831 MW; D15F6F99B68A90AE CRC64;
MESALTARDR VGVQDFVLLE NYTSEAAFIE NLRKRFKENL IYTYIGSVLV SVNPYKELEI
YSKQHMERYR GVSFYEVSPH IYAIADNSYR SLRTERKDQC ILISGESGAG KTEASKKILQ
YYAVTCPVSD QVETVKDRLL QSNPVLEAFG NAKTLRNDNS SRFGKYMDVQ FDYKGAPVGG
HILNYLLEKS RVVHQNHGER NFHIFYQLLE GGEEDLLRRL GLDKNAQNYQ YLIKGQCARV
SSINDKNDWK VVRRALSIIN FNDDDIEELL SIVASVLHLG NVQFATDEHG HAQVTTENQI
KYLARLLSVD STVLRESLIH KKIIAKGEEL NSPLNLEQAA YARDALAKAI YGRTFSWLVS
KINKSLAYKG TDMHKLGSAS VIGLLDIYGF EVFQHNSFEQ FCINFCNEKL QQLFIELTLK
SEQDEYESEG IAWEPVQYFN NKIICDLVEE KFKGIISILD EECLRPGEAT DMTFLEKLED
TVKNHPHFVT HKLGDQKTRK VLGRDEFRLL HYAGEVNYSV AGFLDKNNDL LFRNLKEVMC
DSGNPIAHQC FNRSELTDKK RPETAATQFK NSLSKLMEIL MSKQPSYVRC IKPNDAKQPA
RFDEVLIRHQ VKYLGLIENV RVRRAGFAYR RKYEIFLQRY KSLCPDTWPN WDGRAMDGVA
VLVKSLGYKP EEYKMGRTKI FIRFPKTLFA TEDALEVRKH SIATFLQARW RGYHQRQKFL
HMKHSAVEIQ SWWRGTIGRR KAAKRKWAVD VVRRFIKGFI YRNQPRCTEN EYFLDYIRYS
FLMTLYRNQP KSVLDKSWPV PPPSLREASE LLREMCMNNM VWKYCRRINP EWKQQLEQKV
VASEIFKDKK DNYPQSVPRL FINTRLGNDE INTKILQQLE SQTLTYAVPV VKYDRKGYKP
RRRQLLLTQN AAYLVEEAKM KQRIDYANLT GISVSSLSDN LFVLHVKCED NKQKGDAILQ
SDHVIETLTK VAITAEKINN ININQGSIKF TVGPGKEGII DFTAGSELLI AKAKNGHLSV
VAPRLNSR
//
