Full text data of MYO1D
MYO1D
(KIAA0727)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Unconventional myosin-Id
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Unconventional myosin-Id
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O94832
ID MYO1D_HUMAN Reviewed; 1006 AA.
AC O94832; A6H8V3; Q8NHP9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-JUN-2003, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Unconventional myosin-Id;
GN Name=MYO1D; Synonyms=KIAA0727;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Yamakawa H., Ohara O.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-1006.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-11; 239-248; 534-544; 791-801 AND 985-994,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Dozynkiewicz M., Norman J.C.;
RL Submitted (MAR-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase
CC activity. Unconventional myosins serve in intracellular movements.
CC Their highly divergent tails are presumed to bind to membranous
CC compartments, which would be moved relative to actin filaments (By
CC similarity).
CC -!- SUBUNIT: Binds calmodulin through its IQ motifs (By similarity).
CC -!- TISSUE SPECIFICITY: Expressed in many tissues. Highest levels in
CC brain, followed by lung and ovary; expression is lowest in spleen.
CC -!- SIMILARITY: Contains 2 IQ domains.
CC -!- SIMILARITY: Contains 1 myosin head-like domain.
CC -!- CAUTION: Represents a unconventional myosin. This protein should
CC not be confused with the conventional myosin-1 (MYH1).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34447.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB018270; BAA34447.2; ALT_INIT; mRNA.
DR EMBL; BC146763; AAI46764.1; -; mRNA.
DR RefSeq; NP_056009.1; NM_015194.1.
DR UniGene; Hs.602063; -.
DR ProteinModelPortal; O94832; -.
DR SMR; O94832; 10-736.
DR IntAct; O94832; 8.
DR MINT; MINT-4999277; -.
DR STRING; 9606.ENSP00000324527; -.
DR PhosphoSite; O94832; -.
DR PaxDb; O94832; -.
DR PeptideAtlas; O94832; -.
DR PRIDE; O94832; -.
DR Ensembl; ENST00000318217; ENSP00000324527; ENSG00000176658.
DR GeneID; 4642; -.
DR KEGG; hsa:4642; -.
DR UCSC; uc002hho.1; human.
DR CTD; 4642; -.
DR GeneCards; GC17M030819; -.
DR HGNC; HGNC:7598; MYO1D.
DR HPA; HPA054744; -.
DR MIM; 606539; gene.
DR neXtProt; NX_O94832; -.
DR PharmGKB; PA31400; -.
DR eggNOG; COG5022; -.
DR HOGENOM; HOG000260264; -.
DR HOVERGEN; HBG062373; -.
DR InParanoid; O94832; -.
DR KO; K10356; -.
DR OMA; ILDDACM; -.
DR OrthoDB; EOG7V49XQ; -.
DR PhylomeDB; O94832; -.
DR ChiTaRS; MYO1D; human.
DR GenomeRNAi; 4642; -.
DR NextBio; 17888; -.
DR PRO; PR:O94832; -.
DR ArrayExpress; O94832; -.
DR Bgee; O94832; -.
DR CleanEx; HS_MYO1D; -.
DR Genevestigator; O94832; -.
DR GO; GO:0030673; C:axolemma; IEA:Ensembl.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0030898; F:actin-dependent ATPase activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:Ensembl.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_tail_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
KW Complete proteome; Direct protein sequencing; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1006 Unconventional myosin-Id.
FT /FTId=PRO_0000123447.
FT DOMAIN 2 682 Myosin head-like.
FT DOMAIN 699 719 IQ 1.
FT DOMAIN 721 741 IQ 2.
FT NP_BIND 102 109 ATP (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 200 200 Phosphoserine.
FT MOD_RES 536 536 Phosphotyrosine (By similarity).
FT VARIANT 765 765 P -> S (in dbSNP:rs7209106).
FT /FTId=VAR_050210.
FT VARIANT 771 771 R -> H (in dbSNP:rs7215958).
FT /FTId=VAR_050211.
SQ SEQUENCE 1006 AA; 116202 MW; A8BB08450887168E CRC64;
MAEQESLEFG KADFVLMDTV SMPEFMANLR LRFEKGRIYT FIGEVVVSVN PYKLLNIYGR
DTIEQYKGRE LYERPPHLFA IADAAYKAMK RRSKDTCIVI SGESGAGKTE ASKYIMQYIA
AITNPSQRAE VERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH
INNYLLEKSR VIVQQPGERS FHSFYQLLQG GSEQMLRSLH LQKSLSSYNY IHVGAQLKSS
INDAAEFRVV ADAMKVIGFK PEEIQTVYKI LAAILHLGNL KFVVDGDTPL IENGKVVSII
AELLSTKTDM VEKALLYRTV ATGRDIIDKQ HTEQEASYGR DAFAKAIYER LFCWIVTRIN
DIIEVKNYDT TIHGKNTVIG VLDIYGFEIF DNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ
EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIIAILDDAC MNVGKVTDEM FLEALNSKLG
KHAHFSSRKL CASDKILEFD RDFRIRHYAG DVVYSVIGFI DKNKDTLFQD FKRLMYNSSN
PVLKNMWPEG KLSITEVTKR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNDKKSPQI
FDDERCRHQV EYLGLLENVR VRRAGFAFRQ TYEKFLHRYK MISEFTWPNH DLPSDKEAVK
KLIERCGFQD DVAYGKTKIF IRTPRTLFTL EELRAQMLIR IVLFLQKVWR GTLARMRYKR
TKAALTIIRY YRRYKVKSYI HEVARRFHGV KTMRDYGKHV KWPSPPKVLR RFEEALQTIF
NRWRASQLIK SIPASDLPQV RAKVAAVEML KGQRADLGLQ RAWEGNYLAS KPDTPQTSGT
FVPVANELKR KDKYMNVLFS CHVRKVNRFS KVEDRAIFVT DRHLYKMDPT KQYKVMKTIP
LYNLTGLSVS NGKDQLVVFH TKDNKDLIVC LFSKQPTHES RIGELVGVLV NHFKSEKRHL
QVNVTNPVQC SLHGKKCTVS VETRLNQPQP DFTKNRSGFI LSVPGN
//
ID MYO1D_HUMAN Reviewed; 1006 AA.
AC O94832; A6H8V3; Q8NHP9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-JUN-2003, sequence version 2.
DT 22-JAN-2014, entry version 116.
DE RecName: Full=Unconventional myosin-Id;
GN Name=MYO1D; Synonyms=KIAA0727;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Yamakawa H., Ohara O.;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 333-1006.
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-11; 239-248; 534-544; 791-801 AND 985-994,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Dozynkiewicz M., Norman J.C.;
RL Submitted (MAR-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase
CC activity. Unconventional myosins serve in intracellular movements.
CC Their highly divergent tails are presumed to bind to membranous
CC compartments, which would be moved relative to actin filaments (By
CC similarity).
CC -!- SUBUNIT: Binds calmodulin through its IQ motifs (By similarity).
CC -!- TISSUE SPECIFICITY: Expressed in many tissues. Highest levels in
CC brain, followed by lung and ovary; expression is lowest in spleen.
CC -!- SIMILARITY: Contains 2 IQ domains.
CC -!- SIMILARITY: Contains 1 myosin head-like domain.
CC -!- CAUTION: Represents a unconventional myosin. This protein should
CC not be confused with the conventional myosin-1 (MYH1).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34447.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB018270; BAA34447.2; ALT_INIT; mRNA.
DR EMBL; BC146763; AAI46764.1; -; mRNA.
DR RefSeq; NP_056009.1; NM_015194.1.
DR UniGene; Hs.602063; -.
DR ProteinModelPortal; O94832; -.
DR SMR; O94832; 10-736.
DR IntAct; O94832; 8.
DR MINT; MINT-4999277; -.
DR STRING; 9606.ENSP00000324527; -.
DR PhosphoSite; O94832; -.
DR PaxDb; O94832; -.
DR PeptideAtlas; O94832; -.
DR PRIDE; O94832; -.
DR Ensembl; ENST00000318217; ENSP00000324527; ENSG00000176658.
DR GeneID; 4642; -.
DR KEGG; hsa:4642; -.
DR UCSC; uc002hho.1; human.
DR CTD; 4642; -.
DR GeneCards; GC17M030819; -.
DR HGNC; HGNC:7598; MYO1D.
DR HPA; HPA054744; -.
DR MIM; 606539; gene.
DR neXtProt; NX_O94832; -.
DR PharmGKB; PA31400; -.
DR eggNOG; COG5022; -.
DR HOGENOM; HOG000260264; -.
DR HOVERGEN; HBG062373; -.
DR InParanoid; O94832; -.
DR KO; K10356; -.
DR OMA; ILDDACM; -.
DR OrthoDB; EOG7V49XQ; -.
DR PhylomeDB; O94832; -.
DR ChiTaRS; MYO1D; human.
DR GenomeRNAi; 4642; -.
DR NextBio; 17888; -.
DR PRO; PR:O94832; -.
DR ArrayExpress; O94832; -.
DR Bgee; O94832; -.
DR CleanEx; HS_MYO1D; -.
DR Genevestigator; O94832; -.
DR GO; GO:0030673; C:axolemma; IEA:Ensembl.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005790; C:smooth endoplasmic reticulum; IEA:Ensembl.
DR GO; GO:0030898; F:actin-dependent ATPase activity; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:Ensembl.
DR GO; GO:0010923; P:negative regulation of phosphatase activity; IDA:UniProtKB.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_tail_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00612; IQ; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
KW Complete proteome; Direct protein sequencing; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome;
KW Repeat.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 1006 Unconventional myosin-Id.
FT /FTId=PRO_0000123447.
FT DOMAIN 2 682 Myosin head-like.
FT DOMAIN 699 719 IQ 1.
FT DOMAIN 721 741 IQ 2.
FT NP_BIND 102 109 ATP (Potential).
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 200 200 Phosphoserine.
FT MOD_RES 536 536 Phosphotyrosine (By similarity).
FT VARIANT 765 765 P -> S (in dbSNP:rs7209106).
FT /FTId=VAR_050210.
FT VARIANT 771 771 R -> H (in dbSNP:rs7215958).
FT /FTId=VAR_050211.
SQ SEQUENCE 1006 AA; 116202 MW; A8BB08450887168E CRC64;
MAEQESLEFG KADFVLMDTV SMPEFMANLR LRFEKGRIYT FIGEVVVSVN PYKLLNIYGR
DTIEQYKGRE LYERPPHLFA IADAAYKAMK RRSKDTCIVI SGESGAGKTE ASKYIMQYIA
AITNPSQRAE VERVKNMLLK SNCVLEAFGN AKTNRNDNSS RFGKYMDINF DFKGDPIGGH
INNYLLEKSR VIVQQPGERS FHSFYQLLQG GSEQMLRSLH LQKSLSSYNY IHVGAQLKSS
INDAAEFRVV ADAMKVIGFK PEEIQTVYKI LAAILHLGNL KFVVDGDTPL IENGKVVSII
AELLSTKTDM VEKALLYRTV ATGRDIIDKQ HTEQEASYGR DAFAKAIYER LFCWIVTRIN
DIIEVKNYDT TIHGKNTVIG VLDIYGFEIF DNNSFEQFCI NYCNEKLQQL FIQLVLKQEQ
EEYQREGIPW KHIDYFNNQI IVDLVEQQHK GIIAILDDAC MNVGKVTDEM FLEALNSKLG
KHAHFSSRKL CASDKILEFD RDFRIRHYAG DVVYSVIGFI DKNKDTLFQD FKRLMYNSSN
PVLKNMWPEG KLSITEVTKR PLTAATLFKN SMIALVDNLA SKEPYYVRCI KPNDKKSPQI
FDDERCRHQV EYLGLLENVR VRRAGFAFRQ TYEKFLHRYK MISEFTWPNH DLPSDKEAVK
KLIERCGFQD DVAYGKTKIF IRTPRTLFTL EELRAQMLIR IVLFLQKVWR GTLARMRYKR
TKAALTIIRY YRRYKVKSYI HEVARRFHGV KTMRDYGKHV KWPSPPKVLR RFEEALQTIF
NRWRASQLIK SIPASDLPQV RAKVAAVEML KGQRADLGLQ RAWEGNYLAS KPDTPQTSGT
FVPVANELKR KDKYMNVLFS CHVRKVNRFS KVEDRAIFVT DRHLYKMDPT KQYKVMKTIP
LYNLTGLSVS NGKDQLVVFH TKDNKDLIVC LFSKQPTHES RIGELVGVLV NHFKSEKRHL
QVNVTNPVQC SLHGKKCTVS VETRLNQPQP DFTKNRSGFI LSVPGN
//
MIM
606539
*RECORD*
*FIELD* NO
606539
*FIELD* TI
*606539 MYOSIN ID; MYO1D
;;KIAA0727
*FIELD* TX
Myosins are molecular motors that, upon interaction with actin
read morefilaments, utilize energy from ATP hydrolysis to generate mechanical
force. For further background information on myosins, see MYO1A
(601478).
CLONING
By screening for cDNAs with the potential to encode large proteins
expressed in brain, Nagase et al. (1998) identified a cDNA encoding
MYO1D, which they called KIAA0727. The deduced 674-amino acid protein is
98% identical to rat Myr4. RT-PCR analysis detected expression of
KIAA0727 in all tissues tested, with highest levels in brain, followed
by lung and ovary; expression was lowest in spleen.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the MYO1D gene
to chromosome 17. Hasson et al. (1996) mapped the mouse gene to
chromosome 11 by interspecific backcross analysis and predicted a
localization of 17q11-q12 in human.
ANIMAL MODEL
Hozumi et al. (2006) found that handedness of the embryonic gut and the
adult gut and testes is reversed (not randomized) in viable and fertile
homozygous Myo31DF Drosophila mutants. Myo31DF encodes an unconventional
myosin, Drosophila MyoIA (also referred to as MYO1D in mammals), and is
the first actin-based motor protein to be implicated in left-right
patterning. Hozumi et al. (2006) found that Myo31DF is required in the
hindgut epithelium for normal embryonic handedness. Disruption of actin
filaments in hindgut epithelium randomizes the handedness of the
embryonic gut, suggesting that Myo31DF function requires the actin
cytoskeleton. Consistent with this, Hozumi et al. (2006) found that
Myo31DF colocalizes with the cytoskeleton. Overexpression of Myo61F,
another myosin I, reversed the handedness of the embryonic gut, and its
knockdown also caused a left-right patterning defect. Hozumi et al.
(2006) suggested that these 2 unconventional myosin I proteins may have
antagonistic functions in left-right patterning. They suggested that the
actin cytoskeleton and myosin I proteins may be crucial for generating
left-right asymmetry in invertebrates.
Speder et al. (2006) identified the conserved Myo31DF gene in Drosophila
as a unique situs inversus locus. Myo31DF mutations reversed the dextral
looping of genitalia, a prominent left-right marker in adult flies.
Genetic mosaic analysis pinpointed the A8 segment of the genital disc as
a left-right organizer and revealed an anterior-posterior
compartmentalization of Myo31DF function that directs dextral
development and represses a sinistral default state. As expected of a
determinant, Myo31DF has a trigger-like function and is expressed
symmetrically in the organizer, and its symmetrical overexpression does
not impair left-right asymmetry. Thus, Speder et al. (2006) concluded
that Myo31DF is a dextral gene with actin-based motor activity
controlling situs choice. Like mouse inversin, Myo31DF interacts and
colocalizes with beta-catenin, suggesting that situs inversus genes can
direct left-right development through the adherens junction.
*FIELD* RF
1. Hasson, T.; Skowron, J. F.; Gilbert, D. J.; Avraham, K. B.; Perry,
W. L.; Bement, W. M.; Anderson, B. L.; Sherr, E. H.; Chen, Z.-Y.;
Greene, L. A.; Ward, D. C.; Corey, D. P.; Mooseker, M. S.; Copeland,
N. G.; Jenkins, N. A.: Mapping of unconventional myosins in mouse
and human. Genomics 36: 431-439, 1996.
2. Hozumi, S.; Maeda, R.; Taniguchi, K.; Kanai, M.; Shirakabe, S.;
Sasamura, T.; Speder, P.; Noselli, S.; Aigaki, T.; Murakami, R.; Matsuno,
K.: An unconventional myosin in Drosophila reverses the default handedness
in visceral organs. Nature 440: 798-802, 2006.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XI. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 5: 277-286, 1998.
4. Speder, P.; Adam, G.; Noselli, S.: Type ID unconventional myosin
controls left-right asymmetry in Drosophila. Nature 440: 803-807,
2006.
*FIELD* CN
Ada Hamosh - updated: 6/1/2006
*FIELD* CD
Paul J. Converse: 12/7/2001
*FIELD* ED
alopez: 06/05/2006
terry: 6/1/2006
mgross: 12/7/2001
*RECORD*
*FIELD* NO
606539
*FIELD* TI
*606539 MYOSIN ID; MYO1D
;;KIAA0727
*FIELD* TX
Myosins are molecular motors that, upon interaction with actin
read morefilaments, utilize energy from ATP hydrolysis to generate mechanical
force. For further background information on myosins, see MYO1A
(601478).
CLONING
By screening for cDNAs with the potential to encode large proteins
expressed in brain, Nagase et al. (1998) identified a cDNA encoding
MYO1D, which they called KIAA0727. The deduced 674-amino acid protein is
98% identical to rat Myr4. RT-PCR analysis detected expression of
KIAA0727 in all tissues tested, with highest levels in brain, followed
by lung and ovary; expression was lowest in spleen.
MAPPING
By radiation hybrid analysis, Nagase et al. (1998) mapped the MYO1D gene
to chromosome 17. Hasson et al. (1996) mapped the mouse gene to
chromosome 11 by interspecific backcross analysis and predicted a
localization of 17q11-q12 in human.
ANIMAL MODEL
Hozumi et al. (2006) found that handedness of the embryonic gut and the
adult gut and testes is reversed (not randomized) in viable and fertile
homozygous Myo31DF Drosophila mutants. Myo31DF encodes an unconventional
myosin, Drosophila MyoIA (also referred to as MYO1D in mammals), and is
the first actin-based motor protein to be implicated in left-right
patterning. Hozumi et al. (2006) found that Myo31DF is required in the
hindgut epithelium for normal embryonic handedness. Disruption of actin
filaments in hindgut epithelium randomizes the handedness of the
embryonic gut, suggesting that Myo31DF function requires the actin
cytoskeleton. Consistent with this, Hozumi et al. (2006) found that
Myo31DF colocalizes with the cytoskeleton. Overexpression of Myo61F,
another myosin I, reversed the handedness of the embryonic gut, and its
knockdown also caused a left-right patterning defect. Hozumi et al.
(2006) suggested that these 2 unconventional myosin I proteins may have
antagonistic functions in left-right patterning. They suggested that the
actin cytoskeleton and myosin I proteins may be crucial for generating
left-right asymmetry in invertebrates.
Speder et al. (2006) identified the conserved Myo31DF gene in Drosophila
as a unique situs inversus locus. Myo31DF mutations reversed the dextral
looping of genitalia, a prominent left-right marker in adult flies.
Genetic mosaic analysis pinpointed the A8 segment of the genital disc as
a left-right organizer and revealed an anterior-posterior
compartmentalization of Myo31DF function that directs dextral
development and represses a sinistral default state. As expected of a
determinant, Myo31DF has a trigger-like function and is expressed
symmetrically in the organizer, and its symmetrical overexpression does
not impair left-right asymmetry. Thus, Speder et al. (2006) concluded
that Myo31DF is a dextral gene with actin-based motor activity
controlling situs choice. Like mouse inversin, Myo31DF interacts and
colocalizes with beta-catenin, suggesting that situs inversus genes can
direct left-right development through the adherens junction.
*FIELD* RF
1. Hasson, T.; Skowron, J. F.; Gilbert, D. J.; Avraham, K. B.; Perry,
W. L.; Bement, W. M.; Anderson, B. L.; Sherr, E. H.; Chen, Z.-Y.;
Greene, L. A.; Ward, D. C.; Corey, D. P.; Mooseker, M. S.; Copeland,
N. G.; Jenkins, N. A.: Mapping of unconventional myosins in mouse
and human. Genomics 36: 431-439, 1996.
2. Hozumi, S.; Maeda, R.; Taniguchi, K.; Kanai, M.; Shirakabe, S.;
Sasamura, T.; Speder, P.; Noselli, S.; Aigaki, T.; Murakami, R.; Matsuno,
K.: An unconventional myosin in Drosophila reverses the default handedness
in visceral organs. Nature 440: 798-802, 2006.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XI. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 5: 277-286, 1998.
4. Speder, P.; Adam, G.; Noselli, S.: Type ID unconventional myosin
controls left-right asymmetry in Drosophila. Nature 440: 803-807,
2006.
*FIELD* CN
Ada Hamosh - updated: 6/1/2006
*FIELD* CD
Paul J. Converse: 12/7/2001
*FIELD* ED
alopez: 06/05/2006
terry: 6/1/2006
mgross: 12/7/2001