ID MYO1H_MOUSE Reviewed; 958 AA.
AC Q9D6A1; Q91ZI2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 24-JAN-2024, entry version 134.
DE RecName: Full=Unconventional myosin-Ih;
GN Name=Myo1h;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-902 (ISOFORM 2), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12486594; DOI=10.1007/s101620020049;
RA Dumont R.A., Zhao Y.-D., Holt J.R., Baehler M., Gillespie P.G.;
RT "Myosin-I isozymes in neonatal rodent auditory and vestibular epithelia.";
RL J. Assoc. Res. Otolaryngol. 3:375-389(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=28779001; DOI=10.1136/jmedgenet-2017-104765;
RA Spielmann M., Hernandez-Miranda L.R., Ceccherini I., Weese-Mayer D.E.,
RA Kragesteen B.K., Harabula I., Krawitz P., Birchmeier C., Leonard N.,
RA Mundlos S.;
RT "Mutations in MYO1H cause a recessive form of central hypoventilation with
RT autonomic dysfunction.";
RL J. Med. Genet. 54:754-761(2017).
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}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D6A1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D6A1-2; Sequence=VSP_033495, VSP_033496;
CC -!- TISSUE SPECIFICITY: Highly expressed in the central nervous system,
CC including the forebrain, midbrain and lower medulla. In the lower
CC medulla, it is broadly expressed throughout the reticular formation. It
CC is expressed in the retrotrapezoid nucleus and the nucleus of the
CC solitary tract, as well as motor neurons of the facial, vagal and
CC ambiguus nuclei (PubMed:28779001). Expressed in neonatal inner-ear
CC organs. {ECO:0000269|PubMed:12486594, ECO:0000269|PubMed:28779001}.
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; AK014505; BAB29403.1; -; mRNA.
DR EMBL; AC127255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF426467; AAL26547.1; -; mRNA.
DR AlphaFoldDB; Q9D6A1; -.
DR SMR; Q9D6A1; -.
DR STRING; 10090.ENSMUSP00000144110; -.
DR iPTMnet; Q9D6A1; -.
DR PhosphoSitePlus; Q9D6A1; -.
DR MaxQB; Q9D6A1; -.
DR PaxDb; 10090-ENSMUSP00000132905; -.
DR ProteomicsDB; 286103; -. [Q9D6A1-1]
DR Antibodypedia; 48152; 53 antibodies from 14 providers.
DR Ensembl; ENSMUST00000124316.8; ENSMUSP00000118824.3; ENSMUSG00000066952.12. [Q9D6A1-1]
DR AGR; MGI:1914674; -.
DR MGI; MGI:1914674; Myo1h.
DR VEuPathDB; HostDB:ENSMUSG00000066952; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000156430; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; Q9D6A1; -.
DR PhylomeDB; Q9D6A1; -.
DR ChiTaRS; Myo1h; mouse.
DR PRO; PR:Q9D6A1; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9D6A1; Protein.
DR Bgee; ENSMUSG00000066952; Expressed in ascending aorta and 86 other cell types or tissues.
DR ExpressionAtlas; Q9D6A1; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 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:SF353; UNCONVENTIONAL MYOSIN-IH; 1.
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 Actin-binding; Alternative splicing; ATP-binding; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..958
FT /note="Unconventional myosin-Ih"
FT /id="PRO_0000333236"
FT DOMAIN 12..691
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 694..716
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 717..746
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 773..955
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 568..590
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 105..112
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N1T3"
FT VAR_SEQ 1..809
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12486594,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033495"
FT VAR_SEQ 862..958
FT /note="GVSTSSLSDGILVIHISPADKQQKGDVILQCEHIFEVATKLAMLIRKEHTVR
FT VVQGSLQFYVSPGREGTIVFETGEEDQVYKDKNGQLRVVSAGKKT -> DESNINPKVL
FT QLLGSEKIQYGVPVIKYDRKGFKARQRQLLLTQRSAYLVELSKVKQKIEYAAVRGVSTS
FT SLSDGILVIHISPADKQQKVTTASGHKSSLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12486594,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033496"
SQ SEQUENCE 958 AA; 109993 MW; 7DD587A3F6EB5DFE CRC64;
MEGALTARDK VGVQDFVLLD AYTSESAFLE NLRKRFRENL IYTYIGTLLV SVNPYQELGI
YTASQMELYQ GVNFFELPPH VYAIADNAYR MMCSELNNHF ILISGESGAG KTEASKKILQ
YFAVTCPMTE SLQIARDRLL LSIPVLEAFG NAKTLRNDNS SRFGKYMDIQ FDFQGVPVGG
HIISYLIEKS RVVYQNHGER NFHIFYQLLA GGGSERLASL GLERDPQLYK YLSQGHCARE
SPISDKNDWE TVCGAFSVIG FTEADLENLF GIIASVLHLG NVCFKGDKQG CASVPDTHEI
KWIAKLLGVC PAVLLEALTH RKIEAKTEEV ICPLTVELSV YARDAMAKAV YGRTFTWLVN
RINSSLVNKD FTQKTVIGLL DIYGFEVFDK NGFEQFCINY CNEKLQQLLI ERTLKAEQAE
YESEGIEWET VQYFNNKIIC DLVEERHRGI ISILDEECIR PGPATDLSFL EKLEEKVGKH
AHFQTRKLAG PKGRKRIGWL EFCLLHYAGE VTYCTKGFLE KNNDLLYRHL KEVLCSSKNS
ILRECFLVAE LENRRRPPTV GTQFKNSLSS LLEILISKEP SYIRCIKPNE RKEPSKFDDF
LISHQIKYLG LMEHLRVRRA GFAYRRKYEH FLQRYKSLCP DTWPHWHGPP GEGVERLIKY
IGYQPQDYKL GKTKIFIRFP RTLFATEDAF EFSKHQLVSR IQATYKGCLG RREYMKKRQA
ATKLEAHWRG VLARKEIKRR RWAVQIIRRF VKGFINRDKP LCPDNEEFVV LVRKNYILNL
RYHVPKNVLD KSWLRPPGIL ENASNLLRRM CTRNLVRKYC RGISAERKAM MQQKVVTSEI
FRGKKEGYAE SLNQLFAGSR LGVSTSSLSD GILVIHISPA DKQQKGDVIL QCEHIFEVAT
KLAMLIRKEH TVRVVQGSLQ FYVSPGREGT IVFETGEEDQ VYKDKNGQLR VVSAGKKT
//
