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MYO1H_MOUSE
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   03-AUG-2022, entry version 126.
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.ENSMUSP00000132905; -.
DR   iPTMnet; Q9D6A1; -.
DR   PhosphoSitePlus; Q9D6A1; -.
DR   MaxQB; Q9D6A1; -.
DR   PaxDb; Q9D6A1; -.
DR   PRIDE; Q9D6A1; -.
DR   ProteomicsDB; 286103; -. [Q9D6A1-1]
DR   Antibodypedia; 48152; 28 antibodies from 14 providers.
DR   Ensembl; ENSMUST00000124316; ENSMUSP00000118824; ENSMUSG00000066952. [Q9D6A1-1]
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 84 other tissues.
DR   ExpressionAtlas; Q9D6A1; baseline and differential.
DR   GO; GO:0015629; C:actin cytoskeleton; 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: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; 3.40.850.10; -; 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   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; SSF52540; 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
 
 
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