MYO1G_MOUSE
ID MYO1G_MOUSE Reviewed; 1024 AA.
AC Q5SUA5; Q8BIT8; Q8BJ17; Q8BJ65; Q8R019; Q91ZI1;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Unconventional myosin-Ig;
GN Name=Myo1g;
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].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
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 [LARGE SCALE MRNA] OF 537-1024.
RC STRAIN=C57BL/6J; TISSUE=Thymus;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 869-994.
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20071333; DOI=10.1074/jbc.m109.086959;
RA Patino-Lopez G., Aravind L., Dong X., Kruhlak M.J., Ostap E.M., Shaw S.;
RT "Myosin 1G is an abundant class I myosin in lymphocytes whose localization
RT at the plasma membrane depends on its ancient divergent pleckstrin homology
RT (PH) domain (Myo1PH).";
RL J. Biol. Chem. 285:8675-8686(2010).
RN [7]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-111 AND
RP ARG-167.
RX PubMed=19968988; DOI=10.1016/j.febslet.2009.11.096;
RA Olety B., Walte M., Honnert U., Schillers H., Bahler M.;
RT "Myosin 1G (Myo1G) is a haematopoietic specific myosin that localises to
RT the plasma membrane and regulates cell elasticity.";
RL FEBS Lett. 584:493-499(2010).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF LYS-883 AND
RP ARG-893.
RX PubMed=23038771; DOI=10.1242/jcs.109561;
RA Dart A.E., Tollis S., Bright M.D., Frankel G., Endres R.G.;
RT "The motor protein myosin 1G functions in FcgammaR-mediated phagocytosis.";
RL J. Cell Sci. 125:6020-6029(2012).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25083865; DOI=10.1016/j.cell.2014.05.044;
RA Gerard A., Patino-Lopez G., Beemiller P., Nambiar R., Ben-Aissa K., Liu Y.,
RA Totah F.J., Tyska M.J., Shaw S., Krummel M.F.;
RT "Detection of rare antigen-presenting cells through T cell-intrinsic
RT meandering motility, mediated by Myo1g.";
RL Cell 158:492-505(2014).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24310084; DOI=10.1002/eji.201343873;
RA Maravillas-Montero J.L., Lopez-Ortega O., Patino-Lopez G.,
RA Santos-Argumedo L.;
RT "Myosin 1g regulates cytoskeleton plasticity, cell migration, exocytosis,
RT and endocytosis in B lymphocytes.";
RL Eur. J. Immunol. 44:877-886(2014).
CC -!- FUNCTION: Unconventional myosin required during immune response for
CC detection of rare antigen-presenting cells by regulating T-cell
CC migration (PubMed:25083865). Unconventional myosins are actin-based
CC motor molecules with ATPase activity and serve in intracellular
CC movements. Acts as a regulator of T-cell migration by generating
CC membrane tension, enforcing cell-intrinsic meandering search, thereby
CC enhancing detection of rare antigens during lymph-node surveillance,
CC enabling pathogen eradication (PubMed:25083865). Also required in B-
CC cells, where it regulates different membrane/cytoskeleton-dependent
CC processes (PubMed:24310084). Involved in Fc-gamma receptor (Fc-gamma-R)
CC phagocytosis (PubMed:23038771). {ECO:0000269|PubMed:23038771,
CC ECO:0000269|PubMed:24310084, ECO:0000269|PubMed:25083865}.
CC -!- SUBUNIT: Interacts with calmodulin; via its IQ motifs. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19968988,
CC ECO:0000269|PubMed:20071333, ECO:0000269|PubMed:24310084,
CC ECO:0000269|PubMed:25083865}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333,
CC ECO:0000269|PubMed:24310084, ECO:0000269|PubMed:25083865}. Cell
CC projection, phagocytic cup {ECO:0000269|PubMed:23038771}.
CC Note=Recruited to Fc-gamma receptor (Fc-gamma-R) phagocytic cup
CC (PubMed:23038771). In T-cells, transiently accumulates in discrete
CC areas at the plasma membrane of migrating cells or when membranes are
CC deformed (PubMed:25083865). {ECO:0000269|PubMed:23038771,
CC ECO:0000269|PubMed:25083865}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells.
CC Detected in adult tissues of the immune system such as thymus, lymph
CC nodes and spleen, but not in brain, lung, heart, liver, small
CC intestine, testis and kidney (at protein level). Highly expressed in T-
CC lymphocytes; constitutes the most highly expressed class I myosin in
CC naive CD4 and CD8 T-cells. Also present in B-lymphocytes.
CC {ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333,
CC ECO:0000269|PubMed:24310084, ECO:0000269|PubMed:25083865}.
CC -!- DOMAIN: The myosin tail domain mediates binding to
CC phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2),
CC phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) and
CC phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) and binds to
CC membranous compartments. It is required for recruitment to Fc-gamma
CC receptor (Fc-gamma-R) phagocytic cups. {ECO:0000269|PubMed:23038771}.
CC -!- DISRUPTION PHENOTYPE: T-cells display impaired migration patterns and
CC are less efficient in scanning and evaluating antigen-presenting cells.
CC T-cells show global reduction in membrane tension, while their
CC homeostatic tissue distribution and responsiveness to T-cell receptor
CC (TCR) engagement are unaffected. However, T-cells move faster and
CC straighter, leading to defects in detection of antigen-presenting
CC cells, specifically for detection of rare antigens.
CC {ECO:0000269|PubMed:25083865}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-7 is the initiator.
CC {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-1 (MYH1). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC31139.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK030825; BAC27149.1; -; mRNA.
DR EMBL; AK042033; BAC31139.1; ALT_FRAME; mRNA.
DR EMBL; AK088011; BAC40093.1; -; mRNA.
DR EMBL; AL646047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028661; AAH28661.1; -; mRNA.
DR EMBL; AF426468; AAL26548.1; -; mRNA.
DR CCDS; CCDS24421.1; -.
DR RefSeq; NP_848534.2; NM_178440.4.
DR AlphaFoldDB; Q5SUA5; -.
DR SMR; Q5SUA5; -.
DR BioGRID; 232896; 8.
DR IntAct; Q5SUA5; 3.
DR MINT; Q5SUA5; -.
DR STRING; 10090.ENSMUSP00000003459; -.
DR iPTMnet; Q5SUA5; -.
DR PhosphoSitePlus; Q5SUA5; -.
DR EPD; Q5SUA5; -.
DR MaxQB; Q5SUA5; -.
DR PaxDb; Q5SUA5; -.
DR PeptideAtlas; Q5SUA5; -.
DR PRIDE; Q5SUA5; -.
DR ProteomicsDB; 287584; -.
DR Antibodypedia; 13492; 77 antibodies from 15 providers.
DR DNASU; 246177; -.
DR Ensembl; ENSMUST00000003459; ENSMUSP00000003459; ENSMUSG00000020437.
DR GeneID; 246177; -.
DR KEGG; mmu:246177; -.
DR UCSC; uc007hyt.2; mouse.
DR CTD; 64005; -.
DR MGI; MGI:1927091; Myo1g.
DR VEuPathDB; HostDB:ENSMUSG00000020437; -.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000158053; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; Q5SUA5; -.
DR OMA; NGIMEAR; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; Q5SUA5; -.
DR TreeFam; TF312960; -.
DR BioGRID-ORCS; 246177; 4 hits in 72 CRISPR screens.
DR PRO; PR:Q5SUA5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SUA5; protein.
DR Bgee; ENSMUSG00000020437; Expressed in granulocyte and 73 other tissues.
DR ExpressionAtlas; Q5SUA5; baseline and differential.
DR Genevisible; Q5SUA5; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0030175; C:filopodium; IDA:MGI.
DR GO; GO:0030027; C:lamellipodium; IDA:MGI.
DR GO; GO:0031256; C:leading edge membrane; IDA:MGI.
DR GO; GO:0005902; C:microvillus; IDA:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0001891; C:phagocytic cup; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; TAS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0071976; P:cell gliding; IMP:MGI.
DR GO; GO:0031589; P:cell-substrate adhesion; IMP:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0006887; P:exocytosis; IMP:MGI.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IMP:MGI.
DR GO; GO:0120117; P:T cell meandering migration; IMP:MGI.
DR GO; GO:0002456; P:T cell mediated immunity; IMP:UniProtKB.
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; 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; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Adaptive immunity; ATP-binding; Calmodulin-binding;
KW Cell membrane; Cell projection; Immunity; Lipid-binding; Membrane;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1024
FT /note="Unconventional myosin-Ig"
FT /id="PRO_0000340318"
FT DOMAIN 15..713
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 716..745
FT /note="IQ"
FT DOMAIN 830..1023
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 590..612
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 999..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1008..1024
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 111
FT /note="G->R: Does not affect localization to the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:19968988"
FT MUTAGEN 167
FT /note="R->C: Does not affect localization to the plasma
FT membrane."
FT /evidence="ECO:0000269|PubMed:19968988"
FT MUTAGEN 883
FT /note="K->A: Abolishes localization to phagocytic cups;
FT when associated with A-893."
FT /evidence="ECO:0000269|PubMed:23038771"
FT MUTAGEN 893
FT /note="R->A: Abolishes localization to phagocytic cups;
FT when associated with A-883."
FT /evidence="ECO:0000269|PubMed:23038771"
FT CONFLICT 425
FT /note="L -> Q (in Ref. 1; BAC27149)"
FT /evidence="ECO:0000305"
FT CONFLICT 467
FT /note="H -> R (in Ref. 1; BAC40093)"
FT /evidence="ECO:0000305"
FT CONFLICT 816
FT /note="I -> T (in Ref. 1; BAC40093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1024 AA; 117227 MW; F24181A6D37EE9EA CRC64;
MLAVGRMEDE EGPEYGKPDF VLLDQLTMED FMKNLELRFE KGRIYTYIGE VLVSVNPYQE
LPLYGPEAIA KYQGRELYER PPHLYAVANA AYKAMKRRSR DTCIVISGES GAGKTEASKH
IMQYIAAVTN PSQRAEVERV KNVLLKSTCV LEAFGNARTN RNHNSSRFGK YMDINFDFKG
DPVGGHIHSY LLEKSRVLKQ HVGERNFHAF YQLLRGSEDQ ELQGLHLERN PAVYNFTRQG
AGLNMGVHNA LDSDEKSHQG VMEAMRIIGF SPDEVESIHR ILAAILHLGN IEFVETEENG
PQKGGLEVAD EALVGYVAKL TATPRDLVLR TLLARTVASG GREVIEKSHT VAEASYARDA
CAKAMYQRLF EWVVNKINSI MEPRNRDPRC DGKDTVIGVL DIYGFEVFPV NSFEQFCINY
CNEKLQQLFI QLILKQEQEE YEREGIAWQT IEYFNNATIV ELVEQPHRGI LAVLDEACST
AGPITDRIFL QTLDTHHRHH PHYSSRQLCP TDKTMEFGRD FQIKHYAGDV TYSVEGFIDK
NRDSLFQDFK RLLYNSVDPT LRAMWPDGQQ DITEVTKRPL TAGTLFKNSM VALVENLASK
EPFYVRCIKP NEDKVAGRLD EAHCRHQVEY LGLLENVRVR RAGFASRQPY PRFLLRYKMT
CEYTWPNHLL GSDRDAVSAL LEQHGLQGDV AFGHSKLFIR SPRTLVTLEQ SRARLIPIIV
LLLQKAWRGT LARWHCRRLR AIYTIMRWFR RHKVRAHLIE LQRRFQAARQ PPLYGRDLVW
PTPPAVLQPF QDTCRVLFSR WRARQLVKNI PPSDMIQIKA KVAAMGALQG LRQDWGCQRA
WARDYLSSDT DNPTASHLFA EQLKALREKD GFGSVLFSSH VRKVNRFRKS RDRALLLTDR
YLYKLEPGRQ YRVMRAVPLE AVTGLSVTSG RDQLVVLHAQ GYDDLVVCLH RSQPPLDNRI
GELVGMLAAH CQGEGRTLEV RVSDCIPLSQ RGARRLISVE PRPEQPEPDF QSSRSTFTLL
WPSH
