MYO1B_MOUSE
ID MYO1B_MOUSE Reviewed; 1107 AA.
AC P46735; P70244; Q80VD8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Unconventional myosin-Ib;
DE AltName: Full=MIH-L;
DE AltName: Full=Myosin I alpha;
DE Short=MMI-alpha;
DE Short=MMIa;
GN Name=Myo1b;
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 [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=8449986; DOI=10.1083/jcb.120.6.1405;
RA Sherr E.H., Joyce M.P., Greene L.A.;
RT "Mammalian myosin I alpha, I beta, and I gamma: new widely expressed genes
RT of the myosin I family.";
RL J. Cell Biol. 120:1405-1416(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 13-1107 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=8458427; DOI=10.1016/0014-5793(93)80075-6;
RA Koslovsky J.S., Qian C., Jiang X., Mercer J.A.;
RT "Molecular cloning of a mouse myosin I expressed in brain.";
RL FEBS Lett. 320:121-124(1993).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and 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).
CC -!- FUNCTION: Motor protein that may participate in process critical to
CC neuronal development and function such as cell migration, neurite
CC outgrowth and vesicular transport.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P46735-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46735-2; Sequence=VSP_003347;
CC -!- TISSUE SPECIFICITY: Prominent expression is seen in the brain, lung and
CC liver. It is also expressed in the heart and testis. A high level
CC expression is seen in virtually all neurons (but not glia) in the
CC postnatal and adult mouse brain and in neuroblasts of the cerebellar
CC external granular layer.
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; L00923; AAA39800.1; -; mRNA.
DR EMBL; AK141207; BAE24587.1; -; mRNA.
DR EMBL; CH466548; EDK99961.1; -; Genomic_DNA.
DR EMBL; BC046300; AAH46300.1; -; mRNA.
DR EMBL; X69987; CAA49604.1; -; mRNA.
DR CCDS; CCDS14942.1; -. [P46735-1]
DR CCDS; CCDS69887.1; -. [P46735-2]
DR PIR; A45438; A45438.
DR RefSeq; NP_034993.2; NM_010863.4. [P46735-1]
DR AlphaFoldDB; P46735; -.
DR SMR; P46735; -.
DR BioGRID; 201663; 11.
DR IntAct; P46735; 6.
DR MINT; P46735; -.
DR STRING; 10090.ENSMUSP00000018561; -.
DR iPTMnet; P46735; -.
DR PhosphoSitePlus; P46735; -.
DR SwissPalm; P46735; -.
DR jPOST; P46735; -.
DR MaxQB; P46735; -.
DR PaxDb; P46735; -.
DR PeptideAtlas; P46735; -.
DR PRIDE; P46735; -.
DR ProteomicsDB; 287579; -. [P46735-1]
DR ProteomicsDB; 287580; -. [P46735-2]
DR Antibodypedia; 2858; 127 antibodies from 32 providers.
DR DNASU; 17912; -.
DR Ensembl; ENSMUST00000046390; ENSMUSP00000040447; ENSMUSG00000018417. [P46735-1]
DR GeneID; 17912; -.
DR KEGG; mmu:17912; -.
DR UCSC; uc007axr.3; mouse. [P46735-1]
DR CTD; 4430; -.
DR MGI; MGI:107752; Myo1b.
DR VEuPathDB; HostDB:ENSMUSG00000018417; -.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000155752; -.
DR InParanoid; P46735; -.
DR OrthoDB; 122881at2759; -.
DR BioGRID-ORCS; 17912; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Myo1b; mouse.
DR PRO; PR:P46735; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P46735; protein.
DR Bgee; ENSMUSG00000018417; Expressed in undifferentiated genital tubercle and 266 other tissues.
DR ExpressionAtlas; P46735; baseline and differential.
DR Genevisible; P46735; MM.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0045177; C:apical part of cell; ISO:MGI.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0030175; C:filopodium; ISS:UniProtKB.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:MGI.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0003774; F:cytoskeletal motor activity; ISO:MGI.
DR GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISO:MGI.
DR GO; GO:0033572; P:transferrin transport; IDA:MGI.
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; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Isopeptide bond; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..1107
FT /note="Unconventional myosin-Ib"
FT /id="PRO_0000123443"
FT DOMAIN 15..701
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 704..727
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 728..749
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 750..778
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 780..807
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 808..837
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 923..1107
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 592..599
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43795"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43795"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43795"
FT VAR_SEQ 791..819
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8449986"
FT /id="VSP_003347"
FT CONFLICT 44
FT /note="I -> R (in Ref. 5; CAA49604)"
FT /evidence="ECO:0000305"
FT CONFLICT 260
FT /note="I -> Y (in Ref. 5; CAA49604)"
FT /evidence="ECO:0000305"
FT CONFLICT 304
FT /note="N -> I (in Ref. 1; AAA39800)"
FT /evidence="ECO:0000305"
FT CONFLICT 307..317
FT /note="KEICELTSIDQ -> NEKFASRPASVK (in Ref. 1; AAA39800)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="Q -> R (in Ref. 1; AAA39800)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="G -> D (in Ref. 1; AAA39800)"
FT /evidence="ECO:0000305"
FT CONFLICT 570..571
FT /note="AG -> RS (in Ref. 5; CAA49604)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="A -> E (in Ref. 5; CAA49604)"
FT /evidence="ECO:0000305"
FT CONFLICT 809..810
FT /note="KH -> ND (in Ref. 5; CAA49604)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1107 AA; 128564 MW; 42B339708CA9B7E6 CRC64;
MAKMEVKSSL LDNMIGVGDM VLLEPLNEET FIDNLKKRFD HNEIYTYIGS VVISVNPYRS
LPIYSPEKVE DYRNRNFYEL SPHIFALSDE AYRSLRDQDK DQCILITGES GAGKTEASKL
VMSYVAAVCG KGAEVNQVKE QLLQSNPVLE AFGNAKTVRN DNSSRFGKYM DIEFDFKGDP
LGGVISNYLL EKSRVVKQPR GERNFHVFYQ LLSGASEELL YKLKLERDFS RYNYLSLDSA
KVNGVDDAAN FRTVRNAMQI VGFLDHEAEA VLEVVAAVLK LGNIEFKPES RVNGLDESKI
KDKNELKEIC ELTSIDQVVL ERAFSFRTVE AKQEKVSTTL NVAQAYYARD ALAKNLYSRL
FSWLVNRINE SIKAQTKVRK KVMGVLDIYG FEIFEDNSFE QFIINYCNEK LQQIFIELTL
KEEQEEYIRE DIEWTHIDYF NNAIICDLIE NNTNGILAML DEECLRPGTV TDETFLEKLN
QVCATHQHFE SRMSKCSRFL NDTTLPHSCF RIQHYAGKVL YQVEGFVDKN NDLLYRDLSQ
AMWKAGHSLI KSLFPEGNPA KVNLKRPPTA GSQFKASVAT LMRNLQTKNP NYIRCIKPND
KKAAHIFNES LVCHQIRYLG LLENVRVRRA GYAFRQAYEP CLERYKMLCK QTWPHWKGPA
RSGVEVLFNE LEIPVEEHSF GRSKIFIRNP RTLFQLEDLR KQRLEDLATL IQKIYRGWKC
RTHFLLMKRS QVVIAAWYRR YAQQKRYQQI KSSALVIQSY IRGWKARKIL RELKHQKRCK
EAATTIAAYW HGTQARRELK RLKEEARRKH AVAVIWAYWL GLKVRREYRK FFRANAGKKI
YEFTLQRIVQ KYLLEMKNKM PSLSPIDKNW PSRPYLFLDS THKELKRIFH LWRCKKYRDQ
FTDQQKLIYE EKLEASELFK DKKALYPSSV GQPFQGAYLE INKNPKYKKL KDAIEEKIII
AEVVNKINRA NGKSTSRIFL LTNNNLLLAD QKSGQIKSEV PLVDVTKVSM SSQNDGFFAV
HLKEGSEAAS KGDFLFSSDH LIEMATKLYR TTLSQTKQKL NIEISDEFLV QFRQDKVCVK
FIQGNQKNGS VPTCKRKNNR LLEVAVP
