MYO1E_RAT
ID MYO1E_RAT Reviewed; 1107 AA.
AC Q63356;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Unconventional myosin-Ie;
DE AltName: Full=Myosin heavy chain myr 3;
DE AltName: Full=Unconventional myosin 1E;
GN Name=Myo1e; Synonyms=Myr3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], ACTIN-BINDING, INTERACTION WITH CALM,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=7730414; DOI=10.1083/jcb.129.3.819;
RA Stoeffler H.E., Ruppert C., Reinhard J., Bahler M.;
RT "A novel mammalian myosin I from rat with an SH3 domain localizes to Con A-
RT inducible, F-actin-rich structures at cell-cell contacts.";
RL J. Cell Biol. 129:819-830(1995).
RN [2]
RP TISSUE SPECIFICITY.
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).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails bind to membranous compartments, which are then moved
CC relative to actin filaments. Binds to membranes containing anionic
CC phospholipids via its tail domain. Required for normal morphology of
CC the glomerular basement membrane, normal development of foot processes
CC by kidney podocytes and normal kidney function (By similarity). In
CC dendritic cells, may control the movement of class II-containing
CC cytoplasmic vesicles along the actin cytoskeleton by connecting them
CC with the actin network via ARL14EP and ARL14 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CALM and F-actin (PubMed:7730414). Interacts
CC (via SH3 domain) with SYNJ1, DNM1 and DNM2. Interacts with ARL14EP.
CC Interacts with CARMIL1 (By similarity). {ECO:0000250|UniProtKB:Q12965,
CC ECO:0000269|PubMed:7730414}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7730414}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7730414}. Cytoplasmic
CC vesicle {ECO:0000305|PubMed:7730414}. Cytoplasmic vesicle, clathrin-
CC coated vesicle {ECO:0000250}. Cell junction
CC {ECO:0000269|PubMed:7730414}. Note=In cultured podocytes, it localizes
CC close to and is associated with the cytoplasmic membrane, with
CC enrichment at the lamellipodia tips. Colocalizes with cytoplasmic
CC vesicles, including endocytic clathrin-coated vesicles. Colocalizes
CC with dynamin at cytoplasmic vesicles (By similarity). Detected in
CC cytoplasmic punctae. Colocalizes with F-actin. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in brain stem, brain cortex, cerebellum,
CC stomach, colon, heart, lung, liver, spleen and kidney. Detected in
CC utricle, cochlea, outer hair cell bundle cuticular plate and vestibular
CC epithelia (at protein level). Detected in cochlea and vestibular
CC tissues. Detected in kidney, lung, spleen and intestine.
CC {ECO:0000269|PubMed:12486594, ECO:0000269|PubMed:7730414}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X74815; CAA52815.1; -; mRNA.
DR PIR; S52517; S52517.
DR RefSeq; NP_775124.1; NM_173101.1.
DR AlphaFoldDB; Q63356; -.
DR SMR; Q63356; -.
DR STRING; 10116.ENSRNOP00000016482; -.
DR iPTMnet; Q63356; -.
DR PhosphoSitePlus; Q63356; -.
DR jPOST; Q63356; -.
DR PaxDb; Q63356; -.
DR PRIDE; Q63356; -.
DR Ensembl; ENSRNOT00000104863; ENSRNOP00000083425; ENSRNOG00000061928.
DR GeneID; 25484; -.
DR KEGG; rno:25484; -.
DR UCSC; RGD:3144; rat.
DR CTD; 4643; -.
DR RGD; 3144; Myo1e.
DR eggNOG; KOG0162; Eukaryota.
DR GeneTree; ENSGT00940000157461; -.
DR InParanoid; Q63356; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; Q63356; -.
DR PRO; PR:Q63356; -.
DR Proteomes; UP000002494; Chromosome 8.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0045334; C:clathrin-coated endocytic vesicle; IEA:Ensembl.
DR GO; GO:0032437; C:cuticular plate; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
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:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; ISS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0035091; F:phosphatidylinositol binding; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
DR GO; GO:0032836; P:glomerular basement membrane development; ISS:UniProtKB.
DR GO; GO:0003094; P:glomerular filtration; ISS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; ISO:RGD.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0006807; P:nitrogen compound metabolic process; ISO:RGD.
DR GO; GO:0048008; P:platelet-derived growth factor receptor signaling pathway; ISO:RGD.
DR GO; GO:0072015; P:podocyte development; ISS:UniProtKB.
DR GO; GO:0035166; P:post-embryonic hemopoiesis; ISO:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11827; SH3_MyoIe_If_like; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR035507; Ie/If_SH3.
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 InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Cell junction; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Lipid-binding; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..1107
FT /note="Unconventional myosin-Ie"
FT /id="PRO_0000123451"
FT DOMAIN 19..692
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 695..724
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 730..922
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1050..1107
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 581..591
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 920..1052
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..1011
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1037..1051
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112..119
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1001
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12965"
SQ SEQUENCE 1107 AA; 126827 MW; B9D8FBB0CE047148 CRC64;
MGSKGAYRYH WQSHNVKHSG VDDMVLLSKI TESSIVENLK KRYMDDYIFT YIGSVLISVN
PFKQMPYFGE KEIEMYQGAA QYENPPHIYA LADSMYRNMI IDRENQCVII SGESGAGKTV
AAKYIMSYVS RVSGGGPKVQ HVKDIILQSN PLLEAFGNAK TVRNNNSSRF GKYFEIQFSP
GGEPDGGKIS NFLLEKSRVV MRNPGERSFH IFYQLIEGAS PEQKQSLGIT SMDYYYYLSL
SGSYKVDDID DKRDFQETLH AMNVIGIFSE EQTLVLQIVA GILHLGNINF KEVGNYAAVE
SEEFLAFPAY LLGINQDRLK EKLTSRQMDS KWGGKSESIH VTLNVEQACY TRDALAKALH
ARVFDFLVDS INKAMEKDHE EYNIGVLDIY GFEIFQKNGF EQFCINFVNE KLQQIFIELT
LKAEQEEYVQ EGIRWTPIEY FNNKIVCDLI ESKVNPPGIM SILDDVCATM HAVGEGADQT
LLQKLQMQIG SHEHFNSWNQ GFIIHHYAGK VSYDMDGFCE RNRDVLFMDL IELMQSSELP
FIKSLFPENL QADKKGRPTT AGSKIKKQAN DLVSTLMKCT PHYIRCIKPN ETKKPKDWEE
SRVKHQVEYL GLKENIRVRR AGYAYRRVFQ KFLQRYAILT KATWPVWRGD EKQGVLHLLQ
SVNMDSDQFQ LGRSKVFIKA PESLFLLEEM RERKYDGYAR VIQKTWRKFV ARKKYVQMRE
DASDLLLNKK ERRRNSINRN FIGDYIGMEE HPELQQFVGK REKIDFADIV TKYDRRFKGV
KRDLLLTPKC LYLIGREKVK QGPDKGLVKE VLKRKIEVER ILSVSLSTMQ DDIFILHEQE
YDSLLESVFK TEFLSLLTKR YEEKTQKQLP LKFSNTLELK LKKENWGPWS AGGSRQVQFY
QGFGDLAILK PSNKVLQVSI GPGLPKNARP TRRNTVSSRG YSGGTNNNYP MRAAPAPPGC
HRNGLTRNQF VHPPRASGNQ RSNQKSLYTS MARPPLPRQQ STGSDRLSQT PESLDFLKVP
DQGAAGVRRQ TTSRPPPAGG RPKPQPKPKP QVPQCKALYA YDAQDTDELS FNANDVIDII
KEDPSGWWTG RLRGKQGLFP NNYVTKI
