ID MYO16_RAT Reviewed; 1912 AA.
AC Q9ERC1; Q9QXI0;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 24-JAN-2024, entry version 153.
DE RecName: Full=Unconventional myosin-XVI;
DE AltName: Full=Myosin heavy chain myr 8;
DE AltName: Full=Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3;
DE AltName: Full=Unconventional myosin-16;
GN Name=Myo16 {ECO:0000250|UniProtKB:Q9Y6X6};
GN Synonyms=Myr8 {ECO:0000312|RGD:621561}, Nyap3;
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] {ECO:0000305, ECO:0000312|EMBL:AAG23288.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP PPP1CA; PPP1CC AND F-ACTIN.
RC STRAIN=Sprague-Dawley {ECO:0000312|EMBL:AAG23288.1};
RC TISSUE=Astrocyte {ECO:0000269|PubMed:11588169};
RX PubMed=11588169; DOI=10.1523/jneurosci.21-20-07954.2001;
RA Patel K.G., Liu C., Cameron P.L., Cameron R.S.;
RT "Myr 8, a novel unconventional myosin expressed during brain development
RT associates with the protein phosphatase catalytic subunits 1alpha and
RT 1gamma1.";
RL J. Neurosci. 21:7954-7968(2001).
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). May be
CC involved in targeting of the catalytic subunit of protein phosphatase 1
CC during brain development. Activates PI3K and concomitantly recruits the
CC WAVE1 complex to the close vicinity of PI3K and regulates neuronal
CC morphogenesis (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:11588169}.
CC -!- SUBUNIT: Binds PPP1CA and/or PPP1CC. Binds F-actin in an ATP-sensitive
CC manner (PubMed:11588169). Interacts with ACOT9, ARHGAP26 and PIK3R2.
CC Interacts with components of the WAVE1 complex, CYFIP1 and NCKAP1; this
CC interaction mediates PI3K-WAVE1 association and actin cytoskeleton
CC remodeling (By similarity). Interacts with KIRREL3 (By similarity).
CC {ECO:0000250|UniProtKB:Q5DU14, ECO:0000250|UniProtKB:Q9Y6X6,
CC ECO:0000269|PubMed:11588169}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11588169}.
CC Note=Found in puncta in soma and processes of astrocytes and
CC dissociated cerebellar cells with the morphology of migrating granule
CC cells. {ECO:0000269|PubMed:11588169}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11588169}; Synonyms=Myr8b
CC {ECO:0000269|PubMed:11588169};
CC IsoId=Q9ERC1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:11588169}; Synonyms=Myr8a
CC {ECO:0000269|PubMed:11588169};
CC IsoId=Q9ERC1-2; Sequence=VSP_052444, VSP_052445;
CC -!- TISSUE SPECIFICITY: Highest level of isoform 1 found in brain. Also
CC found in bladder, kidney and lung. Very low or undetectable levels of
CC isoform 2 in all tissues tested. {ECO:0000269|PubMed:11588169}.
CC -!- DEVELOPMENTAL STAGE: Isoform 1 is expressed at all developmental stages
CC with highest levels during the first two weeks after birth when
CC migration of neurons and formation of dendrites and axons is highest.
CC Within the developing brain the highest level is found in granule
CC neurons in the initial stages of migration. Also found in soma and
CC dendrites of developing Purkinje cells. {ECO:0000269|PubMed:11588169}.
CC -!- PTM: Phosphorylated on tyrosine residues by FYN upon stimulation with
CC CNTN5. {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NYAP family.
CC {ECO:0000305}.
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DR EMBL; AF209114; AAF20150.1; -; mRNA.
DR EMBL; AY004215; AAG23288.1; -; mRNA.
DR PIR; A59288; A59288.
DR RefSeq; NP_620248.1; NM_138893.1. [Q9ERC1-1]
DR RefSeq; XP_017455479.1; XM_017599990.1. [Q9ERC1-1]
DR AlphaFoldDB; Q9ERC1; -.
DR SMR; Q9ERC1; -.
DR BioGRID; 251379; 1.
DR STRING; 10116.ENSRNOP00000022741; -.
DR iPTMnet; Q9ERC1; -.
DR PhosphoSitePlus; Q9ERC1; -.
DR PaxDb; 10116-ENSRNOP00000022741; -.
DR Ensembl; ENSRNOT00000022742.4; ENSRNOP00000022741.4; ENSRNOG00000016483.7. [Q9ERC1-1]
DR Ensembl; ENSRNOT00055024752; ENSRNOP00055020230; ENSRNOG00055014411. [Q9ERC1-1]
DR Ensembl; ENSRNOT00060006656; ENSRNOP00060004996; ENSRNOG00060003978. [Q9ERC1-1]
DR GeneID; 192253; -.
DR KEGG; rno:192253; -.
DR UCSC; RGD:621561; rat. [Q9ERC1-1]
DR AGR; RGD:621561; -.
DR CTD; 23026; -.
DR RGD; 621561; Myo16.
DR eggNOG; KOG0505; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000158920; -.
DR HOGENOM; CLU_002267_0_0_1; -.
DR InParanoid; Q9ERC1; -.
DR OMA; RVMYDIV; -.
DR OrthoDB; 1094820at2759; -.
DR PhylomeDB; Q9ERC1; -.
DR TreeFam; TF332267; -.
DR PRO; PR:Q9ERC1; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Bgee; ENSRNOG00000016483; Expressed in frontal cortex and 3 other cell types or tissues.
DR Genevisible; Q9ERC1; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0016459; C:myosin complex; IDA:RGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:HGNC-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:HGNC-UCL.
DR GO; GO:0003779; F:actin binding; IDA:RGD.
DR GO; GO:0051015; F:actin filament binding; IDA:HGNC-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0021549; P:cerebellum development; IEP:HGNC-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:HGNC-UCL.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:BHF-UCL.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
DR GO; GO:0043491; P:phosphatidylinositol 3-kinase/protein kinase B signal transduction; ISO:RGD.
DR CDD; cd14878; MYSc_Myo16; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR036042; MYSc_Myo16.
DR InterPro; IPR039482; NYAP_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47335; UNCONVENTIONAL MYOSIN-XVI; 1.
DR PANTHER; PTHR47335:SF1; UNCONVENTIONAL MYOSIN-XVI; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF15439; NYAP_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00248; ANK; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ANK repeat; ATP-binding; Cytoplasm;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1912
FT /note="Unconventional myosin-XVI"
FT /id="PRO_0000289138"
FT REPEAT 59..88
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 92..121
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 125..154
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 158..189
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REPEAT 191..217
FT /note="ANK 5"
FT /evidence="ECO:0000255"
FT REPEAT 221..250
FT /note="ANK 6"
FT /evidence="ECO:0000255"
FT REPEAT 253..283
FT /note="ANK 7"
FT /evidence="ECO:0000255"
FT REPEAT 287..316
FT /note="ANK 8"
FT /evidence="ECO:0000255"
FT DOMAIN 401..1144
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 1146..1175
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 371..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1365
FT /note="Involved in CYFIP1- and NCKAP1-binding"
FT /evidence="ECO:0000250"
FT REGION 1220..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1259..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1543..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1664..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1756..1794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1869..1912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1260..1282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1543..1576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1581..1647
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1876..1890
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 497..504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1322
FT /note="A -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11588169"
FT /id="VSP_052444"
FT VAR_SEQ 1323..1912
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11588169"
FT /id="VSP_052445"
SQ SEQUENCE 1912 AA; 210691 MW; 7C15014A1A83C9C3 CRC64;
MEIDQCLLES LPLGQRQRLV RRMRCEQIKA YYEREKVFQK QEGLLKRIKP GKSQKVRFGL
ADMIQDAIIH HHDKEVLQLL KEGADPHTLV SSGGSLLHLC ARYDNVFIAE VLIDRGVNVN
HQDEDFWAPM HIACACDNPD IVLLLILAGA NVLLQDVNGN IPLDYAVEGT ESSAILLAYL
DENGVDLNSL RQIKLQRPLS MLTDVRHFLS SGGDVNEKND DGVTLLHMAC ASGYKEVVLL
LLEHGGDLNG MDDGYWTPLH LAAKYGQTTL VKLLLAHQAN PHLVNCNGEK PSDIAASESI
EEMLLKAEIA WEERMKESPS VPSLAQEELY EEILHDLPEL SSKLSPLVLP IAKQDSLLEK
DIMFKDTTKG LCNQESQDGP PETSMVSSSS KPEQVQLTPP APSDDLATLS ELNDSSLLYE
IQKRFGNDQI HTFIGDIFLL VNPFKELPIY STVVSQMYLS PTGQRSPSLP PHLFSCAERA
FHRLFQERRP QNIILSGERG SGKTQASKQI MKHLTSRASS SCTMFDSRFK HAICILEAFG
HAKTTLNNVS SCLIQYWELQ FCQRRKHVTG ARISTYMLEK PRLVAQPPGQ GSFLIFSWLM
DGLSAEEKCG LHLSNFCAHR YVSQGMREDV STAERSLNKE RLADLKHALN VIGFSALEVE
NLFAILSAIL HIGDIQFTAL TEADSAFVSD LQLLEQVADM LQVSTDELAS ALTTDIQYFK
GDVIIRRHTT QIAAFYRDLL AKSLYSRLFG FLINTVNCCL QSQDEYKSLQ TLDIGILDIF
GFEEFQKNEF EQLCVNLTNE KMHHYIQEVL FLQEQTECVQ EGVAMETACS PGNQAGVLDF
FFQKPSGFFS LLDEESQAIW SVEPNLPRKL QGLLESSNTN AVYSPMKDGN GNVAFKGQGA
AFTVMHYAGR VTYEIRGAVE RNKDSLSQNL LFVMKTSENV VISHLFQSKL SPTGSLISSY
PSFKFGGHKS SLLSKRIASS MVGVNKNYLE LSKLLKKKGT CTFLQRLERG DPATTASQLT
KSLADITAKL QKGSPHFILC VKPNTSQLPG VFDHFYVSAQ LQYLGVLGLV RLFRYGYPVR
PSFEDFLSRY EPLASVLLGE KKGQPAEERC RLVLQRCKLQ GWQMGVHKVF LKYWQVDQLG
DLWLQMQRKI VTCQKVIRGF LARQHLLQRM SIKQQEVTSI KSFLQSTEDM ALKTYDALVI
QNASDIAREH DRLRKEVHAA YHRNRQEEGT KRAEDQGGCR HAHSNSVPVP MAVDSLAQAL
AGPSSRSPSL HSVFSMDDST GLPSPRKQPP PKPKRDPNTR LSASYEAVSA CLSATKDAAS
EALTRPRPHS DDYSTMKKIP PRKPKRSPHT KLSGSYEEIW GPRPSGTMGQ VGKHHAPGTL
GVQWASPDSM PQCTPQLPLH LPLPQGDYDD DGEPVYIEMV GNAARAGGSE TDSPDQGESV
YEEMKYVLPE EGCGPGMLTF LPASPPLFLE TRKAIILEAG EGSCQPLKDT CDIPPPFPNL
LPHRPPLLVF PPTPVTCSPA SDESPLTPLE VKKLPVLETN LKYPVQSEGS SPLSPQYSKA
QKGENDQLTS PGFPVFNGPS RISPPATPPP PPGPPPAPCG PPSAPCGPPP APCGPPPVPC
GPPPAPCGPP PAPCGAAPAP CRPPTHFAFP PDSVLVTAAK ALTNSDLPRT QPKPSSAPVL
GPCSPFVKAP YSPGRTARAD LRKASSTFSP PSPYSPPNSR PLSSPLDELA SLFNSGRSVL
RRSAVGRRIR EAEGFETNMN LSSRDEPSSS EMASETQDRN ANNHGTQLSS SLSSVVAAEN
GNPVTNGLAE DDGCSRLCLS GMGTSSFQRH RESHTTQVIH QLRLSENESV ALQELLDWRR
KLCESREGWQ EAMQHPEPRA PPPPPCKKPT LLKKPEGGSC TRLSSQLWDS SI
//
