MYH9_CANLF
ID MYH9_CANLF Reviewed; 1960 AA.
AC Q258K2;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Myosin-9;
DE AltName: Full=Myosin heavy chain 9;
DE AltName: Full=Myosin heavy chain, non-muscle IIa;
DE AltName: Full=Non-muscle myosin heavy chain IIa;
DE Short=NMMHC II-a;
DE Short=NMMHC-IIA;
GN Name=MYH9;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Mieskes K., Wohlke A., Drogemuller C., Distl O.;
RT "Molecular characterization of the canine myosin, heavy polypeptide 9, non-
RT muscle (MYH9) gene on dog chromosome 10q23.2.";
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Cellular myosin that appears to play a role in cytokinesis,
CC cell shape, and specialized functions such as secretion and capping (By
CC similarity). Required for cortical actin clearance prior to oocyte
CC exocytosis (By similarity). Promotes cell motility in conjunction with
CC S100A4 (By similarity). During cell spreading, plays an important role
CC in cytoskeleton reorganization, focal contact formation (in the margins
CC but not the central part of spreading cells), and lamellipodial
CC retraction; this function is mechanically antagonized by MYH10 (By
CC similarity). {ECO:0000250|UniProtKB:P35579,
CC ECO:0000250|UniProtKB:Q8VDD5}.
CC -!- SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy chain
CC subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory
CC light chain subunits (MLC-2) (By similarity). Interacts with RASIP1 (By
CC similarity). Interacts with DDR1 (By similarity). Interacts with PDLIM2
CC (By similarity). Interacts with SVIL (By similarity). Interacts with
CC HTRA3 (By similarity). Interacts with Myo7a (By similarity). Interacts
CC with CFAP95 (By similarity). Interacts with LIMCH1; independently of
CC the integration of MYH9 into the myosin complex (By similarity).
CC Interacts with RAB3A (By similarity). Interacts with ZBED4 (By
CC similarity). Interacts with S100A4; this interaction increases cell
CC motility (By similarity). {ECO:0000250|UniProtKB:P35579,
CC ECO:0000250|UniProtKB:Q62812, ECO:0000250|UniProtKB:Q8VDD5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasm, cell cortex
CC {ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasmic vesicle, secretory vesicle,
CC Cortical granule {ECO:0000250|UniProtKB:Q8VDD5}. Note=Colocalizes with
CC actin filaments at lamellipodia margins and at the leading edge of
CC migrating cells (By similarity). In retinal pigment epithelial cells,
CC predominantly localized to stress fiber-like structures with some
CC localization to cytoplasmic puncta (By similarity).
CC {ECO:0000250|UniProtKB:P35579}.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils.
CC -!- PTM: ISGylated. {ECO:0000250|UniProtKB:P35579,
CC ECO:0000250|UniProtKB:Q8VDD5}.
CC -!- PTM: Ubiquitination. {ECO:0000250|UniProtKB:P35579,
CC ECO:0000250|UniProtKB:Q8VDD5}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {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; AM086385; CAJ31056.1; -; mRNA.
DR RefSeq; NP_001104237.1; NM_001110767.1.
DR BMRB; Q258K2; -.
DR IntAct; Q258K2; 1.
DR STRING; 9615.ENSCAFP00000057173; -.
DR PaxDb; Q258K2; -.
DR PRIDE; Q258K2; -.
DR GeneID; 481280; -.
DR KEGG; cfa:481280; -.
DR CTD; 4627; -.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; Q258K2; -.
DR OrthoDB; 47111at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005826; C:actomyosin contractile ring; ISS:UniProtKB.
DR GO; GO:0005938; C:cell cortex; ISS:UniProtKB.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0060473; C:cortical granule; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; ISS:UniProtKB.
DR GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043495; F:protein-membrane adaptor activity; ISS:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0043534; P:blood vessel endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0060471; P:cortical granule exocytosis; ISS:UniProtKB.
DR GO; GO:0032506; P:cytokinetic process; ISS:UniProtKB.
DR GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
DR GO; GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
DR GO; GO:1903919; P:negative regulation of actin filament severing; ISS:UniProtKB.
DR GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
DR GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
DR GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0006903; P:vesicle targeting; IMP:CAFA.
DR Gene3D; 2.30.30.360; -; 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; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036305; RGS_sf.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Actin-binding; ATP-binding; Calmodulin-binding; Cell adhesion;
KW Cell shape; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Methylation; Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT CHAIN 2..1960
FT /note="Myosin-9"
FT /id="PRO_0000274171"
FT DOMAIN 27..77
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 81..776
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 779..808
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 2..838
FT /note="Mediates interaction with LIMCH1"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT REGION 654..676
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1120..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1874..1918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1934..1960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 837..1926
FT /evidence="ECO:0000255"
FT COMPBIAS 1874..1908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1937..1960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 8
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 11
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 102
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 299
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 435
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35580"
FT MOD_RES 613
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 754
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 850
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 860
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 975
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1024
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1357
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1392
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1404
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1410
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1459
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1638
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1669
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1714
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
FT MOD_RES 1793
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1802
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1845
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8VDD5"
FT MOD_RES 1923
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q61879"
FT MOD_RES 1943
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P35579"
SQ SEQUENCE 1960 AA; 226469 MW; 0D287FE27035D521 CRC64;
MAQQAADKYL YVDKNFINNP LAQADWAAKK LVWVPSDKSG FEPASLKEEV GEEAIVELVE
NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LKEXYYSGLI YTYSGLFCVV
INPYKNLPIY SEEIVEMYKG KKRHEMPPHI YAITDTAYRS MMQDREDQSI LCTGESGAGK
TENTKKVIQY LAHVASSHKS KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR
INFDVNGYIV GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPEEEQMGLL RVISGVLQLG NIVFKKERNT
DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY VQKAQTKEQA DFAIEALAKA
TYERMFRWLV LRINKALDKT KRQGASFIGI LDIAGFEIFD LNSFEQLCIN YTNEKLQQLF
NHTMFILEQE EYQREGIEWN FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK
SFVEKVVQEQ GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL
HQSSDKFVSE LWKDVDRIIG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY KEQLAKLMAT
LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN RVVFQEFRQR
YEILTPNSIP KGFMDGKQAC VLMIKALELD SNLYRIGQSK VFFRAGVLAH LEEERDLKIT
DVIIGFQACC RGYLARKAFA KRQQQLTAMK VLQRNCAAYL KLRNWQWWRL FTKVKPLLQV
SRQEEEMMAK EEELVKVREK QLAAENRLTE METLQSQLMA EKLQLQEQLQ AETELCAEAE
ELRARLTAKK QELEEICHDL EARVEEEEER CQHLQAEKKK MQQNIQELEE QLEEEESARQ
KLQLEKVTTE AKLKKLEEDQ IIMEDQNCKL AKEKKLLEDR IAEFTTNLME EEEKSKSLAK
LKNKHEAMIT DLEERLRREE KQRQELEKTR RKLEGDSTDL NDQIAELQAQ IAELKMQLAK
KEEELQAALA RVEEEATQKN MALKKIRELE SQISELQEDL ESERASRNKA EKQKRDLGEE
LEALKTELED TLDSTAAQQE LRSKREQEVN ILKKTLEEEA RTHEAQIQEM RQKHSQAVEE
LAEQLEQTKR VKANLEKAKQ TLENERGELA NEVKVLQQGK GDSEHKRKKA EAQLQELQVK
FTEGERVRTE LADKVTKLQV ELDNVMGLLT QSDSKSSKLT KDFSALESQL QDTQELLQEE
NRQKLSLSTK LKQMEDEKNS FKEQLEEEEE AKRNLEKQIA TLHAQVTDMK KKMEDGVGCL
ETAEEAKRKL QKDLEGLGQR YEEKVAAYDK LEKTKTRLQQ ELDDLLVDLD HQRRTASNLE
KKQKKFDQLL AEEKTISAKY AEERDRAEAE AREKETKALS LARALEEAME QKAELERLNK
QFRTEMEDLM SSKDDVGKSV HELEKSKRAL EQQVEEMKTQ LEELEDELQA TEDAKLRLEV
NLQAMKAQFE RDLQGRDEQS EEKKKQLVRQ VREMEAELED EKKQRSMAVA ARKKLEMDLK
DLEAHIDSAN KNRDEAIKQL RKLQAQMKDC VRELDDTRAS REEILAQAKE NEKKMKSMEA
EMIQLQEELA AAERAKRQAQ QERDELADEI ANSSGKGALA LEEKRRLEAR IAQLEEELEE
EQGNTELVND RLKKANLQID QINTDLNLER SHAQKNENAR QQLERQNKEL KVKLQEMEGT
VKSKYKASIT ALEAKIAQLE EQLDNETKER QAACKQVRRA EKKLKDVLLQ VDDERRNAEQ
FKDQADKAST RLKQLKRQLE EAEEEAQRAN ASRRKLQREL EDATETADAM NREVSSLKNK
LRRGDLPFVV PRRVARKGAG DCSDEEVDGK ADGAEAKAAE
