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Myosin-9 (Myosin heavy chain 9) (Myosin heavy chain, non-muscle IIa) (Non-muscle myosin heavy chain IIa) (NMMHC II-a) (NMMHC-IIA)

 MYH9_CANLF              Reviewed;        1960 AA.
Q258K2;
06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
18-APR-2006, sequence version 1.
25-APR-2018, entry version 81.
RecName: Full=Myosin-9;
AltName: Full=Myosin heavy chain 9;
AltName: Full=Myosin heavy chain, non-muscle IIa;
AltName: Full=Non-muscle myosin heavy chain IIa;
Short=NMMHC II-a;
Short=NMMHC-IIA;
Name=MYH9;
Canis lupus familiaris (Dog) (Canis familiaris).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
Canis.
NCBI_TaxID=9615;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Mieskes K., Wohlke A., Drogemuller C., Distl O.;
"Molecular characterization of the canine myosin, heavy polypeptide 9,
non-muscle (MYH9) gene on dog chromosome 10q23.2.";
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Cellular myosin that appears to play a role in
cytokinesis, cell shape, and specialized functions such as
secretion and capping. During cell spreading, plays an important
role in cytoskeleton reorganization, focal contacts formation (in
the margins but not the central part of spreading cells), and
lamellipodial retraction; this function is mechanically
antagonized by MYH10 (By similarity). {ECO:0000250}.
-!- SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy
chain subunits (MHC), 2 alkali light chain subunits (MLC) and 2
regulatory light chain subunits (MLC-2) (By similarity). Interacts
with RASIP1 (By similarity). Interacts with DDR1 (By similarity).
Interacts with SLC6A4 (By similarity). Interacts with PDLIM2 (By
similarity). Interacts with SVIL (By similarity). Interacts with
HTRA3 (By similarity). Interacts with Myo7a (By similarity).
Interacts with C9orf135 homolog (By similarity).
{ECO:0000250|UniProtKB:P35579, ECO:0000250|UniProtKB:Q62812,
ECO:0000250|UniProtKB:Q8VDD5}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q8VDD5}. Cytoplasm, cell cortex
{ECO:0000250|UniProtKB:Q8VDD5}. Note=Colocalizes with actin
filaments at lamellipodia margins and at the leading edge of
migrating cells (By similarity). In retinal pigment epithelial
cells, predominantly localized to stress fiber-like structures
with some localization to cytoplasmic puncta (By similarity).
{ECO:0000250|UniProtKB:P35579}.
-!- DOMAIN: The rodlike tail sequence is highly repetitive, showing
cycles of a 28-residue repeat pattern composed of 4 heptapeptides,
characteristic for alpha-helical coiled coils.
-!- PTM: ISGylated. {ECO:0000250|UniProtKB:P35579,
ECO:0000250|UniProtKB:Q8VDD5}.
-!- PTM: Ubiquitination. {ECO:0000250|UniProtKB:P35579,
ECO:0000250|UniProtKB:Q8VDD5}.
-!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
superfamily. Myosin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AM086385; CAJ31056.1; -; mRNA.
RefSeq; NP_001104237.1; NM_001110767.1.
UniGene; Cfa.12211; -.
ProteinModelPortal; Q258K2; -.
STRING; 9615.ENSCAFP00000002455; -.
PaxDb; Q258K2; -.
PRIDE; Q258K2; -.
GeneID; 481280; -.
KEGG; cfa:481280; -.
CTD; 4627; -.
eggNOG; KOG0161; Eukaryota.
eggNOG; COG5022; LUCA.
HOGENOM; HOG000173958; -.
HOVERGEN; HBG004704; -.
InParanoid; Q258K2; -.
KO; K10352; -.
Proteomes; UP000002254; Unplaced.
GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
GO; GO:0005826; C:actomyosin contractile ring; ISS:UniProtKB.
GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0070382; C:exocytic vesicle; IDA:CAFA.
GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
GO; GO:0001726; C:ruffle; ISS:UniProtKB.
GO; GO:0001725; C:stress fiber; ISS:UniProtKB.
GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; ISS:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0000146; F:microfilament motor activity; ISS:UniProtKB.
GO; GO:0008017; F:microtubule binding; IEA:InterPro.
GO; GO:0003777; F:microtubule motor activity; IEA:InterPro.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0043495; F:protein membrane anchor; ISS:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
GO; GO:0030048; P:actin filament-based movement; ISS:UniProtKB.
GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
GO; GO:0043534; P:blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0032506; P:cytokinetic process; ISS:UniProtKB.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; ISS:UniProtKB.
GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
GO; GO:0030224; P:monocyte differentiation; ISS:UniProtKB.
GO; GO:1903919; P:negative regulation of actin filament severing; ISS:UniProtKB.
GO; GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
GO; GO:1903923; P:positive regulation of protein processing in phagocytic vesicle; ISS:UniProtKB.
GO; GO:0015031; P:protein transport; ISS:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
GO; GO:0006903; P:vesicle targeting; IMP:CAFA.
Gene3D; 2.30.30.360; -; 1.
Gene3D; 3.40.850.10; -; 3.
Gene3D; 4.10.270.10; -; 1.
InterPro; IPR000048; IQ_motif_EF-hand-BS.
InterPro; IPR036961; Kinesin_motor_dom_sf.
InterPro; IPR001609; Myosin_head_motor_dom.
InterPro; IPR027401; Myosin_IQ_contain_sf.
InterPro; IPR004009; Myosin_N.
InterPro; IPR008989; Myosin_S1_N.
InterPro; IPR002928; Myosin_tail.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR036305; RGS_sf.
Pfam; PF00063; Myosin_head; 1.
Pfam; PF02736; Myosin_N; 1.
Pfam; PF01576; Myosin_tail_1; 1.
PRINTS; PR00193; MYOSINHEAVY.
SMART; SM00015; IQ; 1.
SMART; SM00242; MYSc; 1.
SUPFAM; SSF48097; SSF48097; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50096; IQ; 1.
PROSITE; PS51456; MYOSIN_MOTOR; 1.
PROSITE; PS51844; SH3_LIKE; 1.
2: Evidence at transcript level;
Acetylation; Actin-binding; ATP-binding; Calmodulin-binding;
Cell adhesion; Cell shape; Coiled coil; Complete proteome; Cytoplasm;
Cytoskeleton; Methylation; Motor protein; Myosin; Nucleotide-binding;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P35579}.
CHAIN 2 1960 Myosin-9.
/FTId=PRO_0000274171.
DOMAIN 27 77 Myosin N-terminal SH3-like.
{ECO:0000255|PROSITE-ProRule:PRU01190}.
DOMAIN 81 776 Myosin motor. {ECO:0000255|PROSITE-
ProRule:PRU00782}.
DOMAIN 779 808 IQ. {ECO:0000255|PROSITE-
ProRule:PRU00116}.
NP_BIND 174 181 ATP. {ECO:0000255}.
REGION 654 676 Actin-binding. {ECO:0000250}.
COILED 837 1926 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 8 8 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 11 11 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 102 102 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 299 299 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 435 435 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35580}.
MOD_RES 613 613 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 628 628 Phosphoserine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 754 754 Phosphotyrosine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 850 850 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 860 860 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 975 975 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1024 1024 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1114 1114 Phosphoserine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1234 1234 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q61879}.
MOD_RES 1249 1249 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1357 1357 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1392 1392 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1404 1404 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1410 1410 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1459 1459 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1638 1638 N6-acetyllysine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1669 1669 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1714 1714 Phosphoserine.
{ECO:0000250|UniProtKB:P35579}.
MOD_RES 1793 1793 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1802 1802 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1845 1845 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q8VDD5}.
MOD_RES 1923 1923 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q61879}.
MOD_RES 1943 1943 Phosphoserine.
{ECO:0000250|UniProtKB:P35579}.
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


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