MYH9_CHICK
ID MYH9_CHICK Reviewed; 1959 AA.
AC P14105; Q9TNS8;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Myosin-9;
DE AltName: Full=Cellular myosin heavy chain, type A;
DE AltName: Full=Myosin heavy chain 9;
DE AltName: Full=Myosin heavy chain, non-muscle IIa;
DE AltName: Full=Non-muscle myosin heavy chain A;
DE Short=NMMHC-A;
DE AltName: Full=Non-muscle myosin heavy chain IIa;
DE Short=NMMHC II-a;
DE Short=NMMHC-IIA;
GN Name=MYH9;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Intestinal epithelium;
RX PubMed=2813355; DOI=10.1073/pnas.86.20.7726;
RA Shohet R.V., Conti M.A., Kawamoto S., Preston Y.A., Brill D.A.,
RA Adelstein R.S.;
RT "Cloning of the cDNA encoding the myosin heavy chain of a vertebrate
RT cellular myosin.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:7726-7730(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 716-1008, AND TISSUE SPECIFICITY.
RX PubMed=2806244; DOI=10.1111/j.1432-1033.1989.tb15057.x;
RA Katsuragawa Y., Yanagisawa M., Inoue A., Masaki T.;
RT "Two distinct nonmuscle myosin-heavy-chain mRNAs are differentially
RT expressed in various chicken tissues. Identification of a novel gene family
RT of vertebrate non-sarcomeric myosin heavy chains.";
RL Eur. J. Biochem. 184:611-616(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1900-1959.
RX PubMed=1512291; DOI=10.1083/jcb.118.5.1085;
RA Hodge T.P., Cross R., Kendrick-Jones J.;
RT "Role of the COOH-terminal nonhelical tailpiece in the assembly of a
RT vertebrate nonmuscle myosin rod.";
RL J. Cell Biol. 118:1085-1095(1992).
CC -!- FUNCTION: Cellular myosin that appears to play a role in cytokinesis,
CC cell shape, and specialized functions such as secretion and capping.
CC {ECO:0000250|UniProtKB:P35579}.
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).
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. {ECO:0000250|UniProtKB:P35579}.
CC -!- TISSUE SPECIFICITY: Expressed in fibroblasts, brain, lung, kidney,
CC spleen, and skeletal, cardiac and smooth muscles.
CC {ECO:0000269|PubMed:2806244}.
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; M26510; AAA48974.1; -; mRNA.
DR PIR; A33977; A33977.
DR RefSeq; NP_990808.1; NM_205477.1.
DR AlphaFoldDB; P14105; -.
DR SMR; P14105; -.
DR STRING; 9031.ENSGALP00000020445; -.
DR iPTMnet; P14105; -.
DR PaxDb; P14105; -.
DR PRIDE; P14105; -.
DR GeneID; 396469; -.
DR KEGG; gga:396469; -.
DR CTD; 4627; -.
DR VEuPathDB; HostDB:geneid_396469; -.
DR eggNOG; KOG0161; Eukaryota.
DR InParanoid; P14105; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; P14105; -.
DR PRO; PR:P14105; -.
DR Proteomes; UP000000539; 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:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IBA:GO_Central.
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:0043621; F:protein self-association; IMP:AgBase.
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: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:0031034; P:myosin filament assembly; IDA:AgBase.
DR GO; GO:0030220; P:platelet formation; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
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 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; 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 Actin-binding; ATP-binding; Calmodulin-binding; Cell shape; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Motor protein; Myosin;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..1959
FT /note="Myosin-9"
FT /id="PRO_0000123419"
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 654..676
FT /note="Actin-binding"
FT REGION 1118..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1694..1717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1879..1917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1936..1959
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 837..1925
FT /evidence="ECO:0000255"
FT COMPBIAS 1118..1149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1694..1710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1879..1907
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"
SQ SEQUENCE 1959 AA; 226503 MW; A75C86086FD3A1A1 CRC64;
MAQRDADKYL YVDKNIINNP LTQADWAAKK LVWVPSEKSG FEAASLKEEV GDEAIVELAE
NGKKVKVNKD DIQKMNPPKF SKVEDMAELT CLNEASVLHN LKERYYSGLI YTYSGLFCVV
INPYKNLPIY SEEIVEMYKG KKRHEMPPHI YAITDTAYRS MMQDREDQSI LCTGESGAGK
TENTKKVIQY LAHVASSHKS KKDQGELERQ LLQANPILEA FGNAKTVKND NSSRFGKFIR
INFDVNGYIV GANIETYLLE KSRAIRQAKE ERTFHIFYYL LSGAGEHLKT DLLLEPYNKY
RFLSNGHVTI PGQQDKDMFQ ETMEAMRIMG IPDEEQIGLL KVISGVLQLG NIVFKKERNT
DQASMPDNTA AQKVSHLLGI NVTDFTRGIL TPRIKVGRDY VQKAQTKEQA DFAIEALAKA
TYEQMFRWLV MRINKALDKT KRQGASFIGI LDIAGFEIFE LNSFEQLCIN YTNEKLQQLF
NHTMFILEQE EYQNEGIEWN FIDFGLDLQP CIDLIEKPAG PPGILALLDE ECWFPKATDK
SFVEKVVQEQ GTHPKFQKPK QLKDKADFCI IHYAGKVDYK ADEWLMKNMD PLNDNIATLL
HQSSDKFVSE LWKDVDRIVG LDQVAGMSET ALPGAFKTRK GMFRTVGQLY KEQLAKLMAT
LRNTNPNFVR CIIPNHEKKA GKLDPHLVLD QLRCNGVLEG IRICRQGFPN RVVFQEFRQR
YEILTPNAIP KGFMDGKQAC VLMIKALELD SNLYRIGQSK VFFRAGVLAH LEEERDLKIT
DVIIGFQACC RGYLARKAFA KRQQQLTAMK VLQRNCAAYL KLRNWQWWRL FTKVKPLLQV
SRQEEEMMAK EEELIKVKEK QLAAENRLSE METFQAQLMA EKMQLQEQLQ AEAELCAEAE
EIRARLTAKK QELEEICHDL EARVEEEEER CQHLQAEKKK MQQNIQELEE QLEEEESARQ
KLQLEKVTTE AKLKKLEEDV IVLEDQNLKL AKEKKLLEDR MSEFTTNLTE EEEKSKSLAK
LKNKHEAMIT DLEERLRREE KQRQELEKTR RKLEGDSSDL HDQIAELQAQ IAELKIQLSK
KEEELQAALA RVEEEAAQKN MALKKIRELE SQITELQEDL ESERASRNKA EKQKRDLGEE
LEALKTELED TLDSTAAQQE LRSKREQEVT VLKKTLEDEA KTHEAQIQEM RQKHSQAIEE
LAEQLEQTKR VKANLEKAKQ ALESERAELS NEVKVLLQGK GDAEHKRKKV DAQLQELQVK
FTEGERVKTE LAERVNKLQV ELDNVTGLLN QSDSKSIKLA KDFSALESQL QDTQELLQEE
TRLKLSFSTK LKQTEDEKNA LKEQLEEEEE AKRNLEKQIS VLQQQAVEAR KKMDDGLGCL
EIAEEAKKKL QKDLESLTQR YEEKIAAYDK LEKTKTRLQQ ELDDIAVDLD HQRQTVSNLE
KKQKKFDQLL AEEKNISAKY AEERDRAEAE AREKETKALS LARALEEAIE QKAELERVNK
QFRTEMEDLM SSKDDVGKSV HELEKAKRAL EQQVEEMKTQ LEELEDELQA TEDAKLRLEV
NQQAMKAQFD RDLLGRDEQN EEKRKQLIRQ VREMEVELED ERKQRSIAVA ARKKLELDLK
DLESHIDTAN KNRDEAIKHV RKLQAQMKDY MRELEDTRTS REEILAQAKE NEKKLKSMEA
EMIQLQEELA AAERAKRQAQ QERDELADEI ANSSGKGALA MEEKRRLEAR IAQLEEELEE
EQGNTEIIND RLKKANLQID QMNADLNAER SNAQKNENAR QQMERQNKEL KLKLQEMESA
VKSKYKATIT ALEAKIVQLE EQLDMETKER QAASKQVRRA EKKLKDILLQ VDDERRNAEQ
FKDQADKANM RLKQLKRQLE EAEEEAQRAN VRRKLQRELD DATETADAMN REVSSLKSKL
RRGDLPFVVT RRLVRKGTGE CSDEEVDGKA EAGDAKATE
