ID G3SDF1_GORGO Unreviewed; 1887 AA.
AC G3SDF1;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Myosin-9 {ECO:0000256|ARBA:ARBA00039816};
DE AltName: Full=Myosin heavy chain 9 {ECO:0000256|ARBA:ARBA00041440};
DE AltName: Full=Myosin heavy chain, non-muscle IIa {ECO:0000256|ARBA:ARBA00042289};
DE AltName: Full=Non-muscle myosin heavy chain IIa {ECO:0000256|ARBA:ARBA00043098};
GN Name=MYH9 {ECO:0000313|Ensembl:ENSGGOP00000026131.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000026131.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000026131.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000026131.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000026131.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, Cortical
CC granule {ECO:0000256|ARBA:ARBA00037865}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; CABD030120996; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030120997; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030120998; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030120999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000025497.2; ENSGGOP00000026131.2; ENSGGOG00000001852.3.
DR GeneTree; ENSGT00940000155632; -.
DR HOGENOM; CLU_000192_4_1_1; -.
DR Proteomes; UP000001519; Chromosome 22.
DR Bgee; ENSGGOG00000001852; Expressed in adult mammalian kidney and 5 other cell types or tissues.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0060473; C:cortical granule; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 5.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 6.10.250.2420; -; 1.
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 Gene3D; 4.10.270.10; Myosin, subunit A; 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; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036305; RGS_sf.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR PANTHER; PTHR45615:SF16; MYOSIN-9; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 6.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT DOMAIN 39..703
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 581..603
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 962..984
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1804..1887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1842..1857
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1864..1887
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1887 AA; 218035 MW; D1D79416388FD037 CRC64;
MQSLRWPLVM KKTKGWKELG ELASVTKEVG IGDPSLLPTY SGLFCVVINP YKNLPIYSEE
IVEMYKGKKR HEMPPHIYAI TDTAYRSMMQ ARDFLASLGS GESGAGKTEN TKKVIQYLAY
VASSHKSKKD QGELERQLLQ ANPILEAFGN AKTVKNDNSS RFGKFIRINF DVNGYIVGAN
IETYLLEKSR AIRQAKEERT FHIFYYLLSG AGEHLKTDLL LEPYNKYRFL SNGHVTIPGQ
QDKDMFQETM EAMRIMGIPE EEQMGLLRVI SGVLQLGNIV FKKERNTDQA SMPDNTAAQK
VSHLLGINVT DFTRGILTPR IKVGRDYVQK AQTKEQADFA IEALAKATYE RMFRWLVLRI
NKALDKTKRQ GASFIGILDI AGFEIFDLNS FEQLCINYTN EKLQQLFNHT MFILEQEEYQ
REGIEWNFID FGLDLQPCID LIEKPAGPPG ILALLDEECW FPKATDKSFV EKVMQEQGTH
PKFQKPKQLK DKADFCIIHY AGKVDYKADE WLMKNMDPLN DNIATLLHQS SDKFVSELWK
DVDRIIGLDQ VAGMSETALP GAFKTRKGMF RTVGQLYKEQ LAKLMATLRN TNPNFVRCII
PNHEKKAGKL DPHLVLDQLR CNGVLEGIRI CRQGFPNRVV FQEFRQRYEI LTPNSIPKGF
MDGKQACVLM IKALELDSNL YRIGQSKVFF RAGVLAHLEE ERDLKITDVI IGFQACCRGY
LARKAFAKRQ QQLTAMKVLQ RNCAAYLKLR NWQWWRLFTK VKPLLQVSRQ EEEMMAKEEE
LVKVREKQLA AENRLTEMET LQSQLMAEKL QLQEQLQAET ELCAEAEELR ARLTAKKQEL
EEICHDLEAR VEEEEERCQH LQAEKKKMQQ NIQELEEQLE EEESARQKLQ LEKVTTEAKL
KKLEEEQIIL EDQNCKLAKE KKLLEDRIAE FTTNLTEEEE KSKSLAKLKN KHEAMITDLE
ERLRREEKQR QELEKTRRKL EGDSTDLSDQ IAELQAQIAE LKMQLAKKEE ELQAALARVE
EEAAQKNMAL KKIRELESQI SELQEDLESE RASRNKAEKQ KRDLGEELEA LKTELEDTLD
STAAQQELRS KREQEVNILK KTLEEEAKTH EAQIQEMRQK HSQAVEELAE QLEQTKRVKA
NLEKAKQTLE NERGELANEV KVLLQGKGDS EHKRKKVEAQ LQELQVKFNE GERVRTELAD
KVTKLQVELD NVTGLLSQSD SKSSKLTKDF SALESQLQDT QELLQEENRQ KLSLSTKLKQ
VEDEKNSFRE QLEEEEEAKH NLEKQIATLH AQVADMKKKM EDSVGCLETA EEVKRKLQKD
LEGLSQRHEE KVAAYDKLEK TKTRLQQELD DLLVDLDHQR QSACNLEKKQ KKFDQLLAEE
KTISAKYAEE RDRAEAEARE KETKALSLAR ALEEAMEQKA ELERLNKQFR TEMEDLMSSK
DDVGKSVHEL EKSKRALEQQ VEEMKTQLEE LEDELQATED AKLRLEVNLQ AMKAQFERDL
QGRDEQSEEK KKQLVRQVRE MEAELEDERK QRSMAVAARK KLEMDLKDLE AHIDSANKNR
DEAIKQLRKL QAQMKDCMRE LDDTRASREE ILAQAKENEK KLKSMEAEMI QLQEELAAAE
RAKRQAQQER DELADEIANS SGKGALALEE KRRLEARIAQ LEEELEEEQG NTELINDRLK
KANLQIDQIN TDLNLERSHA QKNENARQQL ERQNKELKVK LQEMEGTVKS KYKASITALE
AKIAQLEEQL DNETKERQAA CKQVRRTEKK LKDVLLQVDD ERRNAEQYKD QADKASTRLK
QLKRQLEEAE EEAQRANASR RKLQRELEDA TETADAMNRE VSSLKNKLRR GDLPFVVPRR
MARKGAGDGS DEEVDGKADG AEAKPAE
//
