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Database: UniProt
Entry: G3R1V6_GORGO
LinkDB: G3R1V6_GORGO
Original site: G3R1V6_GORGO 
ID   G3R1V6_GORGO            Unreviewed;      2157 AA.
AC   G3R1V6;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   03-JUL-2019, entry version 61.
DE   SubName: Full=Myosin IXB {ECO:0000313|Ensembl:ENSGGOP00000009188};
GN   Name=MYO9B {ECO:0000313|Ensembl:ENSGGOP00000009188};
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Gorilla.
OX   NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000009188, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000009188, 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:ENSGGOP00000009188}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2011) to UniProtKB.
RN   [3] {ECO:0000313|Ensembl:ENSGGOP00000009188}
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.,
RA   Xue Y., Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V.,
RA   Beal K., Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A.,
RA   Gu Y., Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K.,
RA   Lunter G., Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D.,
RA   Phillips A.D., Prado-Martinez J., Rogers A.S., Sajjadian S.,
RA   Schmidt D., Shaw K., Simpson J.T., Stenson P.D., Turner D.J.,
RA   Vigilant L., Vilella A.J., Whitener W., Zhu B., Cooper D.N.,
RA   de Jong P., Dermitzakis E.T., Eichler E.E., Flicek P., Goldman N.,
RA   Mundy N.I., Ning Z., Odom D.T., Ponting C.P., Quail M.A., Ryder O.A.,
RA   Searle S.M., Warren W.C., Wilson R.K., Schierup M.H., Rogers J.,
RA   Tyler-Smith C., Durbin R.;
RT   "Insights into hominid evolution from the gorilla genome sequence.";
RL   Nature 483:169-175(2012).
CC   -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC       superfamily. Myosin family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00782}.
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DR   EMBL; CABD030112150; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030112151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030112152; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030112153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030112154; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030112155; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030112156; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030112157; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030112158; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSGGOT00000009442; ENSGGOP00000009188; ENSGGOG00000009393.
DR   GeneTree; ENSGT00940000156845; -.
DR   InParanoid; G3R1V6; -.
DR   Proteomes; UP000001519; Chromosome 19.
DR   Bgee; ENSGGOG00000009393; Expressed in 7 organ(s), highest expression level in cerebellum.
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:0005096; F:GTPase activator activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR   GO; GO:0030048; P:actin filament-based movement; IEA:InterPro.
DR   GO; GO:0007266; P:Rho protein signal transduction; IEA:InterPro.
DR   CDD; cd00029; C1; 1.
DR   CDD; cd01385; MYSc_Myo9; 1.
DR   Gene3D; 1.10.555.10; -; 1.
DR   Gene3D; 3.40.850.10; -; 2.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR036961; Kinesin_motor_dom_sf.
DR   InterPro; IPR028557; MYO9B.
DR   InterPro; IPR001609; Myosin_head_motor_dom.
DR   InterPro; IPR036023; MYSc_Myo9.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000159; RA_dom.
DR   InterPro; IPR008936; Rho_GTPase_activation_prot.
DR   InterPro; IPR000198; RhoGAP_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR46184:SF2; PTHR46184:SF2; 1.
DR   Pfam; PF00612; IQ; 4.
DR   Pfam; PF00063; Myosin_head; 2.
DR   Pfam; PF00788; RA; 1.
DR   Pfam; PF00620; RhoGAP; 1.
DR   PRINTS; PR00193; MYOSINHEAVY.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00015; IQ; 4.
DR   SMART; SM00242; MYSc; 1.
DR   SMART; SM00314; RA; 1.
DR   SMART; SM00324; RhoGAP; 1.
DR   SUPFAM; SSF48350; SSF48350; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50096; IQ; 3.
DR   PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR   PROSITE; PS50200; RA; 1.
DR   PROSITE; PS50238; RHOGAP; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   3: Inferred from homology;
KW   Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS01194079};
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00875240}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001519};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00253054};
KW   Motor protein {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00874053};
KW   Myosin {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS01033784};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782,
KW   ECO:0000256|SAAS:SAAS00874078};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW   Zinc {ECO:0000256|SAAS:SAAS00253075}.
FT   NP_BIND     239    246       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00782}.
FT   REGION      709    734       Disordered. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
FT   REGION      835    857       Actin-binding. {ECO:0000256|PROSITE-
FT                                ProRule:PRU00782}.
FT   REGION     1046   1300       Disordered. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
FT   REGION     1320   1410       Disordered. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
FT   REGION     1455   1484       Disordered. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
FT   REGION     1981   2157       Disordered. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
FT   COILED     1881   1901       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS   1048   1066       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
FT   COMPBIAS   1138   1179       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
FT   COMPBIAS   1187   1205       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
FT   COMPBIAS   1207   1221       Polar. {ECO:0000256|MobiDB-lite:G3R1V6}.
FT   COMPBIAS   1347   1361       Polar. {ECO:0000256|MobiDB-lite:G3R1V6}.
FT   COMPBIAS   1464   1484       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
FT   COMPBIAS   1981   1997       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
FT   COMPBIAS   2022   2043       Pro-rich. {ECO:0000256|MobiDB-lite:
FT                                G3R1V6}.
SQ   SEQUENCE   2157 AA;  243386 MW;  50299C0CCD566DAD CRC64;
     MSVKEAGSSG RREQAAYHLH IYPQLSTTES QASCRVTATK DSTTSDVIKD AIASLRLDGT
     KCYVLVEVKE SGGEEWVLDA NDSPVHRVLL WPRRAQDEHP QEDGYYFLLQ ERNADGTIKY
     VHMQLVAQAT ATQRLVERGL LPRQQADFDD LCNLPELTEG NLLKNLKHRF LQQKIYTYAG
     SILVAINPFK FLPIYNPKYV KMYENQQLGK LEPHVFALAD VAYYTMLRKR VNQCIVISGE
     SGSGKTQSTN FLIHCLTALS QKGYASGVER TILGAGPVLE AFGNAKTAHN NNSSRFGKFI
     QVSYLESGIV RGAVVEKYLL EKSRLVSQEK DERNYHVFYY LLLGVSEEER QEFQLKQPED
     YFYLNQHNLK IEDGEDLKHD FERLKQAMEM VGFLPATKKQ IFAVLSAILY LGNVTYKKRA
     TGREEGLEVG PPEVLDTLSQ LLKVKREILV EVLTKRKTVT VNDKLILPYS LSEAITARDS
     MAKSLYSALF DWIVLRINHA LLNKKDVEEA VSCLSIGVLD IFGFEDFERN SFEQFCINYA
     NEQLQYYFNQ HIFKLEQEEY QGEGITWHNI GYTDNVGCIH LISKKPTGLF YLLDEESNFP
     HATSQTLLAK FKQQHEDNKY FLGTPVMEPA FIIQHFAGKV KYQIKDFREK NMDYMRPDIV
     ALLRGSDSSY VRELIGMDPV AVFRWAVLRA AIRAMAVLRE AGRLRAERAE KAAGMSSPGA
     QSHPEELPRG ASTPSEKLYR DLHNQMIKSI KGLPWQGEDP RSLLQSLSRL QKPRAFILKS
     KGIKQKQIIP KNLLDSKSLK LIISMTLHDR TTKSLLHLHK KKKPPSISAQ FQTSLNKLLE
     ALGKAEPFFI RCIRSNAEKK ELCFDDELVL QQLRYTGMLE TVRIRRSGYS AKYTFQDFTE
     QFQVLLPKDA QPCREVISTL LEKMKIDKRN YQIGKTKVFL KETERQALQE TLHREVVRKI
     LLLQSWFRMV LERRHFLQMK RATVTIQACW RSYRVRRALE RTQAAVYLQA AWRGYWQRKL
     YRRQKQSIIR LQSLCRGHLQ RKSFSQMISE KQKAEEKERE ALEAARAGAE EGGLGQAAGG
     QQVAEQGTEP AEDGGHLASE PEVQPSDRSP LEHSSPEKEA PSPEKTLPPQ KTVAAESHEK
     VPSSREKRES RRQRGLEHVK FQNKHIQSCK EESALREPSR RVTQEQGVSL LEDKKESRED
     ETLLVVETEA ENTSQKQPTE HPQAMAVGKV SEETEKTLPS ESPRPDQLER PTSLALDSRV
     SPLAPGSAPE TPEDKSKPCG SPRIQEKPDS PGGSTQIQRY LDAERLASAV ELWRGKKLVA
     AASPSAMLSQ SLDLSDRHRA TGAALTPTEE RRTSFSTGDV SKLLPSLAKA QPAAETTDGE
     RSAKKPAVQK KKSGDASSLP DAGLSPGSQV DSKSTFKRLF LHKTKDKKYS LEGAEELENA
     VSGHVVLEAT TMKKGLEAPS GQQHRHAAGE KRTKEPGGKG KKNRNVKIGK ITVSEKWRES
     VFRQITNANE LKYLDEFLLN KINDLRSQKT PIESLFIEAT EKFRSNIKTM YSVPNGKIHV
     GYKDLMENYQ IVVSNLATEC GQKDTNLVLN LFQSLLDEFT RGYTKNDFEP VKQSKAQKKK
     RKQERAVQEH NGHVFASYQV SIPQSCEQCL SYIWLMDKAL LCSVCKMTCH KKCVHKIQSH
     CSYTYGRKGE PGAEPGHFGV CVDSLTSDKA SVPIVLEKLL EHVEMHGLYT EGLYRKSGAA
     NRTRELRQAL QTDPAAVKLE NFPIHAITGV LKQWLRELPE PLMTFAQYGD FLRAVELPEK
     QEQLAAIYAV LEHLPEANHN SLERLIFHLV KVALLEDVNR MSPGALAIIF APCLLRCPDN
     SDPLTSMKDV LKITTCVEML IKEQMRKYKV KMEEISQLEA AESIAFRRLS LLRQNAPWPL
     KLGFSSPYEG VLNKSPKTRD SQEEELEVLL EEEAAGGDED REKEILIERI QSIKEEKQDI
     TYRLPELDPR GSDEENLDSE TSASTESLLE ERAGRGASEG PPAPALPCPG APAPSPLPTV
     AAPPRRRPSS FVTVRVKTPR RTPIMPTANI KLPPGLPSHL PRWAPGAREA AAPVRRREPP
     ARRPDQIHSV YITPGADLPV QGALEPLEED GQPPGAKRRY SDPPTYCLPP ASGQTNG
//
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