ID H2RDA5_PANTR Unreviewed; 1875 AA.
AC H2RDA5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Myosin IXB {ECO:0000313|Ensembl:ENSPTRP00000058528.3};
GN Name=MYO9B {ECO:0000313|Ensembl:ENSPTRP00000058528.3,
GN ECO:0000313|VGNC:VGNC:13235};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000058528.3, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000058528.3, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000058528.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; AACZ04031517; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04031518; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PaxDb; 9598-ENSPTRP00000058528; -.
DR Ensembl; ENSPTRT00000066949.3; ENSPTRP00000058528.3; ENSPTRG00000010658.7.
DR VGNC; VGNC:13235; MYO9B.
DR eggNOG; KOG1453; Eukaryota.
DR eggNOG; KOG4229; Eukaryota.
DR GeneTree; ENSGT00940000156845; -.
DR HOGENOM; CLU_000192_2_2_1; -.
DR OMA; SWFRMAL; -.
DR TreeFam; TF319651; -.
DR Proteomes; UP000002277; Chromosome 19.
DR Bgee; ENSPTRG00000010658; Expressed in spleen and 21 other cell types or tissues.
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:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; IEA:UniProt.
DR CDD; cd20884; C1_Myosin-IXb; 1.
DR CDD; cd01385; MYSc_Myo9; 1.
DR CDD; cd17217; RA_Myosin-IXb; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.20.58.530; -; 2.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 2.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.555.10; Rho GTPase activation protein; 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR046987; Myo9.
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; IPR046989; RA_Myosin-IXb.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR46184:SF2; UNCONVENTIONAL MYOSIN-IXB; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 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; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF48350; GTPase activation domain, GAP; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF54236; Ubiquitin-like; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; GTPase activation {ECO:0000256|ARBA:ARBA00022468};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
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:UP000002277};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 15..114
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 146..953
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 1632..1681
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1703..1875
FT /note="Rho-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50238"
FT REGION 709..734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 835..857
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1046..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1320..1411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1455..1484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1066
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1187..1205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1207..1224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1395..1411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1464..1484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 239..246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1875 AA; 212330 MW; A933293D5955C7C7 CRC64;
MSVKEAGSSG RREQAAYHLH IYPQLSTTES QASCRVTATK DSTTSDVIKD AIASLRLDGT
KCYVLVEVKE SGGEEWVLDA NDSPVHRVLL WPRRAQDEHP QEDGYYFLLQ ERNADGTIKY
VHMQLVAQAT ATRRLVERGL 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 RAAVTIQACW RSYRVRRALE RTQAAVYLQA AWRGYWQRKL
YRHQKQSIIR LQSLCRGHLQ RKSFSQMISE KQKAEEKERE ALEAARAGAE EGGLDQAAGG
QQVAEQGPEP AEDGGHLASE PEVQPSDRSP LEHSSPEKEA PSPEKTLPPQ KTVAAESHEK
VPSSREKRES RRQRGLEHVK FQNKHIQSCK KESALREPSR RVNQEQGVSL LEDKKESRED
ETLLVVETEA ENTSQKQPTE QPQAMAVGKV SEETEKTLPS GSPRPGQLER PTSLALDSRV
SPPAPGSAPE TPEDKSKPCG SPRVQEKPDS PGGSTQIQRY LDAERLASAV ELWRGKKLVA
AASPSAMLSQ SLDLSDRHRA TGAALTPTEE RRTSFSTSDV SKLLPSLAKA QPAAETTDGE
RSAKKPAVQK KKSGDASSLP DTGLSPGSQV DSKSTFKRLF LHKTKDKKYS LEGAEELENA
VSGHVVLEAT TMKKGLEAPS GQQHRHAAGE KRTKEPGGKG KKNRNVKIGK ITVSEKWRES
VFRQITNANE LKYLDEFLLN KINDLRSQKT PIESLFIEAT EKFRSNIKTM YSVPNGKIHV
GYKDLMENYQ IVVSNLATER 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 LKITT
//
