MYO5B_RAT
ID MYO5B_RAT Reviewed; 1846 AA.
AC P70569;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Unconventional myosin-Vb;
DE AltName: Full=Myosin heavy chain myr 6;
GN Name=Myo5b;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8855265; DOI=10.1073/pnas.93.20.10826;
RA Zhao L.P., Koslovsky J.S., Reinhard J., Bahler M., Witt A.E.,
RA Provance D.W., Mercer J.A.;
RT "Cloning and characterization of myr 6, an unconventional myosin of the
RT dilute/myosin-V family.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10826-10831(1996).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=1469047; DOI=10.1083/jcb.119.6.1541;
RA Espreafico E.M., Cheney R.E., Matteoli M., Nascimento A.A.,
RA de Camilli P.V., Larson R.E., Mooseker M.S.;
RT "Primary structure and cellular localization of chicken brain myosin-V
RT (p190), an unconventional myosin with calmodulin light chains.";
RL J. Cell Biol. 119:1541-1557(1992).
CC -!- FUNCTION: May be involved in vesicular trafficking via its association
CC with the CART complex. The CART complex is necessary for efficient
CC transferrin receptor recycling but not for EGFR degradation. Required
CC in a complex with RAB11A and RAB11FIP2 for the transport of NPC1L1 to
CC the plasma membrane. Together with RAB11A participates in CFTR
CC trafficking to the plasma membrane and TF (transferrin) recycling in
CC nonpolarized cells. Together with RAB11A and RAB8A participates in
CC epithelial cell polarization. Together with RAB25 regulates
CC transcytosis. {ECO:0000250|UniProtKB:Q9ULV0}.
CC -!- SUBUNIT: Component of the CART complex, at least composed of ACTN4,
CC HGS/HRS, MYO5B and TRIM3. Interacts with RAB11FIP2 (By similarity).
CC Interacts with RAB11A and RAB8A (By similarity). Found in a complex
CC with CFTR and RAB11A (By similarity). Interacts with NPC1L1 (By
CC similarity). Interacts with LIMA1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:P21271}.
CC -!- INTERACTION:
CC P70569; P19490: Gria1; NbExp=2; IntAct=EBI-975940, EBI-371642;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1469047}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
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DR EMBL; U60416; AAB38840.1; -; mRNA.
DR PIR; A59289; A59289.
DR RefSeq; NP_058779.1; NM_017083.1.
DR AlphaFoldDB; P70569; -.
DR SMR; P70569; -.
DR BioGRID; 247201; 3.
DR IntAct; P70569; 8.
DR STRING; 10116.ENSRNOP00000019512; -.
DR iPTMnet; P70569; -.
DR PhosphoSitePlus; P70569; -.
DR jPOST; P70569; -.
DR PaxDb; P70569; -.
DR PRIDE; P70569; -.
DR GeneID; 25132; -.
DR KEGG; rno:25132; -.
DR CTD; 4645; -.
DR RGD; 621347; Myo5b.
DR eggNOG; KOG0160; Eukaryota.
DR InParanoid; P70569; -.
DR PhylomeDB; P70569; -.
DR Reactome; R-RNO-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR PRO; PR:P70569; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0045179; C:apical cortex; ISS:UniProtKB.
DR GO; GO:0005903; C:brush border; ISO:RGD.
DR GO; GO:0043197; C:dendritic spine; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; IDA:SynGO.
DR GO; GO:0098944; C:postsynaptic recycling endosome membrane; IDA:SynGO.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0051015; F:actin filament binding; IMP:SynGO.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:RGD.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:1905430; P:cellular response to glycine; IEP:RGD.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:0099639; P:neurotransmitter receptor transport, endosome to plasma membrane; IDA:SynGO.
DR GO; GO:0045773; P:positive regulation of axon extension; IMP:RGD.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; IMP:RGD.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:RGD.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IMP:RGD.
DR GO; GO:0015031; P:protein transport; IMP:RGD.
DR GO; GO:0099159; P:regulation of modification of postsynaptic structure; IDA:SynGO.
DR GO; GO:0032880; P:regulation of protein localization; IMP:RGD.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:RGD.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
DR CDD; cd15477; Myo5b_CBD; 1.
DR CDD; cd01380; MYSc_Myo5; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR002710; Dilute_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR037990; Myo5b_CBD.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR036103; MYSc_Myo5.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01843; DIL; 1.
DR Pfam; PF00612; IQ; 6.
DR Pfam; PF00063; Myosin_head; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM01132; DIL; 1.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51126; DILUTE; 1.
DR PROSITE; PS50096; IQ; 6.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1846
FT /note="Unconventional myosin-Vb"
FT /id="PRO_0000123462"
FT DOMAIN 8..60
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 69..763
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 767..788
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 789..813
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 814..837
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 838..861
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 862..884
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 885..914
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1524..1801
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 21..40
FT /note="Requires for interaction with LIMA1"
FT /evidence="ECO:0000250|UniProtKB:Q9ULV0"
FT REGION 599..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..663
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 1088..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 915..1272
FT /evidence="ECO:0000255"
FT COILED 1334..1450
FT /evidence="ECO:0000255"
FT COMPBIAS 602..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 163..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULV0"
SQ SEQUENCE 1846 AA; 213721 MW; AEC1B6F37389EE48 CRC64;
MTYSELYSRY TRVWIPDPDE VWRSAELTKD YKDGDESLQL RLEDDTILDY PIDVQNNQVP
FLRNPDILVG ENDLTALSHL HEPAVLHNLK VRFLESNHIY TYCGIVLVAI NPYEQLPIYG
QDVIYAYSGQ NMGDMDPHIF AVAEEAYKQM ARDEKNQSII VSGESGAGKT VSAKYAMRYF
ATVGGSASDT NIEEKVLASS PIMEAIGNAK TTRNDNSSRF GKYIEIGFDK KYHIIGANMR
TYLLEKSRVV FQADDERNYH IFYQLCAAAS LPEFKELALT CAEDFFYTAH GGNTTIEGVD
DAEDFEKTRQ ALTLLGVRES HQISIFKIIA SILHLGSVEI QAERDGDSCS ISPQDEHLSN
FCRLLGIEHS QMEHWLCHRK LVTTSETYVK TMSLQQVVNA RNALAKHIYA QLFSWIVEHI
NKALQTSLKQ HSFIGVLDIY GFETFEINSF EQFCINYANE KLQQQFNSHV FKLEQEEYMK
EQIPWTLIDF YDNQPCIDLI EAKLGILDLL DEECKVPKGT DQNWAQKLYE RHSNSQHFQK
PRMSNTAFIV IHFADKVEYL SDGFLEKNRD TVYEEQINIL KASKFPLVAD LFRDDEDSVP
ATNTAKSRSS SKINVRSSRP LMKAPNKEHK KSVGYQFRTS LNLLMETLNA TTPHYVRCIK
PNDEKLPFHF DPKRAVQQLR ACGVLETIRI SAAGYPSRWT YHDFFNRYRV LMKKRELANT
TDKKNICKSV LESLIKDPDK FQFGRTKIFF RAGQVAYLEK LRADKFREAT IMIQKTVRGW
LQRVKYRRLR AATLTLQRFC RGYLARRLTE HLRRTRAAIV FQKQYRMLKA RRAYCRVRRA
AVIIQSYTRG HVCTQKLPPV LTEHKATIIQ KYARGWMARR HFQRQRDAAI VIQCAFRRLK
ARQALKALKI EARSAEHLKR LNVGMENKVV QLQRKIDDQN KEFKTLSEQL SAVTSTHAME
VEKLKKELAR YQQNQEADPS LQLQEEVQSL RTELQKAHSE RRVLEDAHNR ENGELRKRVA
DLEHENALLK DEKEHLNHQI LRQSKAESSQ SSVEENLLIK KELEEERSRY QNLVKEYSQL
EQRYENLRDE QQTPGHRKNP SNQSSLESDS NYPSISTSEI GDTEDALQQV EEIGIEKAAM
DMTVFLKLQK RVRELEQERK KLQVQLEKEQ QDSKKVQVEQ QNNGLDVDQD ADIAYNSLKR
QELESENKKL KNDLNERWKA VADQAMQDNS THSSPDSYSL LLNQLKLANE ELEVRKEEVL
ILRTQIMNAD QRRLSGKNME PNINARTSWP NSEKHVDQED AIEAYHGVCQ TNSQTEDWGY
LNEDGELGLA YQGLKQVARL LEAQLQAQNL KHEEEVEHLK AQVEAMKEEM DKQQQTFCQT
LLLSPEAQVE FGVQQEISRL TNENLDFKEL VEKLEKNEKK LKKQLKIYMK KVQDLEAAQA
LAQSDRRHHE LTRQVTVQRK EKDFQGMLEY HKEDEALLIR NLVTDLKPQM LSGTVPCLPA
YILYMCIRHA DYTNDDLKVH SLLSSTINGI KKVLKKHNED FEMTSFWLSN TCRLLHCLKQ
YSGDEGFMTQ NTAKQNEHCL KNFDLTEYRQ VLSDLSIQIY QQLIKIAEGL LQPMIVSAML
ENESIQGLSG VRPTGYRKRS SSMVDGENSY CLEAIIRQMN FFHTVLCDQG LDPEIILQVF
KQLFYMINAV TLNNLLLRKD ACSWSTGMQL RYNISQLEEW LRGKNLQQSG AVQTMEPLIQ
AAQLLQLKKK TQEDAEAICS LCTSLSTQQI VKILNLYTPL NGFEERVTVS FIRTIQAQLQ
ERSDPQQLLL DSKHMFPVLF PFNPSALTMD SIHIPACLNL EFLNEV
