MYO5B_MOUSE
ID MYO5B_MOUSE Reviewed; 1818 AA.
AC P21271; Q148A3; Q69ZR6; Q811F6; Q91X59;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Unconventional myosin-Vb;
GN Name=Myo5b; Synonyms=Kiaa1119;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Colon, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1054-1818 (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1086-1818 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=2236059; DOI=10.1073/pnas.87.21.8491;
RA Huang W.-M., Reed-Fourquet L., Wu E., Wu J.-Y.;
RT "Molecular cloning and amino acid sequence of brain L-glutamate
RT decarboxylase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:8491-8495(1990).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH LIMA1.
RX PubMed=29880681; DOI=10.1126/science.aao6575;
RA Zhang Y.Y., Fu Z.Y., Wei J., Qi W., Baituola G., Luo J., Meng Y.J.,
RA Guo S.Y., Yin H., Jiang S.Y., Li Y.F., Miao H.H., Liu Y., Wang Y., Li B.L.,
RA Ma Y.T., Song B.L.;
RT "A LIMA1 variant promotes low plasma LDL cholesterol and decreases
RT intestinal cholesterol absorption.";
RL Science 360:1087-1092(2018).
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 (PubMed:29880681). {ECO:0000250,
CC ECO:0000269|PubMed:29880681}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P70569}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P21271-1; Sequence=Displayed;
CC Name=3;
CC IsoId=P21271-3; Sequence=VSP_022099;
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a glutamate decarboxylase (GAD).
CC {ECO:0000305|PubMed:2236059}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA37655.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; BC011494; AAH11494.1; -; mRNA.
DR EMBL; BC046444; AAH46444.1; -; mRNA.
DR EMBL; BC118525; AAI18526.1; -; mRNA.
DR EMBL; AK173102; BAD32380.1; -; Transcribed_RNA.
DR EMBL; M55253; AAA37655.1; ALT_SEQ; mRNA.
DR CCDS; CCDS37858.1; -. [P21271-1]
DR PIR; A36481; A36481.
DR AlphaFoldDB; P21271; -.
DR SMR; P21271; -.
DR IntAct; P21271; 1.
DR MINT; P21271; -.
DR STRING; 10090.ENSMUSP00000073790; -.
DR iPTMnet; P21271; -.
DR PhosphoSitePlus; P21271; -.
DR EPD; P21271; -.
DR jPOST; P21271; -.
DR MaxQB; P21271; -.
DR PaxDb; P21271; -.
DR PRIDE; P21271; -.
DR ProteomicsDB; 287588; -. [P21271-1]
DR ProteomicsDB; 287589; -. [P21271-3]
DR MGI; MGI:106598; Myo5b.
DR eggNOG; KOG0160; Eukaryota.
DR InParanoid; P21271; -.
DR PhylomeDB; P21271; -.
DR Reactome; R-MMU-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR ChiTaRS; Myo5b; mouse.
DR PRO; PR:P21271; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P21271; protein.
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; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0098871; C:postsynaptic actin cytoskeleton; ISO:MGI.
DR GO; GO:0098944; C:postsynaptic recycling endosome membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISO:MGI.
DR GO; GO:0016197; P:endosomal transport; ISS:UniProtKB.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IDA:SynGO.
DR GO; GO:0099639; P:neurotransmitter receptor transport, endosome to plasma membrane; ISO:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0050775; P:positive regulation of dendrite morphogenesis; ISO:MGI.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:0015031; P:protein transport; ISO:MGI.
DR GO; GO:0099159; P:regulation of modification of postsynaptic structure; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; ISO:MGI.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:MGI.
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; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Coiled coil; Cytoplasm; Motor protein; Myosin; Nucleotide-binding;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1818
FT /note="Unconventional myosin-Vb"
FT /id="PRO_0000123461"
FT DOMAIN 8..60
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 69..762
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 765..794
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 788..817
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 813..842
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 836..865
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 861..890
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 884..913
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1496..1773
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 641..663
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 1086..1120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1161..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1140..1261
FT /evidence="ECO:0000255"
FT COILED 1313..1415
FT /evidence="ECO:0000255"
FT COMPBIAS 1095..1120
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 1416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ULV0"
FT VAR_SEQ 1310
FT /note="N -> NSQTEDWGYLNEDGELGLAYQGLKQVA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_022099"
FT CONFLICT 829
FT /note="A -> V (in Ref. 1; AAH46444)"
FT /evidence="ECO:0000305"
FT CONFLICT 840
FT /note="T -> A (in Ref. 1; AAH46444)"
FT /evidence="ECO:0000305"
FT CONFLICT 879..880
FT /note="KR -> RC (in Ref. 1; AAH46444)"
FT /evidence="ECO:0000305"
FT CONFLICT 884
FT /note="E -> Q (in Ref. 1; AAH46444)"
FT /evidence="ECO:0000305"
FT CONFLICT 1217..1218
FT /note="KA -> NG (in Ref. 3; AAA37655)"
FT /evidence="ECO:0000305"
FT CONFLICT 1257
FT /note="V -> A (in Ref. 3; AAA37655)"
FT /evidence="ECO:0000305"
FT CONFLICT 1446
FT /note="D -> V (in Ref. 3; AAA37655)"
FT /evidence="ECO:0000305"
FT CONFLICT 1464
FT /note="S -> L (in Ref. 3; AAA37655)"
FT /evidence="ECO:0000305"
FT CONFLICT 1544
FT /note="T -> I (in Ref. 3; AAA37655)"
FT /evidence="ECO:0000305"
FT CONFLICT 1578..1579
FT /note="IA -> MP (in Ref. 3; AAA37655)"
FT /evidence="ECO:0000305"
FT CONFLICT 1620..1631
FT /note="Missing (in Ref. 3; AAA37655)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1818 AA; 210570 MW; 78CFFA626CADC4A0 CRC64;
MSYSELYTRY TRVWIPDPDE VWRSAELTKD YKEGDKSLQL RLEDDTILEY PVDVQNNQVP
FLRNPDILVG ENDLTALSHL HEPAVLHNLK VRFLESNHIY TYCGIVLVAI NPYEQLPIYG
QDVIYAYSGQ NMGDMDPHIF AVAEEAYKQM ARDEKNQSII VSGESGAGKT VSAKYAMRYF
ATVGGSASDT NIEEKVLASS PIMEAIGNAK TTRNDNSSRF GKFIEIGFDK KYHIIGANMR
TYLLEKSRVV FQADDERNYH IFYQLCAAAS LPEFKELALT CAEDFFYTAH GGNTTIEGVN
DADDFEKTRQ ALTLLGVRDS HQISIFKIIA SILHLGSVEI QSERDGDSCS ISPQDEHLSN
FCSLLGIEHS QMEHWLCHRK LVTTSETYVK TMSLQQVVNA RDALAKHIYA QLFSWIVEHI
NKALHTSHKQ HSFIGVLDIY GFETFEINSF EQFCINYANE KLQQQFNSHV FKLEQEEYMK
EQIPWTLIDF YDNQPCIDLI EAKLGILDLL DEECKVPKGT DQNWAQKLYE RHSNSQHFQK
PRMSNTAFIV NHFADKVEYL SDGFLEKNRD TVYEEQINIL KASKFPLVAD LFHDDKDSAP
ATNTAKNRSS SKINVRSSRP LIKVPNKEHK KSVGYQFRTS LNLLMETLNA TTPHYVRCIK
PNDEKLPFHF DPKRAVQQLR ACGVLETIRI SAAGYPSRWT YHDFFNRYRV LMKKRELTNT
DKKNICKSVL ESLIKDPDKF QFGRTKIFFR AGQVAYLEKL RADKFREATI MIQKSVRGWL
QRVKYRRLRA ATLSLQRFCR GYLARRLAEH LRRTRAAIVF QKQYRMLKAR RAYRRVCRAT
VIIQSFTRAM FVRRNYRQVL MEHKATIIQK YARGWMARKR FLRERDAAIV IQCAFRRLKA
RQELKALKIE ARSAEHLKRL NVGMENKVVQ LQRKIDDQNK EFKTLSEQLS AVTSSHAVEV
EKLKKELAHY QQNQEADTSL QLQEEVQSLR TELQKAHSER RVLEDAHNKE NGELRKRVAD
LEHENALLKD EKEYLNNQIL CQSKAESSQS SVEENLLMKK ELEEERSRYQ NLVKEYSQLE
QRYENLRDEQ TPGHRKNPSN QSSLESDSNY PSISTSEIGD TEDALQQVEE IGIEKAAMDM
TVFLKLQKRV RELEQERKKL QAQLEKGQQD SKKGQVEQQN NGLDVDQDAD IAYNSLKRQE
LESENKKLKN DLNELRKAVA DQAMQDNSTH SSPDSYSLLL NQLKLANEEL EVRKEEVLIL
RTQIMNADQR RLSGKNMEPN INARTSWPNS EKHVDQEDAI EAYHGVCQTN RLLEAQLQAQ
SLEHEEEVEH LKAQVEALKE EMDKQQQTFC QTLLLSPEAQ VEFGVQQEIS RLTNENLDFK
ELVEKLEKNE RKLKKQLKIY MKKVQDLEAA QALAQSDRRH HELTRQVTVQ RKEKDFQGML
EYHKEDEALL IRNLVTDLKP QMLSGTVPCL PAYILYMCIR HADYTNDDLK VHSLLSSTIN
GIKKVLKKHN DDFEMTSFWL SNTCRFLHCL KQYSGDEGFM TQNTAKQNEH CLKNFDLTEY
RQVLSDLSIQ IYQQLIKIAE GLLQPMIVSA MLENESIQGL SGVRPTGYRK RSSSMVDGEN
SYCLEAIVRQ MNSFHTVLCD QGLDPEIILQ VFKQLFYMIN AVTLNNLLLR KDACSWSTGM
QLRYNISQLE EWLRGKNLHQ SGAVQTMEPL IQAAQLLQLK KKTHEDAEAI CSLCTSLSTQ
QIVKILNLYT PLNEFEERVT VSFIRTIQAQ LQERNDPQQL LLDSKHVFPV LFPYNPSALT
MDSIHIPACL NLEFLNEV
