MYO5B_HUMAN
ID MYO5B_HUMAN Reviewed; 1848 AA.
AC Q9ULV0; B0I1R3; Q0P656; Q9H6Y6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Unconventional myosin-Vb;
GN Name=MYO5B; Synonyms=KIAA1119;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-126
RP AND LEU-1055 INS.
RC TISSUE=Brain;
RX PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT "Characterization of cDNA clones selected by the GeneMark analysis from
RT size-fractionated cDNA libraries from human brain.";
RL DNA Res. 6:329-336(1999).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS AND 918.
RA Ohara O., Nagase T., Yamakawa H., Kikuno R.;
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ALA-126
RP AND LEU-1055 INS.
RC TISSUE=Brain;
RA Yamakawa H., Kikuno R.F., Nagase T., Ohara O.;
RT "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free
RT recombination: preparation of full-length cDNA clones encoding motor
RT proteins.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Colon;
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 [7]
RP INTERACTION WITH RAB11FIP2.
RX PubMed=11495908; DOI=10.1074/jbc.m104831200;
RA Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R.,
RA Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.;
RT "Identification and characterization of a family of Rab11-interacting
RT proteins.";
RL J. Biol. Chem. 276:39067-39075(2001).
RN [8]
RP IDENTIFICATION IN THE CART COMPLEX.
RX PubMed=15772161; DOI=10.1091/mbc.e04-11-1014;
RA Yan Q., Sun W., Kujala P., Lotfi Y., Vida T.A., Bean A.J.;
RT "CART: an Hrs/actinin-4/BERP/myosin V protein complex required for
RT efficient receptor recycling.";
RL Mol. Biol. Cell 16:2470-2482(2005).
RN [9]
RP FUNCTION, INTERACTION WITH RAB11A, AND IDENTIFICATION IN A COMPLEX WITH
RP RAB11A AND CFTR.
RX PubMed=17462998; DOI=10.1074/jbc.m608531200;
RA Swiatecka-Urban A., Talebian L., Kanno E., Moreau-Marquis S.,
RA Coutermarsh B., Hansen K., Karlson K.H., Barnaby R., Cheney R.E.,
RA Langford G.M., Fukuda M., Stanton B.A.;
RT "Myosin Vb is required for trafficking of the cystic fibrosis transmembrane
RT conductance regulator in Rab11a-specific apical recycling endosomes in
RT polarized human airway epithelial cells.";
RL J. Biol. Chem. 282:23725-23736(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP FUNCTION, AND INTERACTION WITH NPC1L1.
RX PubMed=19542231; DOI=10.1074/jbc.m109.034355;
RA Chu B.-B., Ge L., Xie C., Zhao Y., Miao H.-H., Wang J., Li B.-L.,
RA Song B.-L.;
RT "Requirement of myosin Vb.Rab11a.Rab11-FIP2 complex in cholesterol-
RT regulated translocation of NPC1L1 to the cell surface.";
RL J. Biol. Chem. 284:22481-22490(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1446, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP FUNCTION, VARIANTS DIAR2 ARG-316; SER-456; ARG-514 AND LEU-660, AND VARIANT
RP VAL-1688.
RX PubMed=21206382; DOI=10.1097/mpg.0b013e3181eea177;
RA Szperl A.M., Golachowska M.R., Bruinenberg M., Prekeris R.,
RA Thunnissen A.M., Karrenbeld A., Dijkstra G., Hoekstra D., Mercer D.,
RA Ksiazyk J., Wijmenga C., Wapenaar M.C., Rings E.H., van Ijzendoorn S.C.;
RT "Functional characterization of mutations in the myosin Vb gene associated
RT with microvillus inclusion disease.";
RL J. Pediatr. Gastroenterol. Nutr. 52:307-313(2011).
RN [14]
RP FUNCTION, INTERACTION WITH RAB11A AND RAB8A, AND MUTAGENESIS OF GLN-1300;
RP TYR-1307; TYR-1714 AND GLN-1748.
RX PubMed=21282656; DOI=10.1073/pnas.1010754108;
RA Roland J.T., Bryant D.M., Datta A., Itzen A., Mostov K.E., Goldenring J.R.;
RT "Rab GTPase-Myo5B complexes control membrane recycling and epithelial
RT polarization.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:2789-2794(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 3), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [16]
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).
RN [17]
RP VARIANT DIAR2 LEU-660.
RX PubMed=19006234; DOI=10.1002/ajmg.a.32605;
RA Erickson R.P., Larson-Thome K., Valenzuela R.K., Whitaker S.E., Shub M.D.;
RT "Navajo microvillous inclusion disease is due to a mutation in MYO5B.";
RL Am. J. Med. Genet. A 146A:3117-3119(2008).
RN [18]
RP VARIANTS DIAR2 GLY-108; HIS-219 AND CYS-656.
RX PubMed=18724368; DOI=10.1038/ng.225;
RA Mueller T., Hess M.W., Schiefermeier N., Pfaller K., Ebner H.L.,
RA Heinz-Erian P., Ponstingl H., Partsch J., Roellinghoff B., Koehler H.,
RA Berger T., Lenhartz H., Schlenck B., Houwen R.J., Taylor C.J., Zoller H.,
RA Lechner S., Goulet O., Utermann G., Ruemmele F.M., Huber L.A.,
RA Janecke A.R.;
RT "MYO5B mutations cause microvillus inclusion disease and disrupt epithelial
RT cell polarity.";
RL Nat. Genet. 40:1163-1165(2008).
RN [19]
RP VARIANTS DIAR2 GLU-143; ARG-168; HIS-401; ARG-435 AND ARG-1556.
RX PubMed=20186687; DOI=10.1002/humu.21224;
RA Ruemmele F.M., Muller T., Schiefermeier N., Ebner H.L., Lechner S.,
RA Pfaller K., Thoni C.E., Goulet O., Lacaille F., Schmitz J., Colomb V.,
RA Sauvat F., Revillon Y., Canioni D., Brousse N., de Saint-Basile G.,
RA Lefebvre J., Heinz-Erian P., Enninger A., Utermann G., Hess M.W.,
RA Janecke A.R., Huber L.A.;
RT "Loss-of-function of MYO5B is the main cause of microvillus inclusion
RT disease: 15 novel mutations and a CaCo-2 RNAi cell model.";
RL Hum. Mutat. 31:544-551(2010).
RN [20]
RP VARIANTS DIAR2 SER-538 AND PHE-550.
RX PubMed=24138727; DOI=10.1111/tra.12131;
RA Thoeni C.E., Vogel G.F., Tancevski I., Geley S., Lechner S., Pfaller K.,
RA Hess M.W., Muller T., Janecke A.R., Avitzur Y., Muise A., Cutz E.,
RA Huber L.A.;
RT "Microvillus inclusion disease: loss of Myosin vb disrupts intracellular
RT traffic and cell polarity.";
RL Traffic 15:22-42(2014).
RN [21]
RP VARIANT DIAR2 LEU-660, AND CHARACTERIZATION OF VARIANT DIAR2 LEU-660.
RX PubMed=24892806; DOI=10.1172/jci71651;
RA Knowles B.C., Roland J.T., Krishnan M., Tyska M.J., Lapierre L.A.,
RA Dickman P.S., Goldenring J.R., Shub M.D.;
RT "Myosin Vb uncoupling from RAB8A and RAB11A elicits microvillus inclusion
RT disease.";
RL J. Clin. Invest. 124:2947-2962(2014).
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:0000269|PubMed:21206382,
CC ECO:0000269|PubMed:21282656}.
CC -!- SUBUNIT: Component of the CART complex, at least composed of ACTN4,
CC HGS/HRS, MYO5B and TRIM3. Interacts with RAB11FIP2, RAB11A, and RAB8A.
CC Found in a complex with CFTR and RAB11A. Interacts with NPC1L1;
CC (PubMed:19542231). Interacts with LIMA1 (PubMed:29880681).
CC {ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:15772161,
CC ECO:0000269|PubMed:17462998, ECO:0000269|PubMed:19542231,
CC ECO:0000269|PubMed:21282656, ECO:0000269|PubMed:29880681}.
CC -!- INTERACTION:
CC Q9ULV0; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-311356, EBI-10187270;
CC Q9ULV0; Q12982: BNIP2; NbExp=5; IntAct=EBI-311356, EBI-752094;
CC Q9ULV0; P15884: TCF4; NbExp=3; IntAct=EBI-311356, EBI-533224;
CC Q9ULV0; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-311356, EBI-2130429;
CC Q9ULV0-2; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-14093244, EBI-746752;
CC Q9ULV0-2; Q12982: BNIP2; NbExp=3; IntAct=EBI-14093244, EBI-752094;
CC Q9ULV0-2; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-14093244, EBI-2349927;
CC Q9ULV0-2; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-14093244, EBI-745689;
CC Q9ULV0-2; Q96IK5: GMCL1; NbExp=3; IntAct=EBI-14093244, EBI-2548508;
CC Q9ULV0-2; A8MW99: MEI4; NbExp=3; IntAct=EBI-14093244, EBI-19944212;
CC Q9ULV0-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-14093244, EBI-16439278;
CC Q9ULV0-2; P62491: RAB11A; NbExp=3; IntAct=EBI-14093244, EBI-745098;
CC Q9ULV0-2; Q15907: RAB11B; NbExp=3; IntAct=EBI-14093244, EBI-722234;
CC Q9ULV0-2; P57735: RAB25; NbExp=3; IntAct=EBI-14093244, EBI-1050500;
CC Q9ULV0-2; P15884-3: TCF4; NbExp=3; IntAct=EBI-14093244, EBI-13636688;
CC Q9ULV0-2; O75382: TRIM3; NbExp=3; IntAct=EBI-14093244, EBI-2129889;
CC Q9ULV0-2; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-14093244, EBI-2130429;
CC Q9ULV0-2; O43257: ZNHIT1; NbExp=3; IntAct=EBI-14093244, EBI-347522;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P70569}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ULV0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULV0-2; Sequence=VSP_056199, VSP_056200;
CC Name=3;
CC IsoId=Q9ULV0-3; Sequence=VSP_056198;
CC -!- DISEASE: Diarrhea 2, with microvillus atrophy (DIAR2) [MIM:251850]: A
CC disease characterized by onset of intractable life-threatening watery
CC diarrhea during infancy. Two forms are recognized: early-onset
CC microvillus inclusion disease with diarrhea beginning in the neonatal
CC period, and late-onset, with first symptoms appearing after 3 or 4
CC months of life. {ECO:0000269|PubMed:18724368,
CC ECO:0000269|PubMed:19006234, ECO:0000269|PubMed:20186687,
CC ECO:0000269|PubMed:21206382, ECO:0000269|PubMed:24138727,
CC ECO:0000269|PubMed:24892806}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86433.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB032945; BAA86433.2; ALT_INIT; mRNA.
DR EMBL; AK025336; BAB15114.1; -; mRNA.
DR EMBL; AB290160; BAG06714.1; -; mRNA.
DR EMBL; AC090227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC105224; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033527; AAH33527.1; -; mRNA.
DR CCDS; CCDS42436.1; -. [Q9ULV0-1]
DR RefSeq; NP_001073936.1; NM_001080467.2. [Q9ULV0-1]
DR PDB; 4J5M; X-ray; 2.07 A; A=1453-1848.
DR PDB; 4LNZ; X-ray; 3.11 A; A=1460-1848.
DR PDB; 4LWZ; X-ray; 2.55 A; B/D=1456-1848.
DR PDB; 4LX0; X-ray; 2.19 A; B/D=1456-1848.
DR PDBsum; 4J5M; -.
DR PDBsum; 4LNZ; -.
DR PDBsum; 4LWZ; -.
DR PDBsum; 4LX0; -.
DR AlphaFoldDB; Q9ULV0; -.
DR SMR; Q9ULV0; -.
DR BioGRID; 110729; 96.
DR CORUM; Q9ULV0; -.
DR IntAct; Q9ULV0; 59.
DR MINT; Q9ULV0; -.
DR STRING; 9606.ENSP00000285039; -.
DR iPTMnet; Q9ULV0; -.
DR PhosphoSitePlus; Q9ULV0; -.
DR SwissPalm; Q9ULV0; -.
DR BioMuta; MYO5B; -.
DR DMDM; 296439293; -.
DR EPD; Q9ULV0; -.
DR jPOST; Q9ULV0; -.
DR MassIVE; Q9ULV0; -.
DR MaxQB; Q9ULV0; -.
DR PaxDb; Q9ULV0; -.
DR PeptideAtlas; Q9ULV0; -.
DR PRIDE; Q9ULV0; -.
DR ProteomicsDB; 81062; -.
DR ProteomicsDB; 85128; -. [Q9ULV0-1]
DR Antibodypedia; 49571; 98 antibodies from 25 providers.
DR DNASU; 4645; -.
DR Ensembl; ENST00000285039.12; ENSP00000285039.6; ENSG00000167306.20. [Q9ULV0-1]
DR Ensembl; ENST00000592688.1; ENSP00000466368.1; ENSG00000167306.20. [Q9ULV0-3]
DR GeneID; 4645; -.
DR KEGG; hsa:4645; -.
DR MANE-Select; ENST00000285039.12; ENSP00000285039.6; NM_001080467.3; NP_001073936.1.
DR UCSC; uc002ldz.4; human. [Q9ULV0-1]
DR CTD; 4645; -.
DR DisGeNET; 4645; -.
DR GeneCards; MYO5B; -.
DR HGNC; HGNC:7603; MYO5B.
DR HPA; ENSG00000167306; Tissue enhanced (intestine).
DR MalaCards; MYO5B; -.
DR MIM; 251850; phenotype.
DR MIM; 606540; gene.
DR neXtProt; NX_Q9ULV0; -.
DR OpenTargets; ENSG00000167306; -.
DR Orphanet; 2290; Microvillus inclusion disease.
DR Orphanet; 480491; MYO5B-related progressive familial intrahepatic cholestasis.
DR Orphanet; 79306; Progressive familial intrahepatic cholestasis type 1.
DR PharmGKB; PA31408; -.
DR VEuPathDB; HostDB:ENSG00000167306; -.
DR eggNOG; KOG0160; Eukaryota.
DR GeneTree; ENSGT00940000155402; -.
DR HOGENOM; CLU_000192_9_1_1; -.
DR InParanoid; Q9ULV0; -.
DR OMA; GKQNEHC; -.
DR PhylomeDB; Q9ULV0; -.
DR TreeFam; TF328771; -.
DR PathwayCommons; Q9ULV0; -.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR SignaLink; Q9ULV0; -.
DR BioGRID-ORCS; 4645; 7 hits in 1070 CRISPR screens.
DR ChiTaRS; MYO5B; human.
DR GeneWiki; MYO5B; -.
DR GenomeRNAi; 4645; -.
DR Pharos; Q9ULV0; Tbio.
DR PRO; PR:Q9ULV0; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; Q9ULV0; protein.
DR Bgee; ENSG00000167306; Expressed in ileal mucosa and 152 other tissues.
DR ExpressionAtlas; Q9ULV0; baseline and differential.
DR Genevisible; Q9ULV0; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0045179; C:apical cortex; IDA:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IPI:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0003091; P:renal water homeostasis; TAS:Reactome.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProtKB.
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 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW ATP-binding; Calmodulin-binding; Coiled coil; Cytoplasm; Disease variant;
KW Motor protein; Myosin; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT CHAIN 1..1848
FT /note="Unconventional myosin-Vb"
FT /id="PRO_0000123460"
FT DOMAIN 8..60
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 69..761
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 769..798
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 792..821
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 817..848
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 840..869
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 865..896
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 888..917
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 1526..1803
FT /note="Dilute"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00503"
FT REGION 21..40
FT /note="Requires for interaction with LIMA1"
FT /evidence="ECO:0000269|PubMed:29880681"
FT REGION 596..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..662
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 1093..1123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1166..1192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 899..1266
FT /evidence="ECO:0000255"
FT COILED 1341..1471
FT /evidence="ECO:0000255"
FT COMPBIAS 1095..1123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1183
FT /note="Basic and acidic 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 1446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..1430
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056198"
FT VAR_SEQ 1..859
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056199"
FT VAR_SEQ 1315..1340
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056200"
FT VARIANT 10
FT /note="C -> G (in dbSNP:rs16951438)"
FT /id="VAR_056182"
FT VARIANT 108
FT /note="V -> G (in DIAR2; dbSNP:rs121908103)"
FT /evidence="ECO:0000269|PubMed:18724368"
FT /id="VAR_054993"
FT VARIANT 126
FT /note="T -> A (in dbSNP:rs1815930)"
FT /evidence="ECO:0000269|PubMed:10574461, ECO:0000269|Ref.4"
FT /id="VAR_063141"
FT VARIANT 143
FT /note="A -> E (in DIAR2)"
FT /evidence="ECO:0000269|PubMed:20186687"
FT /id="VAR_071649"
FT VARIANT 168
FT /note="G -> R (in DIAR2; dbSNP:rs1324907355)"
FT /evidence="ECO:0000269|PubMed:20186687"
FT /id="VAR_071650"
FT VARIANT 219
FT /note="R -> H (in DIAR2; dbSNP:rs1053713532)"
FT /evidence="ECO:0000269|PubMed:18724368"
FT /id="VAR_054994"
FT VARIANT 307
FT /note="K -> N (in dbSNP:rs17659179)"
FT /id="VAR_056183"
FT VARIANT 316
FT /note="G -> R (in DIAR2; dbSNP:rs753558336)"
FT /evidence="ECO:0000269|PubMed:21206382"
FT /id="VAR_071651"
FT VARIANT 401
FT /note="R -> H (in DIAR2; dbSNP:rs1555648414)"
FT /evidence="ECO:0000269|PubMed:20186687"
FT /id="VAR_071652"
FT VARIANT 435
FT /note="G -> R (in DIAR2; dbSNP:rs1283622290)"
FT /evidence="ECO:0000269|PubMed:20186687"
FT /id="VAR_071653"
FT VARIANT 456
FT /note="N -> S (in DIAR2)"
FT /evidence="ECO:0000269|PubMed:21206382"
FT /id="VAR_071654"
FT VARIANT 514
FT /note="C -> R (in DIAR2)"
FT /evidence="ECO:0000269|PubMed:21206382"
FT /id="VAR_071655"
FT VARIANT 538
FT /note="F -> S (in DIAR2; found in a compound heterozygote
FT also carrying F-550; enterocytes carrying S-538 and F-550
FT display disruption of cell polarity, mislocalized apical
FT and basolateral transporter proteins and altered
FT distribution of endosomal/lysosomal constituents including
FT Rab GTPases)"
FT /evidence="ECO:0000269|PubMed:24138727"
FT /id="VAR_072814"
FT VARIANT 550
FT /note="I -> F (in DIAR2; found in a compound heterozygote
FT also carrying S-538; enterocytes carrying S-538 and F-550
FT display disruption of cell polarity, mislocalized apical
FT and basolateral transporter proteins and altered
FT distribution of endosomal/lysosomal constituents including
FT Rab GTPases)"
FT /evidence="ECO:0000269|PubMed:24138727"
FT /id="VAR_072815"
FT VARIANT 656
FT /note="R -> C (in DIAR2; dbSNP:rs121908105)"
FT /evidence="ECO:0000269|PubMed:18724368"
FT /id="VAR_054995"
FT VARIANT 660
FT /note="P -> L (in DIAR2; patient enterocytes show
FT alterations in junctional composition, loss of polarity in
FT basolateral and apical compartments, loss of apical brush
FT border and formation of microvillus inclusions in cells at
FT the villus tips; the mutation causes the motor to move
FT slowly along F-actin; dbSNP:rs121908106)"
FT /evidence="ECO:0000269|PubMed:19006234,
FT ECO:0000269|PubMed:21206382, ECO:0000269|PubMed:24892806"
FT /id="VAR_071656"
FT VARIANT 918
FT /note="R -> H (in dbSNP:rs2298624)"
FT /id="VAR_056184"
FT VARIANT 942
FT /note="K -> R (in dbSNP:rs2277716)"
FT /id="VAR_056185"
FT VARIANT 1055
FT /note="L -> LL (in dbSNP:rs72530399)"
FT /evidence="ECO:0000269|PubMed:10574461, ECO:0000269|Ref.4"
FT /id="VAR_063142"
FT VARIANT 1556
FT /note="L -> R (in DIAR2)"
FT /evidence="ECO:0000269|PubMed:20186687"
FT /id="VAR_071657"
FT VARIANT 1688
FT /note="M -> V (in dbSNP:rs112417235)"
FT /evidence="ECO:0000269|PubMed:21206382"
FT /id="VAR_071658"
FT MUTAGEN 1300
FT /note="Q->L: Abolishes interaction with RAB8A and has no
FT effect on RAB11A interaction; when associated with C-1307."
FT /evidence="ECO:0000269|PubMed:21282656"
FT MUTAGEN 1307
FT /note="Y->C: Abolishes interaction with RAB8A and has no
FT effect on RAB11A interaction; when associated with L-1300."
FT /evidence="ECO:0000269|PubMed:21282656"
FT MUTAGEN 1714
FT /note="Y->E: Abolishes interaction with RAB11A; has no
FT effect on RAB8A interaction."
FT /evidence="ECO:0000269|PubMed:21282656"
FT MUTAGEN 1748
FT /note="Q->R: Abolishes interaction with RAB11A; has no
FT effect on RAB8A interaction."
FT /evidence="ECO:0000269|PubMed:21282656"
FT STRAND 1468..1471
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1474..1476
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1477..1484
FT /evidence="ECO:0007829|PDB:4J5M"
FT TURN 1485..1487
FT /evidence="ECO:0007829|PDB:4LX0"
FT HELIX 1490..1493
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1500..1514
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1518..1538
FT /evidence="ECO:0007829|PDB:4J5M"
FT TURN 1539..1541
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1543..1562
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1567..1569
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1575..1578
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1588..1613
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1614..1616
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1617..1622
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1654..1670
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1675..1699
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1701..1703
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1706..1725
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1729..1731
FT /evidence="ECO:0007829|PDB:4LNZ"
FT HELIX 1733..1736
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1738..1746
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1754..1763
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1769..1778
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1791..1800
FT /evidence="ECO:0007829|PDB:4J5M"
FT TURN 1801..1803
FT /evidence="ECO:0007829|PDB:4J5M"
FT HELIX 1831..1833
FT /evidence="ECO:0007829|PDB:4LX0"
FT HELIX 1838..1840
FT /evidence="ECO:0007829|PDB:4J5M"
FT STRAND 1845..1848
FT /evidence="ECO:0007829|PDB:4J5M"
FT MOD_RES Q9ULV0-3:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 1848 AA; 213672 MW; 4EB8FA02F6B38707 CRC64;
MSVGELYSQC TRVWIPDPDE VWRSAELTKD YKEGDKSLQL RLEDETILEY PIDVQRNQLP
FLRNPDILVG ENDLTALSYL HEPAVLHNLK VRFLESNHIY TYCGIVLVAI NPYEQLPIYG
QDVIYTYSGQ NMGDMDPHIF AVAEEAYKQM ARDEKNQSII VSGESGAGKT VSAKYAMRYF
ATVGGSASET NIEEKVLASS PIMEAIGNAK TTRNDNSSRF GKYIQIGFDK RYHIIGANMR
TYLLEKSRVV FQADDERNYH IFYQLCAAAG LPEFKELALT SAEDFFYTSQ GGDTSIEGVD
DAEDFEKTRQ AFTLLGVKES HQMSIFKIIA SILHLGSVAI QAERDGDSCS ISPQDVYLSN
FCRLLGVEHS QMEHWLCHRK LVTTSETYVK TMSLQQVINA RNALAKHIYA QLFGWIVEHI
NKALHTSLKQ HSFIGVLDIY GFETFEVNSF EQFCINYANE KLQQQFNSHV FKLEQEEYMK
EQIPWTLIDF YDNQPCIDLI EAKLGILDLL DEECKVPKGT DQNWAQKLYD RHSSSQHFQK
PRMSNTAFII VHFADKVEYL SDGFLEKNRD TVYEEQINIL KASKFPLVAD LFHDDKDPVP
ATTPGKGSSS KISVRSARPP MKVSNKEHKK TVGHQFRTSL HLLMETLNAT TPHYVRCIKP
NDEKLPFHFD PKRAVQQLRA CGVLETIRIS AAGYPSRWAY HDFFNRYRVL VKKRELANTD
KKAICRSVLE NLIKDPDKFQ FGRTKIFFRA GQVAYLEKLR ADKFRTATIM IQKTVRGWLQ
KVKYHRLKGA TLTLQRYCRG HLARRLAEHL RRIRAAVVLQ KHYRMQRARQ AYQRVRRAAV
VIQAFTRAMF VRRTYRQVLM EHKATTIQKH VRGWMARRHF QRLRDAAIVI QCAFRMLKAR
RELKALRIEA RSAEHLKRLN VGMENKVVQL QRKIDEQNKE FKTLSEQLSV TTSTYTMEVE
RLKKELVHYQ QSPGEDTSLR LQEEVESLRT ELQRAHSERK ILEDAHSREK DELRKRVADL
EQENALLKDE KEQLNNQILC QSKDEFAQNS VKENLMKKEL EEERSRYQNL VKEYSQLEQR
YDNLRDEMTI IKQTPGHRRN PSNQSSLESD SNYPSISTSE IGDTEDALQQ VEEIGLEKAA
MDMTVFLKLQ KRVRELEQER KKLQVQLEKR EQQDSKKVQA EPPQTDIDLD PNADLAYNSL
KRQELESENK KLKNDLNELR KAVADQATQN NSSHGSPDSY SLLLNQLKLA HEELEVRKEE
VLILRTQIVS ADQRRLAGRN AEPNINARSS WPNSEKHVDQ EDAIEAYHGV CQTNSKTEDW
GYLNEDGELG LAYQGLKQVA RLLEAQLQAQ SLEHEEEVEH LKAQLEALKE EMDKQQQTFC
QTLLLSPEAQ VEFGVQQEIS RLTNENLDLK ELVEKLEKNE RKLKKQLKIY MKKAQDLEAA
QALAQSERKR HELNRQVTVQ RKEKDFQGML EYHKEDEALL IRNLVTDLKP QMLSGTVPCL
PAYILYMCIR HADYTNDDLK VHSLLTSTIN GIKKVLKKHN DDFEMTSFWL SNTCRLLHCL
KQYSGDEGFM TQNTAKQNEH CLKNFDLTEY RQVLSDLSIQ IYQQLIKIAE GVLQPMIVSA
MLENESIQGL SGVKPTGYRK RSSSMADGDN SYCLEAIIRQ MNAFHTVMCD QGLDPEIILQ
VFKQLFYMIN AVTLNNLLLR KDVCSWSTGM QLRYNISQLE EWLRGRNLHQ SGAVQTMEPL
IQAAQLLQLK KKTQEDAEAI CSLCTSLSTQ QIVKILNLYT PLNEFEERVT VAFIRTIQAQ
LQERNDPQQL LLDAKHMFPV LFPFNPSSLT MDSIHIPACL NLEFLNEV
