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 27-MAR-2024, entry version 207. 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). RN [22] RP VARIANTS PFIC10 CYS-92; CYS-119; THR-500; PRO-642; TRP-799 AND CYS-824, AND RP INVOLVEMENT IN PFIC10. RX PubMed=27532546; DOI=10.1002/hep.28779; RA Gonzales E., Taylor S.A., Davit-Spraul A., Thebaut A., Thomassin N., RA Guettier C., Whitington P.F., Jacquemin E.; RT "MYO5B mutations cause cholestasis with normal serum gamma-glutamyl RT transferase activity in children without microvillous inclusion disease."; RL Hepatology 65:164-173(2017). RN [23] RP VARIANTS PFIC10 PHE-158; ARG-266; 341-GLN--VAL-1848 DEL; CYS-401; ASN-535; RP ASN-583; CYS-824; SER-934; 1016-ARG--VAL-1848 DEL AND HIS-1079, FUNCTION, RP INVOLVEMENT IN PFIC10, AND CHARACTERIZATION OF VARIANT PFIC10 ARG-266. RX PubMed=28027573; DOI=10.1002/hep.29020; RA Qiu Y.L., Gong J.Y., Feng J.Y., Wang R.X., Han J., Liu T., Lu Y., Li L.T., RA Zhang M.H., Sheps J.A., Wang N.L., Yan Y.Y., Li J.Q., Chen L., RA Borchers C.H., Sipos B., Knisely A.S., Ling V., Xing Q.H., Wang J.S.; RT "Defects in myosin VB are associated with a spectrum of previously RT undiagnosed low gamma-glutamyltransferase cholestasis."; RL Hepatology 65:1655-1669(2017). RN [24] RP VARIANTS DIAR2 LYS-82 AND 1016-ARG--VAL-1848 DEL, AND VARIANTS PFIC10 RP CYS-92; THR-392; THR-488 AND CYS-824. RX PubMed=32304554; DOI=10.1097/mpg.0000000000002740; RA Cockar I., Foskett P., Strautnieks S., Clinch Y., Fustok J., Rahman O., RA Sutton H., Mtegha M., Fessatou S., Kontaki E., Papaevangelou V., RA Deheragoda M., Thompson R.J., Grammatikopoulos T.; RT "Mutations in myosin 5B in children with early-onset cholestasis."; RL J. Pediatr. Gastroenterol. Nutr. 71:184-188(2020). RN [25] RP VARIANTS PFIC10 CYS-92; LEU-557 AND 1375-GLN--VAL-1848 DEL, AND VARIANTS RP DIAR2 ARG-81; LYS-82; 149-GLN--VAL-1848 DEL; VAL-316; ARG-336; RP 363-ARG--VAL-1848 DEL; THR-392; ASN-416; GLY-492; PHE-497; RP 526-GLN--VAL-1848 DEL; 574-GLU--VAL-1848 DEL; PRO-580; CYS-656; RP 672-LYS--VAL-1848 DEL; MET-686; 749-ARG--VAL-1848 DEL; 1016-ARG--VAL-1848 RP DEL; 1064-ARG--VAL-1848 DEL; 1172-GLN--VAL-1848 DEL; PRO-1361; RP 1467-GLN--VAL-1848 DEL; 1600-GLN--VAL-1848 DEL AND 1795-ARG--VAL-1848 DEL. RX PubMed=33525641; DOI=10.3390/jcm10030481; RA Aldrian D., Vogel G.F., Frey T.K., Ayyildiz Civan H., Aksu A.U., RA Avitzur Y., Ramos Boluda E., Cakir M., Demir A.M., Deppisch C., Duba H.C., RA Dueker G., Gerner P., Hertecant J., Hornova J., Kathemann S., RA Koeglmeier J., Koutroumpa A., Lanzersdorfer R., Lev-Tzion R., Lima R., RA Mansour S., Meissl M., Melek J., Miqdady M., Montoya J.H., Posovszky C., RA Rachman Y., Siahanidou T., Tabbers M., Uhlig H.H., Uenal S., Wirth S., RA Ruemmele F.M., Hess M.W., Huber L.A., Mueller T., Sturm E., Janecke A.R.; RT "Congenital diarrhea and cholestatic liver disease: phenotypic spectrum RT associated with MYO5B mutations."; RL J. Clin. Med. 10:0-0(2021). RN [26] RP VARIANTS PFIC10 CYS-92; 252-GLN--VAL-1848 DEL; LEU-517; CYS-654 AND RP CYS-824. RX PubMed=35129155; DOI=10.1097/mpg.0000000000003399; RA Matarazzo L., Bianco A.M., Athanasakis E., Serveres M., Francalanci P., RA Cenacchi G., Maggiore G., D'Adamo A.P.; RT "MYO5B gene mutations: a not negligible cause of intrahepatic cholestasis RT of infancy with normal gamma-glutamyl transferase phenotype."; RL J. Pediatr. Gastroenterol. Nutr. 74:e115-e121(2022). RN [27] RP VARIANTS DIAR2 HIS-219; 536-GLN--VAL-1848 DEL AND 874-TRP--VAL-1848 DEL. RX PubMed=34816459; DOI=10.1002/pd.6068; RA Lu J., Qi Y., Ding H., Yin A.; RT "Two cases of microvillus inclusion disease caused by MYO5B deficiency with RT prenatal abnormalities."; RL Prenat. Diagn. 42:136-140(2022). 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. Required for proper localization of bile salt export pump CC ABCB11 at the apical/canalicular plasma membrane of hepatocytes CC (PubMed:34816459). {ECO:0000269|PubMed:21206382, CC ECO:0000269|PubMed:21282656, ECO:0000269|PubMed:34816459}. 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; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-14093244, EBI-745689; 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; 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, with or without CC cholestasis (DIAR2) [MIM:251850]: A disease characterized by onset of CC intractable life-threatening watery diarrhea during infancy. Two forms CC are recognized: early-onset microvillus inclusion disease with diarrhea CC beginning in the neonatal period, and late-onset, with first symptoms CC appearing after 3 or 4 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, ECO:0000269|PubMed:32304554, CC ECO:0000269|PubMed:33525641, ECO:0000269|PubMed:34816459}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Cholestasis, progressive familial intrahepatic, 10 (PFIC10) CC [MIM:619868]: A form of progressive cholestasis, a disorder CC characterized by early onset of cholestasis that progresses to hepatic CC fibrosis, cirrhosis, and end-stage liver disease. PFIC10 is an CC autosomal recessive form with highly variable phenotype and severity, CC manifesting in the first months or years of life. CC {ECO:0000269|PubMed:27532546, ECO:0000269|PubMed:28027573, CC ECO:0000269|PubMed:32304554, ECO:0000269|PubMed:33525641, CC ECO:0000269|PubMed:35129155}. 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; 108. DR CORUM; Q9ULV0; -. DR IntAct; Q9ULV0; 60. 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; 9606-ENSP00000285039; -. DR PeptideAtlas; Q9ULV0; -. DR ProteomicsDB; 81062; -. DR ProteomicsDB; 85128; -. [Q9ULV0-1] DR Pumba; Q9ULV0; -. DR Antibodypedia; 49571; 105 antibodies from 25 providers. DR DNASU; 4645; -. DR Ensembl; ENST00000285039.12; ENSP00000285039.6; ENSG00000167306.21. [Q9ULV0-1] DR Ensembl; ENST00000592688.1; ENSP00000466368.1; ENSG00000167306.21. [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 AGR; HGNC:7603; -. 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 MIM; 619868; phenotype. 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; KVQDLEX; -. DR OrthoDB; 1094820at2759; -. 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; 8 hits in 1148 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 154 other cell types or tissues. DR ExpressionAtlas; Q9ULV0; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central. DR GO; GO:0045179; C:apical cortex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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:0031982; C:vesicle; IBA:GO_Central. 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; 1.10.10.820; -; 1. DR Gene3D; 1.20.5.190; -; 3. DR Gene3D; 1.20.58.530; -; 1. DR Gene3D; 6.20.240.20; -; 1. DR Gene3D; 3.40.850.10; Kinesin motor domain; 1. DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 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 PANTHER; PTHR13140; MYOSIN; 1. DR PANTHER; PTHR13140:SF706; MYOSIN-11; 1. 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; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51126; DILUTE; 1. DR PROSITE; PS50096; IQ; 6. DR PROSITE; PS51456; MYOSIN_MOTOR; 1. DR PROSITE; PS51844; SH3_LIKE; 1. DR Genevisible; Q9ULV0; HS. 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 Intrahepatic cholestasis; Motor protein; Myosin; Nucleotide-binding; KW Phosphoprotein; 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 81 FT /note="H -> R (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087245" FT VARIANT 82 FT /note="E -> K (in DIAR2)" FT /evidence="ECO:0000269|PubMed:32304554, FT ECO:0000269|PubMed:33525641" FT /id="VAR_087246" FT VARIANT 92 FT /note="R -> C (in PFIC10)" FT /evidence="ECO:0000269|PubMed:27532546, FT ECO:0000269|PubMed:32304554, ECO:0000269|PubMed:33525641, FT ECO:0000269|PubMed:35129155" FT /id="VAR_087247" FT VARIANT 108 FT /note="V -> G (in DIAR2; dbSNP:rs121908103)" FT /evidence="ECO:0000269|PubMed:18724368" FT /id="VAR_054993" FT VARIANT 119 FT /note="Y -> C (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27532546" FT /id="VAR_087248" 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 149..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087249" FT VARIANT 158 FT /note="S -> F (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28027573" FT /id="VAR_087250" 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 ECO:0000269|PubMed:34816459" FT /id="VAR_054994" FT VARIANT 252..1848 FT /note="Missing (in PFIC10)" FT /evidence="ECO:0000269|PubMed:35129155" FT /id="VAR_087251" FT VARIANT 266 FT /note="C -> R (in PFIC10; decreased ABCB11 targeting to the FT apical/canalicular plasma membrane in hepatocytes from a FT homozygous patient)" FT /evidence="ECO:0000269|PubMed:28027573" FT /id="VAR_087252" 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 316 FT /note="G -> V (in DIAR2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087253" FT VARIANT 336 FT /note="G -> R (in DIAR2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087254" FT VARIANT 341..1848 FT /note="Missing (in PFIC10)" FT /evidence="ECO:0000269|PubMed:28027573" FT /id="VAR_087255" FT VARIANT 363..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087256" FT VARIANT 392 FT /note="M -> T (in PFIC10 and DIAR2)" FT /evidence="ECO:0000269|PubMed:32304554, FT ECO:0000269|PubMed:33525641" FT /id="VAR_087257" FT VARIANT 401 FT /note="R -> C (in PFIC10)" FT /evidence="ECO:0000269|PubMed:28027573" FT /id="VAR_087258" FT VARIANT 401 FT /note="R -> H (in DIAR2; dbSNP:rs1555648414)" FT /evidence="ECO:0000269|PubMed:20186687" FT /id="VAR_071652" FT VARIANT 416 FT /note="I -> N (in DIAR2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087259" 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 488 FT /note="I -> T (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:32304554" FT /id="VAR_087260" FT VARIANT 492 FT /note="D -> G (in DIAR2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087261" FT VARIANT 497 FT /note="I -> F (in DIAR2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087262" FT VARIANT 500 FT /note="I -> T (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27532546" FT /id="VAR_087263" FT VARIANT 514 FT /note="C -> R (in DIAR2)" FT /evidence="ECO:0000269|PubMed:21206382" FT /id="VAR_071655" FT VARIANT 517 FT /note="P -> L (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:35129155" FT /id="VAR_087264" FT VARIANT 526..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087265" FT VARIANT 535 FT /note="S -> N (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28027573" FT /id="VAR_087266" FT VARIANT 536..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:34816459" FT /id="VAR_087267" 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 557 FT /note="V -> L (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087268" FT VARIANT 574..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087269" FT VARIANT 580 FT /note="L -> P (in DIAR2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087270" FT VARIANT 583 FT /note="S -> N (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28027573" FT /id="VAR_087271" FT VARIANT 642 FT /note="L -> P (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27532546" FT /id="VAR_087272" FT VARIANT 654 FT /note="Y -> C (in PFIC10)" FT /evidence="ECO:0000269|PubMed:35129155" FT /id="VAR_087273" FT VARIANT 656 FT /note="R -> C (in DIAR2; dbSNP:rs121908105)" FT /evidence="ECO:0000269|PubMed:18724368, FT ECO:0000269|PubMed:33525641" 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 672..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087274" FT VARIANT 686 FT /note="T -> M (in DIAR2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087275" FT VARIANT 749..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087276" FT VARIANT 799 FT /note="R -> W (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:27532546" FT /id="VAR_087277" FT VARIANT 824 FT /note="R -> C (in PFIC10)" FT /evidence="ECO:0000269|PubMed:27532546, FT ECO:0000269|PubMed:28027573, ECO:0000269|PubMed:32304554, FT ECO:0000269|PubMed:35129155" FT /id="VAR_087278" FT VARIANT 874..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:34816459" FT /id="VAR_087279" FT VARIANT 918 FT /note="R -> H (in dbSNP:rs2298624)" FT /id="VAR_056184" FT VARIANT 934 FT /note="I -> S (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28027573" FT /id="VAR_087280" FT VARIANT 942 FT /note="K -> R (in dbSNP:rs2277716)" FT /id="VAR_056185" FT VARIANT 1016..1848 FT /note="Missing (in DIAR2 and PFIC10)" FT /evidence="ECO:0000269|PubMed:28027573, FT ECO:0000269|PubMed:32304554, ECO:0000269|PubMed:33525641" FT /id="VAR_087281" 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 1064..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087282" FT VARIANT 1079 FT /note="Q -> H (in PFIC10; uncertain significance)" FT /evidence="ECO:0000269|PubMed:28027573" FT /id="VAR_087283" FT VARIANT 1172..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087284" FT VARIANT 1361 FT /note="L -> P (in DIAR2; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087285" FT VARIANT 1375..1848 FT /note="Missing (in PFIC10)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087286" FT VARIANT 1467..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087287" FT VARIANT 1556 FT /note="L -> R (in DIAR2)" FT /evidence="ECO:0000269|PubMed:20186687" FT /id="VAR_071657" FT VARIANT 1600..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087288" FT VARIANT 1688 FT /note="M -> V (in dbSNP:rs112417235)" FT /evidence="ECO:0000269|PubMed:21206382" FT /id="VAR_071658" FT VARIANT 1795..1848 FT /note="Missing (in DIAR2)" FT /evidence="ECO:0000269|PubMed:33525641" FT /id="VAR_087289" 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 //