ID PKHM2_HUMAN Reviewed; 1019 AA. AC Q8IWE5; O94928; Q5VT65; Q5VVD7; Q6NUH9; Q7L8G1; Q8IVT7; Q8N2T4; Q96AY0; AC Q9NTF7; DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 2. DT 27-MAR-2024, entry version 149. DE RecName: Full=Pleckstrin homology domain-containing family M member 2 {ECO:0000305}; DE Short=PH domain-containing family M member 2; DE AltName: Full=Salmonella-induced filaments A and kinesin-interacting protein {ECO:0000303|PubMed:22172677}; DE Short=SifA and kinesin-interacting protein {ECO:0000303|PubMed:22172677}; GN Name=PLEKHM2 {ECO:0000312|HGNC:HGNC:29131}; GN Synonyms=KIAA0842, SKIP {ECO:0000303|PubMed:22172677, GN ECO:0000303|PubMed:28325809}; 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]. RC TISSUE=Brain; RX PubMed=10048485; DOI=10.1093/dnares/5.6.355; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:355-364(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone, Cervix, Kidney, Ovary, and Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 824-1019. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIF5B AND SALMONELLA RP TYPHIMURIUM SIFA PROTEIN (MICROBIAL INFECTION). RX PubMed=15905402; DOI=10.1126/science.1110225; RA Boucrot E., Henry T., Borg J.-P., Gorvel J.-P., Meresse S.; RT "The intracellular fate of Salmonella depends on the recruitment of RT kinesin."; RL Science 308:1174-1178(2005). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [8] 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 [9] RP FUNCTION, INTERACTION WITH ARL8B, SUBCELLULAR LOCATION, ALTERNATIVE RP SPLICING, AND MUTAGENESIS OF 207-TRP-ASP-208 AND 236-TRP-GLU-237. RX PubMed=22172677; DOI=10.1016/j.devcel.2011.10.007; RA Rosa-Ferreira C., Munro S.; RT "Arl8 and SKIP act together to link lysosomes to kinesin-1."; RL Dev. Cell 21:1171-1178(2011). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS RP 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 [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] RP FUNCTION. RX PubMed=24088571; DOI=10.1091/mbc.e13-05-0259; RA Tuli A., Thiery J., James A.M., Michelet X., Sharma M., Garg S., RA Sanborn K.B., Orange J.S., Lieberman J., Brenner M.B.; RT "Arf-like GTPase Arl8b regulates lytic granule polarization and natural RT killer cell-mediated cytotoxicity."; RL Mol. Biol. Cell 24:3721-3735(2013). RN [13] RP FUNCTION, AND INTERACTION WITH BORCS5. RX PubMed=25898167; DOI=10.1016/j.devcel.2015.02.011; RA Pu J., Schindler C., Jia R., Jarnik M., Backlund P., Bonifacino J.S.; RT "BORC, a multisubunit complex that regulates lysosome positioning."; RL Dev. Cell 33:176-188(2015). RN [14] RP FUNCTION, INTERACTION WITH ARL8A AND ARL8B, AND SUBCELLULAR LOCATION. RX PubMed=28325809; DOI=10.1083/jcb.201607085; RA Marwaha R., Arya S.B., Jagga D., Kaur H., Tuli A., Sharma M.; RT "The Rab7 effector PLEKHM1 binds Arl8b to promote cargo traffic to RT lysosomes."; RL J. Cell Biol. 216:1051-1070(2017). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 773-884 IN COMPLEX WITH RP SALMONELLA TYPHIMURIUM SIFA PROTEIN (MICROBIAL INFECTION), AND MUTAGENESIS RP OF GLY-828; ARG-830; ARG-831 AND CYS-869. RX PubMed=18996344; DOI=10.1016/j.chom.2008.08.012; RA Ohlson M.B., Huang Z., Alto N.M., Blanc M.-P., Dixon J.E., Chai J., RA Miller S.I.; RT "Structure and function of Salmonella SifA indicate that its interactions RT with SKIP, SseJ, and RhoA family GTPases induce endosomal tubulation."; RL Cell Host Microbe 4:434-446(2008). CC -!- FUNCTION: Plays a role in lysosomes movement and localization at the CC cell periphery acting as an effector of ARL8B. Required for ARL8B to CC exert its effects on lysosome location, recruits kinesin-1 to lysosomes CC and hence direct their movement toward microtubule plus ends. Binding CC to ARL8B provides a link from lysosomal membranes to plus-end-directed CC motility (PubMed:28325809, PubMed:22172677, PubMed:25898167, CC PubMed:24088571). Critical factor involved in NK cell-mediated CC cytotoxicity. Drives the polarization of cytolytic granules and CC microtubule-organizing centers (MTOCs) toward the immune synapse CC between effector NK lymphocytes and target cells (PubMed:24088571). CC Required for maintenance of the Golgi apparatus organization CC (PubMed:22172677). May play a role in membrane tubulation CC (PubMed:15905402). {ECO:0000269|PubMed:15905402, CC ECO:0000269|PubMed:22172677, ECO:0000269|PubMed:24088571, CC ECO:0000269|PubMed:25898167, ECO:0000269|PubMed:28325809}. CC -!- SUBUNIT: Interacts with KLC2 (via TPR repeats) (Probable). Interacts CC with KIF5B (PubMed:15905402). Interacts with BORCS5 (PubMed:25898167). CC Interacts (via RUN domain) with ARL8B (GTP-bound form); PLEKHM1 and CC PLEKHM2 compete for interaction with ARL8B (PubMed:28325809, CC PubMed:22172677). Interacts with ARL8A (PubMed:28325809). CC {ECO:0000269|PubMed:15905402, ECO:0000269|PubMed:22172677, CC ECO:0000269|PubMed:25898167, ECO:0000269|PubMed:28325809, CC ECO:0000305|PubMed:22172677}. CC -!- SUBUNIT: (Microbial infection) Interacts with the S.typhimurium sifA CC protein; required for S.typhimurium infection. CC {ECO:0000269|PubMed:15905402, ECO:0000269|PubMed:18996344}. CC -!- INTERACTION: CC Q8IWE5; P51151: RAB9A; NbExp=4; IntAct=EBI-726484, EBI-4401353; CC Q8IWE5; Q91YS4: Klc2; Xeno; NbExp=4; IntAct=EBI-726484, EBI-6272135; CC Q8IWE5; A0A0F6B063: sifA; Xeno; NbExp=3; IntAct=EBI-726484, EBI-11477981; CC Q8IWE5; Q56061: sifA; Xeno; NbExp=3; IntAct=EBI-726484, EBI-10765408; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15905402}. Lysosome CC membrane {ECO:0000269|PubMed:22172677}; Peripheral membrane protein CC {ECO:0000305}; Cytoplasmic side {ECO:0000305|PubMed:22172677}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8IWE5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8IWE5-2; Sequence=VSP_061018; CC -!- SEQUENCE CAUTION: CC Sequence=AAH40441.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAA74865.1; Type=Erroneous initiation; 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; AB020649; BAA74865.1; ALT_INIT; mRNA. DR EMBL; AL450998; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL606758; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121992; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471167; EAW51745.1; -; Genomic_DNA. DR EMBL; BC008002; AAH08002.1; -; mRNA. DR EMBL; BC016488; AAH16488.1; -; mRNA. DR EMBL; BC030545; AAH30545.1; -; mRNA. DR EMBL; BC040441; AAH40441.1; ALT_INIT; mRNA. DR EMBL; BC042103; AAH42103.1; -; mRNA. DR EMBL; AL137297; CAB70684.1; -; mRNA. DR CCDS; CCDS44063.1; -. [Q8IWE5-1] DR CCDS; CCDS90868.1; -. [Q8IWE5-2] DR PIR; T46361; T46361. DR RefSeq; NP_055979.2; NM_015164.3. [Q8IWE5-1] DR RefSeq; XP_005245847.1; XM_005245790.3. DR PDB; 3CXB; X-ray; 2.60 A; B=773-884. DR PDB; 3HW2; X-ray; 3.30 A; B=771-875. DR PDB; 3ZFW; X-ray; 2.90 A; X/Y=203-212. DR PDBsum; 3CXB; -. DR PDBsum; 3HW2; -. DR PDBsum; 3ZFW; -. DR AlphaFoldDB; Q8IWE5; -. DR SMR; Q8IWE5; -. DR BioGRID; 116814; 13. DR CORUM; Q8IWE5; -. DR DIP; DIP-46410N; -. DR ELM; Q8IWE5; -. DR IntAct; Q8IWE5; 8. DR STRING; 9606.ENSP00000364956; -. DR iPTMnet; Q8IWE5; -. DR PhosphoSitePlus; Q8IWE5; -. DR BioMuta; PLEKHM2; -. DR DMDM; 160419243; -. DR EPD; Q8IWE5; -. DR jPOST; Q8IWE5; -. DR MassIVE; Q8IWE5; -. DR MaxQB; Q8IWE5; -. DR PaxDb; 9606-ENSP00000364956; -. DR PeptideAtlas; Q8IWE5; -. DR ProteomicsDB; 65459; -. DR ProteomicsDB; 70850; -. DR Pumba; Q8IWE5; -. DR Antibodypedia; 47979; 78 antibodies from 22 providers. DR DNASU; 23207; -. DR Ensembl; ENST00000375793.2; ENSP00000364950.2; ENSG00000116786.13. [Q8IWE5-2] DR Ensembl; ENST00000375799.8; ENSP00000364956.3; ENSG00000116786.13. [Q8IWE5-1] DR GeneID; 23207; -. DR KEGG; hsa:23207; -. DR MANE-Select; ENST00000375799.8; ENSP00000364956.3; NM_015164.4; NP_055979.2. DR UCSC; uc010obo.2; human. [Q8IWE5-1] DR AGR; HGNC:29131; -. DR DisGeNET; 23207; -. DR GeneCards; PLEKHM2; -. DR HGNC; HGNC:29131; PLEKHM2. DR HPA; ENSG00000116786; Tissue enhanced (brain). DR MalaCards; PLEKHM2; -. DR MIM; 609613; gene. DR neXtProt; NX_Q8IWE5; -. DR OpenTargets; ENSG00000116786; -. DR Orphanet; 54260; Left ventricular noncompaction. DR PharmGKB; PA134888781; -. DR VEuPathDB; HostDB:ENSG00000116786; -. DR eggNOG; KOG1829; Eukaryota. DR GeneTree; ENSGT00390000015175; -. DR HOGENOM; CLU_012258_0_0_1; -. DR InParanoid; Q8IWE5; -. DR OMA; PSEMIHS; -. DR OrthoDB; 5400354at2759; -. DR PhylomeDB; Q8IWE5; -. DR TreeFam; TF332641; -. DR PathwayCommons; Q8IWE5; -. DR SignaLink; Q8IWE5; -. DR BioGRID-ORCS; 23207; 17 hits in 1155 CRISPR screens. DR ChiTaRS; PLEKHM2; human. DR EvolutionaryTrace; Q8IWE5; -. DR GeneWiki; PLEKHM2; -. DR GenomeRNAi; 23207; -. DR Pharos; Q8IWE5; Tbio. DR PRO; PR:Q8IWE5; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q8IWE5; Protein. DR Bgee; ENSG00000116786; Expressed in right frontal lobe and 189 other cell types or tissues. DR ExpressionAtlas; Q8IWE5; baseline and differential. DR GO; GO:0010008; C:endosome membrane; IDA:AgBase. DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB. DR GO; GO:0019894; F:kinesin binding; IDA:UniProtKB. DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB. DR GO; GO:0032418; P:lysosome localization; IDA:UniProtKB. DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IMP:UniProtKB. DR GO; GO:0032880; P:regulation of protein localization; IMP:AgBase. DR CDD; cd13309; PH_SKIP; 1. DR CDD; cd17680; RUN_PLEKHM2; 1. DR Gene3D; 1.20.58.900; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR004012; Run_dom. DR InterPro; IPR037213; Run_dom_sf. DR InterPro; IPR047327; RUN_PLEKHM2. DR PANTHER; PTHR46556; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY M MEMBER 2; 1. DR PANTHER; PTHR46556:SF1; PLECKSTRIN HOMOLOGY DOMAIN-CONTAINING FAMILY M MEMBER 2; 1. DR Pfam; PF00169; PH; 1. DR Pfam; PF02759; RUN; 1. DR SMART; SM00233; PH; 1. DR SMART; SM00593; RUN; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR SUPFAM; SSF140741; RUN domain-like; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. DR PROSITE; PS50826; RUN; 1. DR Genevisible; Q8IWE5; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Lysosome; KW Membrane; Phosphoprotein; Reference proteome. FT CHAIN 1..1019 FT /note="Pleckstrin homology domain-containing family M FT member 2" FT /id="PRO_0000309455" FT DOMAIN 36..158 FT /note="RUN" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178" FT DOMAIN 771..873 FT /note="PH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145" FT REGION 1..310 FT /note="Interaction with KIF5B" FT /evidence="ECO:0000269|PubMed:15905402" FT REGION 230..458 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 471..525 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 557..581 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 762..885 FT /note="Interaction with sifA" FT COMPBIAS 237..294 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 352..366 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 374..389 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 413..435 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 441 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q80TQ5" FT VAR_SEQ 218..237 FT /note="Missing (in isoform 2)" FT /id="VSP_061018" FT VARIANT 32 FT /note="I -> T (in dbSNP:rs12091750)" FT /id="VAR_036950" FT MUTAGEN 207..208 FT /note="WD->AA: No effect on lysosomal location; loss of FT interaction with kinesin-1 and movement of lysosomes to the FT periphery; when associated with A-236-237-A." FT /evidence="ECO:0000269|PubMed:22172677" FT MUTAGEN 236..237 FT /note="WE->AA: No effect on lysosomal location; loss of FT interaction with kinesin-1 and movement of lysosomes to the FT periphery; when associated with A-207-208-A." FT /evidence="ECO:0000269|PubMed:22172677" FT MUTAGEN 828 FT /note="G->D: Loss of interaction with sifA." FT /evidence="ECO:0000269|PubMed:18996344" FT MUTAGEN 830 FT /note="R->D: Loss of interaction with sifA." FT /evidence="ECO:0000269|PubMed:18996344" FT MUTAGEN 831 FT /note="R->A: Alters interaction with sifA." FT /evidence="ECO:0000269|PubMed:18996344" FT MUTAGEN 869 FT /note="C->D: Loss of interaction with sifA." FT /evidence="ECO:0000269|PubMed:18996344" FT CONFLICT 600..602 FT /note="VFR -> ASG (in Ref. 4; AAH30545)" FT /evidence="ECO:0000305" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:3ZFW" FT STRAND 774..780 FT /evidence="ECO:0007829|PDB:3CXB" FT STRAND 787..789 FT /evidence="ECO:0007829|PDB:3HW2" FT STRAND 793..800 FT /evidence="ECO:0007829|PDB:3CXB" FT STRAND 803..811 FT /evidence="ECO:0007829|PDB:3CXB" FT STRAND 816..820 FT /evidence="ECO:0007829|PDB:3CXB" FT STRAND 826..831 FT /evidence="ECO:0007829|PDB:3CXB" FT STRAND 840..845 FT /evidence="ECO:0007829|PDB:3CXB" FT STRAND 851..854 FT /evidence="ECO:0007829|PDB:3CXB" FT HELIX 858..872 FT /evidence="ECO:0007829|PDB:3CXB" SQ SEQUENCE 1019 AA; 112780 MW; FFD857F4C11BC0DB CRC64; MEPGEVKDRI LENISLSVKK LQSYFAACED EIPAIRNHDK VLQRLCEHLD HALLYGLQDL SSGYWVLVVH FTRREAIKQI EVLQHVATNL GRSRAWLYLA LNENSLESYL RLFQENLGLL HKYYVKNALV CSHDHLTLFL TLVSGLEFIR FELDLDAPYL DLAPYMPDYY KPQYLLDFED RLPSSVHGSD SLSLNSFNSV TSTNLEWDDS AIAPSSEDYD FGDVFPAVPS VPSTDWEDGD LTDTVSGPRS TASDLTSSKA STRSPTQRQN PFNEEPAETV SSSDTTPVHT TSQEKEEAQA LDPPDACTEL EVIRVTKKKK IGKKKKSRSD EEASPLHPAC SQKKCAKQGD GDSRNGSPSL GRDSPDTMLA SPQEEGEGPS STTESSERSE PGLLIPEMKD TSMERLGQPL SKVIDQLNGQ LDPSTWCSRA EPPDQSFRTG SPGDAPERPP LCDFSEGLSA PMDFYRFTVE SPSTVTSGGG HHDPAGLGQP LHVPSSPEAA GQEEEGGGGE GQTPRPLEDT TREAQELEAQ LSLVREGPVS EPEPGTQEVL CQLKRDQPSP CLSSAEDSGV DEGQGSPSEM VHSSEFRVDN NHLLLLMIHV FRENEEQLFK MIRMSTGHME GNLQLLYVLL TDCYVYLLRK GATEKPYLVE EAVSYNELDY VSVGLDQQTV KLVCTNRRKQ FLLDTADVAL AEFFLASLKS AMIKGCREPP YPSILTDATM EKLALAKFVA QESKCEASAV TVRFYGLVHW EDPTDESLGP TPCHCSPPEG TITKEGMLHY KAGTSYLGKE HWKTCFVVLS NGILYQYPDR TDVIPLLSVN MGGEQCGGCR RANTTDRPHA FQVILSDRPC LELSAESEAE MAEWMQHLCQ AVSKGVIPQG VAPSPCIPCC LVLTDDRLFT CHEDCQTSFF RSLGTAKLGD ISAVSTEPGK EYCVLEFSQD SQQLLPPWVI YLSCTSELDR LLSALNSGWK TIYQVDLPHT AIQEASNKKK FEDALSLIHS AWQRSDSLCR GRASRDPWC //