PKHM2_HUMAN
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 03-AUG-2022, entry version 140.
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};
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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 PIR; T46361; T46361.
DR RefSeq; NP_055979.2; NM_015164.3. [Q8IWE5-1]
DR RefSeq; XP_005245847.1; XM_005245790.3. [Q8IWE5-2]
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; 8.
DR CORUM; Q8IWE5; -.
DR DIP; DIP-46410N; -.
DR ELM; Q8IWE5; -.
DR IntAct; Q8IWE5; 9.
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; Q8IWE5; -.
DR PeptideAtlas; Q8IWE5; -.
DR PRIDE; Q8IWE5; -.
DR ProteomicsDB; 65459; -.
DR ProteomicsDB; 70850; -.
DR Antibodypedia; 47979; 76 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 CTD; 23207; -.
DR DisGeNET; 23207; -.
DR GeneCards; PLEKHM2; -.
DR HGNC; HGNC:29131; PLEKHM2.
DR HPA; ENSG00000116786; Low tissue specificity.
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; 58687at2759; -.
DR PhylomeDB; Q8IWE5; -.
DR TreeFam; TF332641; -.
DR PathwayCommons; Q8IWE5; -.
DR SignaLink; Q8IWE5; -.
DR BioGRID-ORCS; 23207; 16 hits in 1079 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 187 other tissues.
DR ExpressionAtlas; Q8IWE5; baseline and differential.
DR Genevisible; Q8IWE5; HS.
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:1903527; P:positive regulation of membrane tubulation; IDA:AgBase.
DR GO; GO:0032880; P:regulation of protein localization; IMP:AgBase.
DR Gene3D; 1.20.58.900; -; 1.
DR Gene3D; 2.30.29.30; -; 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 Pfam; PF00169; PH; 1.
DR Pfam; PF02759; RUN; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00593; RUN; 1.
DR SUPFAM; SSF140741; SSF140741; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50826; RUN; 1.
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
