PKHM2_MOUSE
ID PKHM2_MOUSE Reviewed; 1018 AA.
AC Q80TQ5; A2ADE1; Q3U0Q7; Q6PD22;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Pleckstrin homology domain-containing family M member 2 {ECO:0000305};
DE Short=PH domain-containing family M member 2;
GN Name=Plekhm2 {ECO:0000312|MGI:MGI:1916832}; Synonyms=Kiaa0842;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 73-1018 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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. Critical factor involved in NK cell-mediated cytotoxicity.
CC Drives the polarization of cytolytic granules and microtubule-
CC organizing centers (MTOCs) toward the immune synapse between effector
CC NK lymphocytes and target cells. Required for maintenance of the Golgi
CC apparatus organization. May play a role in membrane tubulation.
CC {ECO:0000250|UniProtKB:Q8IWE5}.
CC -!- SUBUNIT: Interacts with KLC2 (via TPR repeats). Interacts with KIF5B.
CC Interacts with BORCS5. Interacts (via RUN domain) with ARL8B (GTP-bound
CC form); PLEKHM1 and PLEKHM2 compete for interaction with ARL8B.
CC Interacts with ARL8A. {ECO:0000250|UniProtKB:Q8IWE5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8IWE5}.
CC Lysosome membrane {ECO:0000250|UniProtKB:Q8IWE5}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q8IWE5}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q8IWE5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q80TQ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TQ5-2; Sequence=VSP_029163, VSP_029164;
CC Name=3;
CC IsoId=Q80TQ5-3; Sequence=VSP_029162, VSP_029163, VSP_029164;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65668.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK122386; BAC65668.1; ALT_INIT; mRNA.
DR EMBL; AK156652; BAE33794.1; -; mRNA.
DR EMBL; AL670446; CAM19908.1; -; Genomic_DNA.
DR EMBL; BC058984; AAH58984.1; -; mRNA.
DR RefSeq; NP_001028322.1; NM_001033150.1.
DR AlphaFoldDB; Q80TQ5; -.
DR SMR; Q80TQ5; -.
DR STRING; 10090.ENSMUSP00000081221; -.
DR iPTMnet; Q80TQ5; -.
DR PhosphoSitePlus; Q80TQ5; -.
DR MaxQB; Q80TQ5; -.
DR PaxDb; Q80TQ5; -.
DR PeptideAtlas; Q80TQ5; -.
DR PRIDE; Q80TQ5; -.
DR ProteomicsDB; 289912; -. [Q80TQ5-1]
DR ProteomicsDB; 289913; -. [Q80TQ5-2]
DR ProteomicsDB; 289914; -. [Q80TQ5-3]
DR GeneID; 69582; -.
DR KEGG; mmu:69582; -.
DR CTD; 23207; -.
DR MGI; MGI:1916832; Plekhm2.
DR eggNOG; KOG4381; Eukaryota.
DR InParanoid; Q80TQ5; -.
DR OrthoDB; 58687at2759; -.
DR TreeFam; TF332641; -.
DR BioGRID-ORCS; 69582; 4 hits in 74 CRISPR screens.
DR ChiTaRS; Plekhm2; mouse.
DR PRO; PR:Q80TQ5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q80TQ5; protein.
DR GO; GO:0044754; C:autolysosome; ISS:UniProtKB.
DR GO; GO:0010008; C:endosome membrane; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0061909; P:autophagosome-lysosome fusion; ISS:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; ISO:MGI.
DR GO; GO:1902774; P:late endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; ISS:UniProtKB.
DR GO; GO:1903527; P:positive regulation of membrane tubulation; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISO:MGI.
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 Acetylation; Alternative splicing; Cytoplasm; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..1018
FT /note="Pleckstrin homology domain-containing family M
FT member 2"
FT /id="PRO_0000309456"
FT DOMAIN 36..158
FT /note="RUN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00178"
FT DOMAIN 770..872
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..289
FT /note="Interaction with KIF5B"
FT /evidence="ECO:0000250"
FT REGION 210..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 555..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 313..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..583
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q8IWE5"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..165
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029162"
FT VAR_SEQ 217
FT /note="E -> EDYDFGDVFPAVPSVPSTDWE (in isoform 2 and isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029163"
FT VAR_SEQ 527..532
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029164"
FT CONFLICT 490
FT /note="G -> GG (in Ref. 3; CAM19908 and 4; AAH58984)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="V -> L (in Ref. 3; CAM19908 and 4; AAH58984)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="R -> L (in Ref. 4; AAH58984)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1018 AA; 112734 MW; 1024AD61CE90767D CRC64;
MEPREVKDRI LENISLSVKK LQSYFAACED ETPAIRNHDK VLQRLCEHLD HALLYGLQDL
SSGYWVLVVH FTRREAIRQI EVLQHVATNL GRSRAWLYLA LNENSLESYL RLFQENLGLL
QKYYVRNALV CSHDHLTLFL TLVSGLEFIR FDLDLDAPYL DLAPYMPDYY KPQYLLDFED
RLPSSVHGSD SLSLNSFNSV TSTNLEWDDS AIAPSSEDGD LTDTISGPRS TASDLTSSKT
STKSPTQRHN PFNEEQAETA SSDTTPVHTT SQEKEEAQAP DQPDACTELE VIRVTKKKKI
GKKKKTKLDE DASPLHPTSS QQKCGQQGEG DGLVGTPGLA RDPSDTVLAS PQEQGEGLSS
TAGSSELSEL SQMGLLIPEM KDTSMECLGQ PLSKVIDKLH GQLDPSTWCS HADPPEQSFR
AGSPGEAPEK PPFCDFSEGL PAPMDFYRFT VESPSTVAPG GGHHDPPGPS QPLHVPGSPA
AALQEEEEGG RGEGQTSQPV EDRQGEEIQE PEPQEPDSQL PLVSQEPLVS QEPVPEPVSQ
PEPGTHEALC KLKRDQPSPC LSSAEDSGVE EGQGSPSEMT HPSEFRVDNN HLLLLMIHVF
RENEEQLFKM IRMSTGHMEG NLQLLYVLLT DCYVYLLRKG ATEKPYLVEE AVSYNELDYV
SVGLDQQTVK LVCTNRRKQF LLDTADVALA ELFLASLKSA MIKGCREPPY PSILTDATME
KLALAKFVAQ ESKCEASAVT VHFYGLVHWE DPMEEALGPV PCQCSPAEGT ITKEGMLHYK
ASTSYLGKEH WKACFVVLSN GILYQYPDRT DVIPLLSVNM GGEQCGGCRR SNTTDRPHAF
QVILADRPCL ELSADSEAEM ADWMQHLCQA VSKGVIPQGI APSPCIPCCL VITEDRLFTC
HEDCQTSFFR SLGTARLADI TAISTELGKE YCVLEFSQDS PQLLQPWVIY LSCTSELDRF
LTALSSGWKA IYQVDLPHKA IHEASIKQKF EDALSLIHSA WQRSDSLCRG RASRDPWC
