PKHM3_MOUSE
ID PKHM3_MOUSE Reviewed; 761 AA.
AC Q8BM47; Q3T9Y1;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Pleckstrin homology domain-containing family M member 3;
DE Short=PH domain-containing family M member 3;
DE AltName: Full=Differentiation-associated protein {ECO:0000303|PubMed:19028694};
GN Name=Plekhm3 {ECO:0000312|MGI:MGI:2443627};
GN Synonyms=Dapr {ECO:0000303|PubMed:19028694};
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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).
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH AKT1, AND
RP FUNCTION.
RX PubMed=19028694; DOI=10.1074/jbc.m807000200;
RA Virtanen C., Paris J., Takahashi M.;
RT "Identification and characterization of a novel gene, dapr, involved in
RT skeletal muscle differentiation and protein kinase B signaling.";
RL J. Biol. Chem. 284:1636-1643(2009).
CC -!- FUNCTION: Involved in skeletal muscle differentiation
CC (PubMed:19028694). May act as a scaffold protein for AKT1 during muscle
CC differentiation (PubMed:19028694). {ECO:0000269|PubMed:19028694}.
CC -!- SUBUNIT: Interacts with AKT1. {ECO:0000269|PubMed:19028694}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19028694}. Golgi
CC apparatus {ECO:0000269|PubMed:19028694}. Cell membrane
CC {ECO:0000269|PubMed:19028694}. Note=Before differentiation of muscle
CC cells, localized to the cytosol. During muscle differentiation shuttles
CC to the plasma membrane. {ECO:0000269|PubMed:19028694}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BM47-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BM47-2; Sequence=VSP_032514, VSP_032515;
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:19028694). Expressed in
CC C2C12 cells (at protein level) (PubMed:19028694).
CC {ECO:0000269|PubMed:19028694}.
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DR EMBL; AK034959; BAC28895.1; -; mRNA.
DR EMBL; AK172220; BAE42889.1; -; mRNA.
DR EMBL; BC063098; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS15009.1; -. [Q8BM47-1]
DR RefSeq; NP_001034582.1; NM_001039493.1. [Q8BM47-1]
DR RefSeq; XP_006496045.1; XM_006495982.1. [Q8BM47-1]
DR AlphaFoldDB; Q8BM47; -.
DR SMR; Q8BM47; -.
DR STRING; 10090.ENSMUSP00000095320; -.
DR iPTMnet; Q8BM47; -.
DR PhosphoSitePlus; Q8BM47; -.
DR EPD; Q8BM47; -.
DR jPOST; Q8BM47; -.
DR MaxQB; Q8BM47; -.
DR PaxDb; Q8BM47; -.
DR PeptideAtlas; Q8BM47; -.
DR PRIDE; Q8BM47; -.
DR ProteomicsDB; 289661; -. [Q8BM47-1]
DR ProteomicsDB; 289662; -. [Q8BM47-2]
DR Antibodypedia; 34191; 57 antibodies from 21 providers.
DR DNASU; 241075; -.
DR Ensembl; ENSMUST00000097713; ENSMUSP00000095320; ENSMUSG00000051344. [Q8BM47-1]
DR Ensembl; ENSMUST00000139649; ENSMUSP00000138002; ENSMUSG00000051344. [Q8BM47-1]
DR GeneID; 241075; -.
DR KEGG; mmu:241075; -.
DR UCSC; uc007bha.1; mouse. [Q8BM47-1]
DR UCSC; uc007bhb.1; mouse. [Q8BM47-2]
DR CTD; 389072; -.
DR MGI; MGI:2443627; Plekhm3.
DR VEuPathDB; HostDB:ENSMUSG00000051344; -.
DR eggNOG; KOG1829; Eukaryota.
DR GeneTree; ENSGT00940000159743; -.
DR HOGENOM; CLU_021585_0_0_1; -.
DR InParanoid; Q8BM47; -.
DR OMA; CELCHNG; -.
DR OrthoDB; 177737at2759; -.
DR PhylomeDB; Q8BM47; -.
DR TreeFam; TF317067; -.
DR BioGRID-ORCS; 241075; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Plekhm3; mouse.
DR PRO; PR:Q8BM47; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BM47; protein.
DR Bgee; ENSMUSG00000051344; Expressed in dorsal root ganglion and 208 other tissues.
DR ExpressionAtlas; Q8BM47; baseline and differential.
DR Genevisible; Q8BM47; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045445; P:myoblast differentiation; IDA:UniProtKB.
DR CDD; cd14674; PH_PLEKHM3_1; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037812; PLEKHM3_PH_1.
DR InterPro; IPR025258; Zf-RING_9.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF13901; zf-RING_9; 1.
DR SMART; SM01175; DUF4206; 1.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Golgi apparatus; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Zinc;
KW Zinc-finger.
FT CHAIN 1..761
FT /note="Pleckstrin homology domain-containing family M
FT member 3"
FT /id="PRO_0000326035"
FT DOMAIN 212..309
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 361..456
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT ZN_FING 669..722
FT /note="Phorbol-ester/DAG-type"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT VAR_SEQ 1..275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032514"
FT VAR_SEQ 652..761
FT /note="IEGKLAPFLGKVIKFATAHVYSCSLCSQKGFICEICNNGEILYPFEDISTSR
FT CESCGAVFHSECKEKSVPCPRCVRRELQKKQKSFWRQLNVDESLEEACAMFELSYQST
FT -> CAQRAFRFHFLSEVTLWIVVWALN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032515"
FT CONFLICT 617
FT /note="S -> C (in Ref. 1; BAE42889)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 761 AA; 86553 MW; 58EB8DEF72F4E7B0 CRC64;
MEALEVDDIS PALEVTEDFF STFDSKLEKA VQQAEVYGIQ EVPELVGHEV LGNIADNGAL
RSVASLGKGT MIWDHCKSRL LETKAQNVFP AKEQLMVQRG TAPDNLSWMA QKEASTFNFF
NICQRRRDRP RSVNDLLDET TTFKPGHARS RSDVTHVDWR VVLSTMPLQQ QQQQQQASLQ
GIHFPGPSFL LSSPSKVEDA QGNTEHKQTF PNILKKGYLE IRKNHDSYWQ SCYAELSPYN
LNFYSLDSSG NQNLYATYQL SHFQSISVLG NLEARMVDTV LYDNSQLQLK AESPWEALDW
GQKLWEVVHA AVPNYMGRQG EMANSPGLIH HGDCAQNHCL QKKSSGLLAS PVLDSPKQYQ
NILKSGTLYR LTVQNNWKAF TFVLSKAYLM AFHPGKLDED PLLSYNVDVC LAVQIDNLDG
CDSCFQVIFP QDVLRLRAET RQRAQEWMEA LKTAANAARS SEQNLQVTLR NKPKDQLDGR
ELRKNKRQSV TTSFLSILTT LSLERGLTAQ SFKCAGCQRS IGLSNGKAKV CNYSGWYYCS
SCHVDDSFLI PARIVHNWDT SKYKVSKQAK EFLEYVYEEP LIDIQQENPM LYLHAEPLAT
VVRLRQRLKS LRAYLFSCRA AVAEDLRRRI FPREYLLQQI HLYSLADLQQ VIEGKLAPFL
GKVIKFATAH VYSCSLCSQK GFICEICNNG EILYPFEDIS TSRCESCGAV FHSECKEKSV
PCPRCVRREL QKKQKSFWRQ LNVDESLEEA CAMFELSYQS T
