PEPL_MOUSE
ID PEPL_MOUSE Reviewed; 1755 AA.
AC Q9R269; O70231; Q9CUT1; Q9JLZ7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Periplakin;
GN Name=Ppl;
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 [MRNA], AND INTERACTION WITH AKT1 AND VIM.
RC TISSUE=Embryo;
RX PubMed=12244133; DOI=10.1242/jcs.00069;
RA van den Heuvel A.P., de Vries-Smits A.M.M., van Weeren P.C., Dijkers P.F.,
RA de Bruyn K.M., Riedl J.A., Burgering B.M.T.;
RT "Binding of protein kinase B to the plakin family member periplakin.";
RL J. Cell Sci. 115:3957-3966(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DEVELOPMENTAL
RP STAGE.
RC STRAIN=129/Sv;
RX PubMed=15226441; DOI=10.1128/mcb.24.14.6410-6418.2004;
RA Aho S., Li K., Ryoo Y., McGee C., Ishida-Yamamoto A., Uitto J.,
RA Klement J.F.;
RT "Periplakin gene targeting reveals a constituent of the cornified cell
RT envelope dispensable for normal mouse development.";
RL Mol. Cell. Biol. 24:6410-6418(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1643-1755.
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1647-1755.
RC STRAIN=C57BL/6J;
RX PubMed=9521878; DOI=10.1006/geno.1997.5188;
RA Aho S., McLean W.H.I., Li K., Uitto J.;
RT "cDNA cloning, mRNA expression, and chromosomal mapping of human and mouse
RT periplakin genes.";
RL Genomics 48:242-247(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1656, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH BFSP1 AND BFSP2, INTERACTION WITH VIM AND
RP BFSP2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP REGION.
RX PubMed=19029034; DOI=10.1167/iovs.08-2894;
RA Yoon K.H., FitzGerald P.G.;
RT "Periplakin interactions with lens intermediate and beaded filaments.";
RL Invest. Ophthalmol. Vis. Sci. 50:1283-1289(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1656, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and 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).
CC -!- FUNCTION: Component of the cornified envelope of keratinocytes. May
CC link the cornified envelope to desmosomes and intermediate filaments.
CC May act as a localization signal in PKB/AKT-mediated signaling.
CC -!- SUBUNIT: Homodimer or a heterodimer with EVPL (By similarity). Found in
CC a complex composed of PPL (via C-terminal linker domain), BFSP1 and
CC BFSP2 in the retinal lens (PubMed:19029034). Within the complex
CC interacts (via C-terminal linker domain) with BFSP2 (PubMed:19029034).
CC Interacts with VIM (PubMed:12244133, PubMed:19029034). Binds to the PH
CC domain of AKT1 (PubMed:12244133). Interacts with FCGR1A (By
CC similarity). May interact with PPHLN1 (By similarity).
CC {ECO:0000250|UniProtKB:O60437, ECO:0000269|PubMed:12244133,
CC ECO:0000269|PubMed:19029034}.
CC -!- INTERACTION:
CC Q9R269; P20152: Vim; NbExp=2; IntAct=EBI-368293, EBI-299269;
CC Q9R269; Q01314: AKT1; Xeno; NbExp=2; IntAct=EBI-368293, EBI-368344;
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome
CC {ECO:0000269|PubMed:15226441}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O60437}. Cell membrane
CC {ECO:0000269|PubMed:19029034}. Cytoplasm {ECO:0000269|PubMed:19029034}.
CC -!- TISSUE SPECIFICITY: Expressed in the retinal lens (at protein level).
CC {ECO:0000269|PubMed:19029034}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the upper granular cell layer of
CC dorsal lip and tongue, palate and dorsal epidermis of newborns
CC (PubMed:15226441). Expressed in the corneal epithelium and conjunctiva,
CC with expression prevalent in the cytoplasm of anterior lens epithelial
CC cells, becoming predominantly membrane expressed in epithelial cells as
CC they elongate into fiber cells at 3 weeks of age (PubMed:19029034).
CC {ECO:0000269|PubMed:15226441, ECO:0000269|PubMed:19029034}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
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DR EMBL; AF126834; AAD20642.1; -; mRNA.
DR EMBL; AF116523; AAF29436.2; -; Genomic_DNA.
DR EMBL; AF116519; AAF29436.2; JOINED; Genomic_DNA.
DR EMBL; AF116520; AAF29436.2; JOINED; Genomic_DNA.
DR EMBL; AF116521; AAF29436.2; JOINED; Genomic_DNA.
DR EMBL; AF116522; AAF29436.2; JOINED; Genomic_DNA.
DR EMBL; AK014700; BAB29510.1; -; mRNA.
DR EMBL; AF013715; AAC40068.1; -; Genomic_DNA.
DR RefSeq; NP_032935.2; NM_008909.2.
DR AlphaFoldDB; Q9R269; -.
DR SMR; Q9R269; -.
DR BioGRID; 202331; 9.
DR IntAct; Q9R269; 4.
DR STRING; 10090.ENSMUSP00000039360; -.
DR iPTMnet; Q9R269; -.
DR PhosphoSitePlus; Q9R269; -.
DR MaxQB; Q9R269; -.
DR PaxDb; Q9R269; -.
DR PRIDE; Q9R269; -.
DR ProteomicsDB; 287916; -.
DR DNASU; 19041; -.
DR GeneID; 19041; -.
DR KEGG; mmu:19041; -.
DR CTD; 5493; -.
DR MGI; MGI:1194898; Ppl.
DR eggNOG; KOG0516; Eukaryota.
DR InParanoid; Q9R269; -.
DR OrthoDB; 35436at2759; -.
DR PhylomeDB; Q9R269; -.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR Reactome; R-MMU-8851680; Butyrophilin (BTN) family interactions.
DR BioGRID-ORCS; 19041; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ppl; mouse.
DR PRO; PR:Q9R269; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9R269; protein.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; TAS:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0002786; P:regulation of antibacterial peptide production; IGI:MGI.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR CDD; cd00176; SPEC; 1.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR001101; Plectin_repeat.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR PANTHER; PTHR23169; PTHR23169; 1.
DR Pfam; PF17902; SH3_10; 1.
DR SMART; SM00250; PLEC; 2.
DR SMART; SM00150; SPEC; 4.
DR SUPFAM; SSF75399; SSF75399; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Keratinization; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW SH3 domain.
FT CHAIN 1..1755
FT /note="Periplakin"
FT /id="PRO_0000078150"
FT REPEAT 214..315
FT /note="Spectrin 1"
FT REPEAT 321..483
FT /note="Spectrin 2"
FT DOMAIN 397..453
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 503..610
FT /note="Spectrin 3"
FT REPEAT 1650..1684
FT /note="Plectin 1"
FT REPEAT 1699..1734
FT /note="Plectin 2"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1755
FT /note="Interacts with BFSP2 and VIM"
FT /evidence="ECO:0000269|PubMed:19029034"
FT COILED 16..125
FT /evidence="ECO:0000255"
FT COILED 182..387
FT /evidence="ECO:0000255"
FT COILED 611..819
FT /evidence="ECO:0000255"
FT COILED 883..1644
FT /evidence="ECO:0000255"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60437"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60437"
FT MOD_RES 885
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60437"
FT MOD_RES 947
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60437"
FT MOD_RES 1583
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60437"
FT MOD_RES 1656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 166
FT /note="E -> Q (in Ref. 2; AAF29436)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="N -> T (in Ref. 2; AAF29436)"
FT /evidence="ECO:0000305"
FT CONFLICT 648
FT /note="R -> S (in Ref. 2; AAF29436)"
FT /evidence="ECO:0000305"
FT CONFLICT 671..672
FT /note="GK -> EQ (in Ref. 2; AAF29436)"
FT /evidence="ECO:0000305"
FT CONFLICT 983
FT /note="T -> A (in Ref. 2; AAF29436)"
FT /evidence="ECO:0000305"
FT CONFLICT 1325
FT /note="G -> R (in Ref. 2; AAF29436)"
FT /evidence="ECO:0000305"
FT CONFLICT 1344..1345
FT /note="QR -> G (in Ref. 2; AAF29436)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1755 AA; 204004 MW; 3FEA343086E4CB8F CRC64;
MHSLFRKRNK GKYSPTVQTR SISNKELSDL IEQLQKNADQ VERNIVDTEA KMQSDLARMQ
EGQLPEHRDA ALQNVSDSEK LLYVLEADSA IAKHMKHPQG DMIAEDIRQL KERVTNLRGK
HKQMYSLAVK EADPRVNWDT LVDEKLDKLS SQSFGTDLPL VDSQVEQHNI FHNEVKAIGP
HLAKDKEQNS ELQAKYQKLL TASQARQQHL SSLQDYMQRC TNELYWLDQQ AKGRMQYDWS
DRNLDYPSRR RQYENFINRN LEAKEERINK LHTEGDQLLT AEHPGRNSIE AHMEAVHAEW
KEYLNLLICE ESHLKYMEDY HQFHKDMKDA QELLRKVDSD LNQKYSPDFK DRYQIELLLR
ELDDQEKALD KYEDVVRGLQ RRGQQVVPLK YRRETPLKPI PVEALCDFES DQGLISRGYS
YTLQKNNGES WELTDSTGKK LAAPAVCFII PPTDPEALAL ADSLGSQYRS VRQKATGSKH
ALQQRHEVLR TENPGDASDL QGRQLLAGLD KVASDLDRQE KAITGILRPP LEQGRAIEDS
AERAKGLKNI TNELLQIEPE KTQCTAECEA FVQALPASGT APLLKTRVED TNQKYERLVW
LLEAAQEKVD VANRLENSLQ RGRELLASYE NRLIQDDTMP ESGHVLDRKR QELEAMASEL
QAHKSLLGEV GKNLQVAKQC SSSLASRFQE HCPDLERQEA EVHKLNQRFN NLSQQVERRA
QSLQSARAAY DEYCSGYNRV LQFLAKTPSY EPQETDSLGQ METKLKNQKN LLDELASREQ
EVQKVYADSQ QYQQAVKDYE LEAEKLRSLL DLENGRNSHV NKRARLQSPA AKVKEEEAAL
AAKFTEVNAI NRQRLQNLEF ALNLLRQQPE AGVTHETLQG GKLSSGMEET WKIKKELEEE
IERRQQLENE VKSAQEEIQT LKDQGPQESL VRKEVLKKVP DPALEESFQQ LQQTLAEEQH
KNQLLQEELG ALQLRLQALE QETRDGGQEY VVKEVLRIEP DRAQEDEVLQ LREELEALRR
QKGAREAEVL LLQQRVAALA AEKSRVQEKV TEREVVKLQN DPQLEAEYRR LQEEHQREGT
LREKQEEELS FLQAKLRRLE KERAMAEGKI TVKEVLKVEK DAAVEREVND LTRQYEDEAA
KARSGQREKT ELLRKIWALE EENAKVVVQE KVREIVRPDP KAESEVANLR LELVEQERKF
RGAEEQLKSY QSELEALRNR GPQVEVKEVT KEVIKYTTDP ETEQELQRLR EEIMDKTRLI
ERCDLEIYQL KQEIQALKDT KPQVQTREVV QEILQFQEDP QTKKEVESLR IQLSEEQKKQ
VDLEGERASQ EEKIKRKEEE LAQQRKERVV RQEVVQYEDE PDLRAEVTAF TNSIDAELRQ
IDKLHVELRR LQHRRAELER QLEELERERQ ARRAAELEVQ RLQQRLAALE QEEAKTGEKV
THTQKVVLQQ DPQQTREHAL LRAQLEEERH RRQLLEGELE PLRRKLAALE KAEIKEKVVF
SESVQVEKGD TEQEIQRLKK SLEEESQSKR ELDSEVTRLE AKLSELEFYN SKSSKELDFL
REENHKLQLE RQNLQLETRR LQSEIEMAAT ETRDLKNITT IDSGTHLNSR LWSLEKELDD
LKKMSKDKDL EIDELQRRLG SVAVKREQRE NHLRRSIVVI DPDTGRELSP EEAHRAGLID
WKMFVKLRSQ ECDWEEISVK GPNGESSVIH DRKSGKKFSI EDALQSGRLT AAQYDRYVNK
DMSIQELAVL VSGQK
