ID EVPL_MOUSE Reviewed; 2035 AA.
AC Q9D952; B1AU57;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 27-MAR-2024, entry version 165.
DE RecName: Full=Envoplakin;
DE AltName: Full=210 kDa cornified envelope precursor protein;
DE AltName: Full=p210;
GN Name=Evpl;
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 [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10747979; DOI=10.1074/jbc.m001028200;
RA Maatta A., Ruhrberg C., Watt F.M.;
RT "Structure and regulation of the envoplakin gene.";
RL J. Biol. Chem. 275:19857-19865(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1860-2035.
RC STRAIN=C57BL/6J; TISSUE=Pancreas;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1576, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Component of the cornified envelope of keratinocytes. May
CC link the cornified envelope to desmosomes and intermediate filaments.
CC -!- SUBUNIT: May form a homodimer or a heterodimer with PPL.
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250}. Cornified
CC envelope {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Note=Colocalized with DSP at desmosomes and along intermediate
CC filaments. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
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DR EMBL; AJ309317; CAC38864.2; -; Genomic_DNA.
DR EMBL; AJ319607; CAC38864.2; JOINED; Genomic_DNA.
DR EMBL; AJ319608; CAC38864.2; JOINED; Genomic_DNA.
DR EMBL; AJ319609; CAC38864.2; JOINED; Genomic_DNA.
DR EMBL; AJ319610; CAC38864.2; JOINED; Genomic_DNA.
DR EMBL; AJ319611; CAC38864.2; JOINED; Genomic_DNA.
DR EMBL; AJ319612; CAC38864.2; JOINED; Genomic_DNA.
DR EMBL; AJ319613; CAC38864.2; JOINED; Genomic_DNA.
DR EMBL; AL669925; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK007353; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS25661.1; -.
DR RefSeq; NP_079552.3; NM_025276.3.
DR AlphaFoldDB; Q9D952; -.
DR SMR; Q9D952; -.
DR BioGRID; 199548; 24.
DR IntAct; Q9D952; 18.
DR STRING; 10090.ENSMUSP00000037850; -.
DR GlyGen; Q9D952; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9D952; -.
DR PhosphoSitePlus; Q9D952; -.
DR MaxQB; Q9D952; -.
DR PaxDb; 10090-ENSMUSP00000037850; -.
DR PeptideAtlas; Q9D952; -.
DR ProteomicsDB; 271507; -.
DR Pumba; Q9D952; -.
DR Antibodypedia; 46112; 79 antibodies from 19 providers.
DR DNASU; 14027; -.
DR Ensembl; ENSMUST00000037007.4; ENSMUSP00000037850.4; ENSMUSG00000034282.4.
DR GeneID; 14027; -.
DR KEGG; mmu:14027; -.
DR UCSC; uc007mkp.1; mouse.
DR AGR; MGI:107507; -.
DR CTD; 2125; -.
DR MGI; MGI:107507; Evpl.
DR VEuPathDB; HostDB:ENSMUSG00000034282; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000153578; -.
DR HOGENOM; CLU_001780_0_0_1; -.
DR InParanoid; Q9D952; -.
DR OMA; TEHACGA; -.
DR OrthoDB; 5357436at2759; -.
DR PhylomeDB; Q9D952; -.
DR TreeFam; TF342779; -.
DR Reactome; R-MMU-6809371; Formation of the cornified envelope.
DR BioGRID-ORCS; 14027; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Evpl; mouse.
DR PRO; PR:Q9D952; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9D952; Protein.
DR Bgee; ENSMUSG00000034282; Expressed in esophagus and 134 other cell types or tissues.
DR Genevisible; Q9D952; MM.
DR GO; GO:0001533; C:cornified envelope; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
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:0030216; P:keratinocyte differentiation; ISO:MGI.
DR GO; GO:0002786; P:regulation of antibacterial peptide production; IGI:MGI.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR Gene3D; 1.20.58.60; -; 4.
DR Gene3D; 3.30.160.780; -; 1.
DR Gene3D; 3.90.1290.10; Plakin repeat; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR049538; PCN-like_spectrin-like_rpt.
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; ENVOPLAKIN; 1.
DR PANTHER; PTHR23169:SF7; ENVOPLAKIN; 1.
DR Pfam; PF00681; Plectin; 3.
DR Pfam; PF17902; SH3_10; 1.
DR Pfam; PF21020; Spectrin_4; 1.
DR SMART; SM00250; PLEC; 8.
DR SMART; SM00150; SPEC; 1.
DR SUPFAM; SSF75399; Plakin repeat; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell junction; Coiled coil; Cytoplasm; Cytoskeleton; Keratinization;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..2035
FT /note="Envoplakin"
FT /id="PRO_0000078148"
FT REPEAT 229..330
FT /note="Spectrin"
FT DOMAIN 413..470
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 1186..1227
FT /note="Plectin 1"
FT REPEAT 1679..1714
FT /note="Plectin 2"
FT REPEAT 1819..1856
FT /note="Plectin 3"
FT REPEAT 1857..1894
FT /note="Plectin 4"
FT REPEAT 1895..1932
FT /note="Plectin 5"
FT REPEAT 1933..1970
FT /note="Plectin 6"
FT REPEAT 1971..2008
FT /note="Plectin 7"
FT REGION 1..841
FT /note="Globular 1"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 12..28
FT /note="4 X 4 AA tandem repeats of K-G-S-P"
FT REGION 63..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..1674
FT /note="Central fibrous rod domain"
FT REGION 1607..1637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1675..2035
FT /note="Globular 2"
FT COILED 842..1664
FT /evidence="ECO:0000255"
FT COMPBIAS 67..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1607..1631
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1576
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1800
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92817"
FT MOD_RES 2026
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92817"
FT CONFLICT 282
FT /note="S -> N (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 437
FT /note="Y -> C (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="C -> W (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 476
FT /note="A -> G (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 604
FT /note="L -> V (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 610..611
FT /note="LN -> FH (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 843
FT /note="R -> E (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 852
FT /note="S -> N (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 858
FT /note="K -> N (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1013
FT /note="P -> L (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1635
FT /note="R -> W (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1830..1832
FT /note="GIY -> EIF (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
FT CONFLICT 1861..1864
FT /note="EAQA -> RPRQ (in Ref. 1; CAC38864)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2035 AA; 232012 MW; 92CD7FB7DE50ECC6 CRC64;
MFKGLSKGSQ GKGSPKGSPA KGSPKGSPNK HNRAATQELA LLISRMQANA DQVERDILET
QKKLQQDRQN GEQNQALQHQ QETGRNLKEA EVLLKDLFLD VDKARRLKHP QAEEIEKDIK
QLHERVTQEC SEYRALYEKM VLPPDVGPRV DWARVLEQKQ NLVREGHYGP GMAELEQQVA
EHNILQREIE AYGQQLRTLV GPDANTIRNQ YRELLKAASW RRQSLGSLYT HLQGCTKQLS
ALADQQGRIL QQDWSDLMPD PAGVRREYEH FKQHELLAQE RSINQLEDDA DRMVELGHPA
IGPIQVHQEA LKMEWQNFLN LCICQESQLQ RVEDYRRFQE EADSVSQTLA KLSSNLDTKY
GFGTGDSSGS PTELLLQLEA EEKQLAIAER AVGDLQQRSQ EVAPLPQRRN PSKQPLHVDS
ICDWDSGEVQ LLRGERYTLK DNADPYTWLV QGPGGETKSA PAACLCIPAP DPEAVAKASR
LATELQTLKQ KLSTEKNRLK AAAVEHLQPG QQAPAGSAPA DPQGQTLLSQ MTQLDGDLGQ
IERQVLSWAR SPLSQSSSLK DLEGRIHSCE GTAQRLQSLG AEKEAAQQEC EAFLSTKPTG
SAALQLPVVL NSVKNRYNDV QSLCHLYGEK AKAALGLEKQ IQEADRVIQG FEAALALEGP
VPEGSGALQE RVSELQRQRK ELLQQQACVL GLHRQLKATE HACSALQNNF QEFCQDLPRQ
QRQVRALTDR YHAVGDQLDL REKIVQDASL TYQQLRNSRD NLSSWLEQLP HHRVQPSDGP
SQISYKLQAQ KRLIQEILGR EQDQATVSRL TRDLQEALQD YELQADTYRC SLEPALAVSA
PKRLRVISLQ ESIQAQEKNL AKAYTEVAAA EQQQLRQLEF AKKMLRKKEL DEDIQAIHSA
RQGSGSPAHA RTAESEVLKT QLEEERKRVA EVQRDLEEQR QRLLQLRTQQ PVARLEEKEV
VEFYRDPQLE SNLSQAASRV EEEGKRRARL QAELEAVAQK VVHLEGKRKT MQPHLLTKEV
TQIERDPGLD SQVTQLHSEM QRLRGENGVL TARLEELKDE LLALEQKEMN VKEKVVVKEV
VKVEKDLEMV KAAQTLRLQI EEDAARRKGA KETVAKIQAR IKDLEQAISS VEPKVIVKEV
KKVEQDPGLL KEASRLRSLL EEEKNNNVAL ARELQELQEK YRVVEKQKPK VQLQERVSEI
FQVLPETEQE IRRLRAQLQE TGSKKSGVEQ EVEKLLPELE VLRAQKPVVE YKEVTQEVVR
HEKNPEVLRE IDRLKAQLNE LVNTNGRSQE QLIRLQGERD EWKRERSKVE TKMVSKEVVR
HEKDPVLEKE AERLRQEVRE AVQRRRATED AVYELQNKLL LLERRRPEEQ IVVQEVVVTQ
KDPKLREEHS RLSRSLDEEV GRRRQLELEV RQLGARVEEE EARLSFEEDR SKKLAAEREL
RQLTLKIQEL EKRPPALQEK IIMEEVVKLE KDPDLERSTE ALRRELDQEK NRVTELHREC
QGLQVQVDLL QKTKSQEKTI YKEVIRVEKD PVLEGERARV WEILNRERAA RKGREEDVRS
LQERIDRAEA LRRSWSREEA ELQRARDQAS QDCGRLQRQL RELEQQKQQK ARQLQEEGRL
LSQKTESERQ KAAQRSQAVT QLEAAILQEK DKIYEKERTL RDLHTKVSRE ELNQETQTRE
TNLSTKICIL EPETGNDMSP YEAYKRGVID RGQYLQLQEL ECDWEEVTTS SPCGEESVLL
DRKSGKQYSI EAALRCRRIS KEEYHRYKDG RLPISEFALL VAGETKPSSS LSIGSIISKS
PVCSPGPQST GFFSPGLSFG LTEDSFPIAG IYDTTTDNKC SIKAAVAKNM LDPITGQKLL
EAQAATGGIV DLLSRERYSV HKAVERGLIE NTSTQRLLNA QKAFTGIEDP VTRKRLSVGE
AIQKGWMPQE SVLPHLLVQH LTGGLIDPKR TGRIPVPQAV LCGMISEDLG QLLQDESGYE
KDLTDPITKE RLSYKEAMGR CRKDPLSGLL LLPAMLEGYR CYRAASPTLP RSCVR
//
