PLET1_MOUSE
ID PLET1_MOUSE Reviewed; 237 AA.
AC Q8VEN2; Q05DM2; Q9DAT1; Q9DCI0;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Placenta-expressed transcript 1 protein;
DE AltName: Full=Antigen mAgK114;
DE Flags: Precursor;
GN Name=Plet1;
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] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=FVB/NJ;
RX PubMed=15203209; DOI=10.1016/j.ygeno.2004.02.006;
RA Zhao S.-H., Simmons D.G., Cross J.C., Scheetz T.E., Casavant T.L.,
RA Soares M.B., Tuggle C.K.;
RT "PLET1 (C11orf34), a highly expressed and processed novel gene in pig and
RT mouse placenta, is transcribed but poorly spliced in human.";
RL Genomics 84:114-125(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Placenta;
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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=16219980; DOI=10.2108/zsj.22.995;
RA Takeuchi M., Tatefuji T., Kayano T., Okura T., Mori T., Ohta T.,
RA Kurimoto M.;
RT "Distribution of a novel protein AgK114 expression in the normal tissues of
RT adult mice: dual expression of AgK114 and growth hormone in anterior
RT pituitary cells.";
RL Zool. Sci. 22:995-1001(2005).
RN [5]
RP POSSIBLE FUNCTION.
RX PubMed=16651715; DOI=10.1248/bpb.29.896;
RA Tatefuji T., Arai C., Mori T., Okuda Y., Kayano T., Mizote A., Okura T.,
RA Takeuchi M., Ohta T., Kurimoto M.;
RT "The effect of AgK114 on wound healing.";
RL Biol. Pharm. Bull. 29:896-902(2006).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=17302988; DOI=10.1186/1471-213x-7-8;
RA Frankenberg S., Smith L., Greenfield A., Zernicka-Goetz M.;
RT "Novel gene expression patterns along the proximo-distal axis of the mouse
RT embryo before gastrulation.";
RL BMC Dev. Biol. 7:8-8(2007).
RN [7]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=18195351; DOI=10.1073/pnas.0711170105;
RA Depreter M.G.L., Blair N.F., Gaskell T.L., Nowell C.S., Davern K.,
RA Pagliocca A., Stenhouse F.H., Farley A.M., Fraser A., Vrana J.,
RA Robertson K., Morahan G., Tomlinson S.R., Blackburn C.C.;
RT "Identification of Plet-1 as a specific marker of early thymic epithelial
RT progenitor cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:961-966(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, GPI-ANCHOR, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=20130590; DOI=10.1038/jid.2010.4;
RA Raymond K., Richter A., Kreft M., Frijns E., Janssen H., Slijper M.,
RA Praetzel-Wunder S., Langbein L., Sonnenberg A.;
RT "Expression of the orphan protein Plet-1 during trichilemmal
RT differentiation of anagen hair follicles.";
RL J. Invest. Dermatol. 130:1500-1513(2010).
CC -!- FUNCTION: Modulates leading keratinocyte migration and cellular
CC adhesion to matrix proteins during a wound-healing response and
CC promotes wound repair. May play a role during trichilemmal
CC differentiation of the hair follicle. {ECO:0000269|PubMed:20130590}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:20130590}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:20130590}. Note=Localized at the apical membrane of
CC the most differentiated keratinocytes of the outer root sheath (ORS),
CC clustered mainly in planar regions of the plasma membrane at the base
CC of microvilli.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8VEN2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8VEN2-2; Sequence=VSP_031770;
CC -!- TISSUE SPECIFICITY: Present in hair follicle cells and sebaceous gland
CC of skin, ciliated epithelial cells of trachea and bronchial tube,
CC striated portion of submandibular gland, distal convoluted tubule cells
CC of kidney, ciliated epithelial cells of oviduct, medulla of adrenal
CC gland and anterior lobe of pituitary gland. Expressed in keratinocytes
CC of the hair follicle at the trichilemmal zone corresponding to the
CC terminally differentiated outermost suprabasal outer root sheath (ORS),
CC including that of the sebaceous gland duct (SGD) and the directly
CC adjacent upper distal end of the companion layer (CL). Expression is
CC similar in all hair follicle growth stages. Also detected during both
CC the early and late anagen phases above the bulge of stem cells.
CC Expressed at the leading edge of the epidermal wound. Not expressed in
CC the interfollicular epidermis (IFE), inner root sheath (IRS) and hair
CC fiber. Highly expressed in placenta. Detected in mammary and prostate
CC epithelia and in the pancreas (at protein level).
CC {ECO:0000269|PubMed:15203209, ECO:0000269|PubMed:16219980,
CC ECO:0000269|PubMed:18195351, ECO:0000269|PubMed:20130590}.
CC -!- DEVELOPMENTAL STAGE: In early embryos before gastrulation, it is
CC specifically expressed in the distal-most part of the extraembryonic
CC ectoderm, adjacent to the epiblast. Expression is highly restricted to
CC the developing pharyngeal endoderm and mesonephros until day 11.5 of
CC embryogenesis. {ECO:0000269|PubMed:17302988,
CC ECO:0000269|PubMed:18195351}.
CC -!- INDUCTION: Up-regulated during calcium-induced terminal differentiation
CC of outer root sheath (ORS) keratinocytes.
CC {ECO:0000269|PubMed:20130590}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:20130590}.
CC -!- PTM: GPI-anchored.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB24118.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY364436; AAQ72439.1; -; mRNA.
DR EMBL; AK002767; BAB22342.1; -; mRNA.
DR EMBL; AK005558; BAB24118.1; ALT_FRAME; mRNA.
DR EMBL; BC017624; AAH17624.1; -; mRNA.
DR EMBL; BC022950; AAH22950.1; -; mRNA.
DR CCDS; CCDS40619.1; -. [Q8VEN2-1]
DR RefSeq; NP_083915.2; NM_029639.2. [Q8VEN2-1]
DR AlphaFoldDB; Q8VEN2; -.
DR STRING; 10090.ENSMUSP00000110118; -.
DR GlyGen; Q8VEN2; 4 sites.
DR PhosphoSitePlus; Q8VEN2; -.
DR MaxQB; Q8VEN2; -.
DR PaxDb; Q8VEN2; -.
DR PeptideAtlas; Q8VEN2; -.
DR PRIDE; Q8VEN2; -.
DR ProteomicsDB; 289761; -. [Q8VEN2-1]
DR ProteomicsDB; 289762; -. [Q8VEN2-2]
DR Antibodypedia; 51858; 69 antibodies from 16 providers.
DR DNASU; 76509; -.
DR Ensembl; ENSMUST00000114474; ENSMUSP00000110118; ENSMUSG00000032068. [Q8VEN2-1]
DR Ensembl; ENSMUST00000188047; ENSMUSP00000139422; ENSMUSG00000032068. [Q8VEN2-2]
DR GeneID; 76509; -.
DR KEGG; mmu:76509; -.
DR UCSC; uc009pjo.1; mouse. [Q8VEN2-1]
DR CTD; 349633; -.
DR MGI; MGI:1923759; Plet1.
DR VEuPathDB; HostDB:ENSMUSG00000032068; -.
DR eggNOG; ENOG502RTZP; Eukaryota.
DR GeneTree; ENSGT00390000014690; -.
DR HOGENOM; CLU_099483_0_0_1; -.
DR InParanoid; Q8VEN2; -.
DR OMA; YMTVLEA; -.
DR OrthoDB; 1472106at2759; -.
DR PhylomeDB; Q8VEN2; -.
DR TreeFam; TF344172; -.
DR Reactome; R-MMU-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR BioGRID-ORCS; 76509; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Plet1; mouse.
DR PRO; PR:Q8VEN2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8VEN2; protein.
DR Bgee; ENSMUSG00000032068; Expressed in ectoplacental cone and 134 other tissues.
DR Genevisible; Q8VEN2; MM.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; IMP:UniProtKB.
DR InterPro; IPR026184; PLET1.
DR PANTHER; PTHR22527; PTHR22527; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Differentiation; Glycoprotein;
KW GPI-anchor; Lipoprotein; Membrane; Reference proteome; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..218
FT /note="Placenta-expressed transcript 1 protein"
FT /id="PRO_0000320954"
FT PROPEP 219..237
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424669"
FT REGION 145..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 218
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 149..237
FT /note="VQPSASTPIPESSETSQTINTTPTVNTAKTTAKDTANTTAVTTANTTANTTA
FT VTTAKTTAKSLAIRTLGSPLAGALHILLVFLISKLLF -> GPLLARSGQLPHPSLQSA
FT PLTLVNSARSVPAHSGPRIYLLLYISTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031770"
FT CONFLICT 189
FT /note="V -> G (in Ref. 2; BAB24118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 237 AA; 25006 MW; CF6E144B6D9C902B CRC64;
MLSLRSLLPH LGLFLCLALH LSPSLSASDN GSCVVLDNIY TSDILEISTM ANVSGGDVTY
TVTVPVNDSV SAVILKAVKE DDSPVGTWSG TYEKCNDSSV YYNLTSQSQS VFQTNWTVPT
SEDVTKVNLQ VLIVVNRTAS KSSVKMEQVQ PSASTPIPES SETSQTINTT PTVNTAKTTA
KDTANTTAVT TANTTANTTA VTTAKTTAKS LAIRTLGSPL AGALHILLVF LISKLLF
