PLET1_RAT
ID PLET1_RAT Reviewed; 255 AA.
AC Q5HZW7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Placenta-expressed transcript 1 protein;
DE Flags: Precursor;
GN Name=Plet1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Ovary;
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250}; Lipid-anchor,
CC GPI-anchor {ECO:0000250}. Note=Localized at the apical membrane of the
CC 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. {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: GPI-anchored. {ECO:0000250}.
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DR EMBL; BC088858; AAH88858.1; -; mRNA.
DR RefSeq; NP_001014231.1; NM_001014209.1.
DR AlphaFoldDB; Q5HZW7; -.
DR STRING; 10116.ENSRNOP00000055980; -.
DR GlyGen; Q5HZW7; 3 sites.
DR PaxDb; Q5HZW7; -.
DR GeneID; 363060; -.
DR KEGG; rno:363060; -.
DR UCSC; RGD:1359217; rat.
DR CTD; 349633; -.
DR RGD; 1359217; Plet1.
DR VEuPathDB; HostDB:ENSRNOG00000024346; -.
DR eggNOG; ENOG502RTZP; Eukaryota.
DR HOGENOM; CLU_099483_0_0_1; -.
DR InParanoid; Q5HZW7; -.
DR OMA; FIVINRT; -.
DR OrthoDB; 1472106at2759; -.
DR PhylomeDB; Q5HZW7; -.
DR TreeFam; TF344172; -.
DR Reactome; R-RNO-163125; Post-translational modification: synthesis of GPI-anchored proteins.
DR PRO; PR:Q5HZW7; -.
DR Proteomes; UP000002494; Chromosome 8.
DR Bgee; ENSRNOG00000024346; Expressed in ovary and 13 other tissues.
DR Genevisible; Q5HZW7; RN.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0001953; P:negative regulation of cell-matrix adhesion; ISS:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0035313; P:wound healing, spreading of epidermal cells; ISS:UniProtKB.
DR InterPro; IPR026184; PLET1.
DR PANTHER; PTHR22527; PTHR22527; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Differentiation; Glycoprotein; GPI-anchor; Lipoprotein;
KW Membrane; Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..236
FT /note="Placenta-expressed transcript 1 protein"
FT /id="PRO_0000320956"
FT PROPEP 237..255
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424670"
FT LIPID 236
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
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 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 255 AA; 26849 MW; FD5E1B2EB8CB7091 CRC64;
MPALRTLLPH LGLFLCLALC FSPSFSLSNN ESCILYDQVY PSDNLINASA EEVSGENTTY
TVTVPVNDSV SAVILKAEKD NKPVGTWSGA YEKCNNSVVY NLTSLNNSAF QTNWTVPSSE
DVTKVNLTIF IVINRTATVS SVKLEPKETS SLASTPESQT SAMTTAMTSA MTTAKTTAVA
TNSSTDVTSD NSTAVTTANS TAVTTANSTA VTTAKTTTMT TATTTAKSLA IRTLCSPLAG
ALHILLVFLI SKLLF