PLET1_MESAU
ID PLET1_MESAU Reviewed; 242 AA.
AC Q5W9T8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 33.
DE RecName: Full=Placenta-expressed transcript 1 protein;
DE AltName: Full=Antigen AgK114;
DE Flags: Precursor;
GN Name=PLET1;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=15516716; DOI=10.1248/bpb.27.1742;
RA Tatefuji T., Arai C., Okura T., Kayano T., Mori T., Takakura-Yamamoto R.,
RA Takeuchi M., Ohta T., Kurimoto M.;
RT "Identification of the novel membrane-associated protein AgK114 on hamster
RT keratinocytes recognized by a monoclonal antibody K114.";
RL Biol. Pharm. Bull. 27:1742-1749(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 -!- TISSUE SPECIFICITY: Present at high level in the dermal sheath cells
CC near the bulge area of the hair follicle and in the differentiated
CC sebocytes of the normal adult skin (at protein level).
CC {ECO:0000269|PubMed:15516716}.
CC -!- INDUCTION: Following tissue damages of the skin.
CC {ECO:0000269|PubMed:15516716}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: GPI-anchored. {ECO:0000250}.
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DR EMBL; AB154828; BAD69587.1; -; mRNA.
DR AlphaFoldDB; Q5W9T8; -.
DR STRING; 10036.XP_005069349.1; -.
DR eggNOG; ENOG502RTZP; Eukaryota.
DR Proteomes; UP000189706; Unplaced.
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: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 1: Evidence at protein 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..223
FT /note="Placenta-expressed transcript 1 protein"
FT /id="PRO_0000320953"
FT PROPEP 224..242
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000424668"
FT LIPID 223
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 242 AA; 25595 MW; 223D190D747E1E8F CRC64;
MAVLRSLLPQ LGLFLCLALC FSPALSASYN DPCTVFDTIS TTNLRVNITA EGSGENITYT
VWVHVNSSVS VVILKAVNQD NKPVGTWVGA TQECNDSSVL YRVTPSDNSD FQATWIVPNS
EDITKVNLHV LMAIGNGTAA VTSVNLGEPQ TSTPLRPTPE ISETNQTTTM TTDKTPAMTT
AKTPAMTTAK TTAKTTAKTT VKTTAMTTAK TTAKSLAVNA LGSPLAGALH ILLVFLISKL
LF