ID   PLET1_BOVIN             Reviewed;         242 AA.
AC   A5D7U1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Placenta-expressed transcript 1 protein;
DE   Flags: Precursor;
GN   Name=PLET1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Placenta;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250}.
CC       Note=Localized at the apical membrane of the most differentiated
CC       keratinocytes of the outer root sheath (ORS), clustered mainly in
CC       planar regions of the plasma membrane at the base of microvilli.
CC       {ECO:0000250}.
CC   -!- PTM: N-glycosylated. {ECO:0000250}.
CC   -!- CAUTION: For human, rat and golden hamster orthologs, a GPI-anchor has
CC       been predicted. However, in the case of pig and bovine, no GPI-anchor
CC       motifs have been detected, but it does not rule out the possibility of
CC       a GPI-anchor instead of a single-pass type I membrane protein.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI40682.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BC140681; AAI40682.1; ALT_INIT; mRNA.
DR   RefSeq; NP_001107010.1; NM_001113538.1.
DR   AlphaFoldDB; A5D7U1; -.
DR   STRING; 9913.ENSBTAP00000020999; -.
DR   PaxDb; A5D7U1; -.
DR   GeneID; 505518; -.
DR   KEGG; bta:505518; -.
DR   CTD; 505518; -.
DR   eggNOG; ENOG502RTZP; Eukaryota.
DR   HOGENOM; CLU_099483_0_0_1; -.
DR   InParanoid; A5D7U1; -.
DR   OrthoDB; 1306307at2759; -.
DR   TreeFam; TF344172; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..242
FT                   /note="Placenta-expressed transcript 1 protein"
FT                   /id="PRO_0000320951"
FT   TOPO_DOM        27..220
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        242
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          162..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        28
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   242 AA;  26609 MW;  20206AD46038AC0F CRC64;
     MAILRSLLLP LGLLLCLWLL CSPASCTNST TNCKPFLSVT TKKSSLIHIS PDIYKSNTLY
     TVSTQVSHGI ISVVLEARDQ NKSVIGSWEN PSDHCEGRAE YYLKGNFSTL FKAKWMSPNS
     TDITTVKINI YTVNSLRNAE LDSITLPEVG TVTVKHVSTK QVITTPTHKP TPAPPKPTTN
     PQKTTTNHSI PTTSLPKPTT SLYTSHPKLT TTHKSSANRA FLCPVREAIQ ILFIFLIGTL
     LF