PMID- 10397730
OWN - NLM
STAT- MEDLINE
DCOM- 19990805
LR  - 20061115
IS  - 0006-4971 (Print)
IS  - 0006-4971 (Linking)
VI  - 94
IP  - 2
DP  - 1999 Jul 15
TI  - Structural and functional implications of the intron/exon organization of the
      human endothelial cell protein C/activated protein C receptor (EPCR) gene:
      comparison with the structure of CD1/major histocompatibility complex alpha1 and 
      alpha2 domains.
PG  - 632-41
AB  - The endothelial cell protein C/activated protein C receptor (EPCR) is located
      primarily on the surface of the large vessels of the vasculature. In vitro
      studies suggest that it is involved in the protein C anticoagulant pathway. We
      report the organization and nucleotide sequence of the human EPCR gene. It spans 
      approximately 6 kbp of genomic DNA, with a transcription initiation point 79 bp
      upstream of the translation initiation (Met) codon in close proximity to a TATA
      box and other promoter element consensus sequences. The human EPCR gene has been 
      localized to 20q11.2 and consists of four exons interrupted by three introns, all
      of which obey the GT-AG rule. Exon I encodes the 5' untranslated region and the
      signal peptide, and exon IV encodes the transmembrane domain, the cytoplasmic
      tail, and the 3' untranslated region. Exons II and III encode most of the
      extracellular region of the EPCR. These exons have been found to correspond to
      those encoding the alpha1 and alpha2 domains of the CD1/major histocompatibility 
      complex (MHC) class I superfamily. Flanking and intervening introns are of the
      same phase (phase I) and the position of the intervening intron is identically
      located. Secondary structure prediction for the amino acid sequence of exons II
      and III corresponds well with the actual secondary structure elements determined 
      for the alpha1 and alpha2 domains of HLA-A2 and murine CD1.1 from crystal
      structures. These findings suggest that the EPCR folds with a beta-sheet platform
      supporting two alpha-helical regions collectively forming a potential binding
      pocket for protein C/activated protein C.
FAU - Simmonds, R E
AU  - Simmonds RE
AD  - Department of Haematology, Imperial College School of Medicine, London, UK.
      r.simmonds@ic.ac.uk
FAU - Lane, D A
AU  - Lane DA
LA  - eng
SI  - GENBANK/AF106202
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Blood
JT  - Blood
JID - 7603509
RN  - 0 (Antigens, CD1)
RN  - 0 (Blood Coagulation Factors)
RN  - 0 (Codon)
RN  - 0 (DNA, Complementary)
RN  - 0 (HLA-A2 Antigen)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (activated protein C receptor)
SB  - AIM
SB  - IM
MH  - Amino Acid Sequence
MH  - Antigens, CD1/*genetics
MH  - Base Sequence
MH  - *Blood Coagulation Factors
MH  - Chromosome Mapping
MH  - Chromosomes, Human, Pair 20/genetics
MH  - Cloning, Molecular
MH  - Codon/genetics
MH  - DNA, Complementary/genetics
MH  - Exons/genetics
MH  - *Genes
MH  - Genes, MHC Class I
MH  - HLA-A2 Antigen/*genetics
MH  - Humans
MH  - Introns/genetics
MH  - Molecular Sequence Data
MH  - Receptors, Cell Surface/*genetics
MH  - Regulatory Sequences, Nucleic Acid
MH  - Sequence Alignment
MH  - Sequence Homology
MH  - Structure-Activity Relationship
MH  - Transcription, Genetic
EDAT- 1999/07/09 00:00
MHDA- 1999/07/09 00:01
CRDT- 1999/07/09 00:00
PHST- 1999/07/09 00:00 [pubmed]
PHST- 1999/07/09 00:01 [medline]
PHST- 1999/07/09 00:00 [entrez]
PST - ppublish
SO  - Blood. 1999 Jul 15;94(2):632-41.