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PR00528

Identifier
GLCORTICOIDR  [View Relations]  [View Alignment]  
Accession
PR00528
No. of Motifs
6
Creation Date
07-JUN-1996  (UPDATE 07-JUN-1999)
Title
Glucocorticoid receptor (3C nuclear receptor) signature
Database References
PRINTS; PR00398 STRDHORMONER
INTERPRO; IPR001409
PDB; 1GDC
SCOP; 1GDC
Literature References
1. NUCLEAR RECEPTORS NOMENCLATURE COMMITTEE
A unified nomenclature system for the nuclear receptor superfamily.
CELL 97 161-163 (1999).
 
2. NISHIKAWA, J-I., KITAURA, M., IMAGAWA, M. AND NISHIHARA, T.
Vitamin D receptor contains multiple dimerisation interfaces that
are functionally different.
NUCLEIC ACIDS RES. 23(4) 606-611 (1995).
 
3. DE VOS, P., SCHMITT, J., VERHOEVEN, G. AND STUNNENBERG, G.
Human androgen receptor expressed in HeLa cells activates transcription
in vitro.
NUCLEIC ACIDS RES. 22(7) 1161-1166 (1994).
 
4. MING-JER, T. AND O'MALLEY, B.
Molecular mechanisms of action of steroid/thyroid receptor superfamily
members.
ANNU.REV.BIOCHEMISTRY 63 451-486 (1994).
 
5. BEATO, M., HERRLICH, P. AND SCHUTZ, G.
Steroid hormone receptors: many actors in search of a plot.
CELL 83 851-857 (1995).

Documentation
Steroid or nuclear hormone receptors (NRs) constitute an important super-
family of transcription regulators that are involved in widely diverse 
physiological functions, including control of embryonic development, cell
differentiation and homeostasis [1]. Members of the superfamily include the
steroid hormone receptors and receptors for thyroid hormone, retinoids, 
1,25-dihydroxy-vitamin D3 and a variety of other ligands. The proteins 
function as dimeric molecules in nuclei to regulate the transcription of 
target genes in a ligand-responsive manner [1-5]. In addition to C-terminal
ligand-binding domains, these nuclear receptors contain a highly-conserved,
N-terminal zinc-finger that mediates specific binding to target DNA 
sequences, termed ligand-responsive elements. In the absence of ligand,
steroid hormone receptors are thought to be weakly associated with nuclear
components; hormone binding greatly increases receptor affinity.
 
NRs are extremely important in medical research, a large number of them
being implicated in diseases such as cancer, diabetes, hormone resistance
syndromes, etc. [1]. While several NRs act as ligand-inducible transcription
factors, many do not yet have a defined ligand and are accordingly termed 
"orphan" receptors. During the last decade, more than 300 NRs have been
described, many of which are orphans, which cannot easily be named due to 
current nomenclature confusions in the literature. However, a new system 
has recently been introduced in an attempt to rationalise the increasingly 
complex set of names used to describe superfamily members [1].
 
The glucocorticoid receptor consists of 3 functional and structural
domains: an N-terminal (modulatory) domain; a DNA binding domain that
mediates specific binding to target DNA sequences (ligand-responsive
elements); and a hormone binding domain. The N-terminal domain is unique
to the glucocorticoid receptors; it spans the first 440 residues, and is
primarily responsible for transcriptional activation. The smaller (around
65 residues), highly-conserved central portion of the protein is the DNA 
binding domain, which plays a role in DNA binding specificity, homo-
dimerisation and in interactions with other proteins. The hormone binding 
domain comprises approximately 250 residues at the C-terminus of the
receptor. This domain mediates receptor activity via interaction with heat
shock proteins and cyclophilins, or with hormone. For more information, see
the GRR resource at http://biochem1.basic-sci.georgetown.edu/GRR/GRR.html.
 
GLCORTICOIDR is a 6-element fingerprint that provides a signature for the
glucocorticoid receptors. The fingerprint was derived from an initial 
alignment of 5 sequences: the motifs span the N-terminal modulatory domain
preceding the highly-conserved zinc-binding region shared by the steroid
hormone receptor family. Two iterations on OWL28.0 were required to reach
convergence, at which point a true set comprising 9 sequences was
identified. Two partial matches were also found (GCR_SHEEP and S76851),
both of which are fragments.
 
An update on SPTR37_9f identified a true set of 11 sequences.
Summary Information
11 codes involving  6 elements
0 codes involving 5 elements
0 codes involving 4 elements
0 codes involving 3 elements
0 codes involving 2 elements
Composite Feature Index
6111111111111
5000000
4000000
3000000
2000000
123456
True Positives
GCR_AOTNA     GCR_CAVPO     GCR_HUMAN     GCR_MOUSE     
GCR_RAT GCR_SAGOE GCR_SAIBB GCR_TUPGB
GCR_XENLA O08624 O46567
Sequence Titles
GCR_AOTNA   GLUCOCORTICOID RECEPTOR (GR) - AOTUS NANCYMAAE (OWL MONKEY). 
GCR_CAVPO GLUCOCORTICOID RECEPTOR (GR) - CAVIA PORCELLUS (GUINEA PIG).
GCR_HUMAN GLUCOCORTICOID RECEPTOR (GR) - HOMO SAPIENS (HUMAN).
GCR_MOUSE GLUCOCORTICOID RECEPTOR (GR) - MUS MUSCULUS (MOUSE).
GCR_RAT GLUCOCORTICOID RECEPTOR (GR) - RATTUS NORVEGICUS (RAT).
GCR_SAGOE GLUCOCORTICOID RECEPTOR (GR) - SAGUINUS OEDIPUS (COTTON-TOP TAMARIN).
GCR_SAIBB GLUCOCORTICOID RECEPTOR (GR) - SAIMIRI BOLIVIENSIS BOLIVIENSIS (BOLIVIAN SQUIRREL MONKEY).
GCR_TUPGB GLUCOCORTICOID RECEPTOR (GR) - TUPAIA GLIS BELANGERI (COMMON TREE SHREW).
GCR_XENLA GLUCOCORTICOID RECEPTOR (GR) - XENOPUS LAEVIS (AFRICAN CLAWED FROG).
O08624 GLUCOCORTICOID RECEPTOR - RATTUS NORVEGICUS (RAT).
O46567 GLUCOCORTICOID RECEPTOR (GR) - SAIMIRI SCIUREUS (COMMON SQUIRREL MONKEY).
Scan History
OWL28_0    2  50   NSINGLE    
SPTR37_9f 2 12 NSINGLE
Initial Motifs
Motif 1  width=21
Element Seqn Id St Int Rpt
VIDFYKTVRGGATVKVSASSP GCR_CAVPO 25 25 -
VMDLYKTLRGGATVKVSASSP GCR_MOUSE 27 27 -
VMDFYKSLRGGATVKVSASSP GCR_RAT 27 27 -
VMDFYKTLRGGATVKVSASSP GCRB_HUMAN 26 26 -
VMDFYKTLRGGATVKVSASSP GCRA_HUMAN 26 26 -

Motif 2 width=21
Element Seqn Id St Int Rpt
PDLSKAVSLSMGLYMGETETK GCR_RAT 97 49 -
PDLSKAVSLSMGLYMGETETK GCRA_HUMAN 76 29 -
PDLSKAVSLSMGLYMGETETK GCRB_HUMAN 76 29 -
PDLSKAVSLSMGLYMGETETK GCR_MOUSE 85 37 -
PDLSKAVSLSMGLYMGETETK GCR_CAVPO 75 29 -

Motif 3 width=21
Element Seqn Id St Int Rpt
QLGLSSGETDFRLLEESIANL GCR_MOUSE 118 12 -
QISLSSGETDLKLLEESIANL GCRB_HUMAN 109 12 -
QISLSSGETDLKLLEESIANL GCRA_HUMAN 109 12 -
QLGLSSGETDFRLLEESIANL GCR_RAT 130 12 -
QISLPSGETDFRLLEESIANL GCR_CAVPO 108 12 -

Motif 4 width=22
Element Seqn Id St Int Rpt
QVKTEKDDFIELCTPGVIKQEK GCR_RAT 295 144 -
QVKIGKEDFIELCTPGVIKQEK GCR_CAVPO 271 142 -
QVKTEKEDFIELCTPGVIKQEK GCRB_HUMAN 275 145 -
QVKTEKEDFIELCTPGVIKQEK GCRA_HUMAN 275 145 -
QVKTEKDDFIELCTPGVIKQEK GCR_MOUSE 283 144 -

Motif 5 width=19
Element Seqn Id St Int Rpt
HGVSTSGGQMYHYDMNTAS GCRB_HUMAN 322 25 -
HGVSTSGGQMYHYDMNTAS GCR_RAT 342 25 -
HGVSTSGGQMYHYDMNTAS GCR_MOUSE 330 25 -
HGVSTSGGQMYHYDMNTAS GCR_CAVPO 318 25 -
HGVSTSGGQMYHYDMNTAS GCRA_HUMAN 322 25 -

Motif 6 width=20
Element Seqn Id St Int Rpt
NFPGRSVFSNGYSSPGMRPD GCR_RAT 402 41 -
NFPGRSVFSNGYSSPGLRPD GCR_CAVPO 378 41 -
NFAGRSVFSNGYSSPGMRPD GCR_MOUSE 390 41 -
NFPGRTVFSNGYSSPSMRPD GCRB_HUMAN 382 41 -
NFPGRTVFSNGYSSPSMRPD GCRA_HUMAN 382 41 -
Final Motifs
Motif 1  width=21
Element Seqn Id St Int Rpt
VMDFYKTLRGGATVKVSASSP GCR_HUMAN 26 26 -
VMDFCKILRGGATLKVSVSST GCR_SAGOE 26 26 -
VMDFCKILRGGATLKVSVSST GCR_SAIBB 26 26 -
VMDFCKILRGGATLKVSVSST O46567 26 26 -
VMDFYKSLRGGATVKVSASSP GCR_RAT 27 27 -
VMDFYKSLRGGATVKVSASSP O08624 27 27 -
VMDFSKILRGGATLKVSVSST GCR_AOTNA 26 26 -
VMDLYKTLRGGATVKVSASSP GCR_MOUSE 27 27 -
VIDFYKTVRGGATVKVSASSP GCR_CAVPO 25 25 -
VMDFYKTRRGGATVKVFMPSP GCR_TUPGB 26 26 -
VIEFFGNYRGGVSVSVSASCP GCR_XENLA 29 29 -

Motif 2 width=21
Element Seqn Id St Int Rpt
PDLSKAVSLSMGLYMGETETK GCR_HUMAN 76 29 -
PDLSKAVSLSMGLYMGETETK GCR_SAGOE 76 29 -
PDLSKAVSLSMGLYMGETETK GCR_SAIBB 76 29 -
PDLSKAVSLSMGLYMGETETK O46567 76 29 -
PDLSKAVSLSMGLYMGETETK GCR_RAT 97 49 -
PDLSKAVSLSMGLYMGETETK O08624 97 49 -
PDLSKAVSLSMGLYMGETETK GCR_AOTNA 76 29 -
PDLSKAVSLSMGLYMGETETK GCR_MOUSE 85 37 -
PDLSKAVSLSMGLYMGETETK GCR_CAVPO 75 29 -
PDLSKAVSLSMGLYMGETETK GCR_TUPGB 76 29 -
PDLSKAVSLSMGLYMGESDTK GCR_XENLA 85 35 -

Motif 3 width=21
Element Seqn Id St Int Rpt
QISLSSGETDLKLLEESIANL GCR_HUMAN 109 12 -
QISLSSGETDLQLLEESIANL GCR_SAGOE 109 12 -
QISLSSGETDLQLLEESIANL GCR_SAIBB 109 12 -
QISLSSGETDLQLLEESIANL O46567 109 12 -
QLGLSSGETDFRLLEESIANL GCR_RAT 130 12 -
QLGLSSGETDFRLLEESIANL O08624 130 12 -
QISLSSGETDLQLLEESIANL GCR_AOTNA 109 12 -
QLGLSSGETDFRLLEESIANL GCR_MOUSE 118 12 -
QISLPSGETDFRLLEESIANL GCR_CAVPO 108 12 -
QITLSSGETNLQLLEESIANL GCR_TUPGB 109 12 -
QIGISTGETDFSLLEESIANL GCR_XENLA 118 12 -

Motif 4 width=22
Element Seqn Id St Int Rpt
QVKTEKEDFIELCTPGVIKQEK GCR_HUMAN 275 145 -
QVKTEKEDFIELCTPGVIKQEK GCR_SAGOE 275 145 -
QVKTEKEDFIELCTPGVIKQEK GCR_SAIBB 275 145 -
QVKTEKEDFIELCTPGVIKQEK O46567 275 145 -
QVKTEKDDFIELCTPGVIKQEK GCR_RAT 295 144 -
QVKTEKDDFIELCTPGVIKQEK O08624 295 144 -
QVKTEKEDFIELCTPGVIKQEK GCR_AOTNA 275 145 -
QVKTEKDDFIELCTPGVIKQEK GCR_MOUSE 283 144 -
QVKIGKEDFIELCTPGVIKQEK GCR_CAVPO 271 142 -
QVKTEKEDFIELCTPGVIKQEK GCR_TUPGB 275 145 -
QVKTEKEDYIELCTPGVVNEEK GCR_XENLA 276 137 -

Motif 5 width=19
Element Seqn Id St Int Rpt
HGVSTSGGQMYHYDMNTAS GCR_HUMAN 322 25 -
HGVSTSGGQMYHYDMNTAS GCR_SAGOE 322 25 -
HGVSTSGGQMYHYDMNTAS GCR_SAIBB 322 25 -
HGVSTSGGQMYHYDMNTAS O46567 322 25 -
HGVSTSGGQMYHYDMNTAS GCR_RAT 342 25 -
HGVSTSGGQMYHYDMNTAS O08624 342 25 -
HGVSTSGGQMYHYDMNTAS GCR_AOTNA 322 25 -
HGVSTSGGQMYHYDMNTAS GCR_MOUSE 330 25 -
HGVSTSGGQMYHYDMNTAS GCR_CAVPO 318 25 -
HGVSTSGGQMYHYDMNTAT GCR_TUPGB 322 25 -
HGVSTSGGQMYHYDLNTAT GCR_XENLA 323 25 -

Motif 6 width=20
Element Seqn Id St Int Rpt
NFPGRTVFSNGYSSPSMRPD GCR_HUMAN 382 41 -
NFPGRTVFSNGYSSPSMRPD GCR_SAGOE 382 41 -
NFPGRTVFSNGYSSPSMRPD GCR_SAIBB 382 41 -
NFPGRTVFSNGYSSPSMRPD O46567 382 41 -
NFPGRSVFSNGYSSPGMRPD GCR_RAT 402 41 -
NFPGRSVFSNGYSSPGMRPD O08624 402 41 -
NFPGRTVFSNGYSSPSMRPD GCR_AOTNA 382 41 -
NFAGRSVFSNGYSSPGMRPD GCR_MOUSE 390 41 -
NFPGRSVFSNGYSSPGLRPD GCR_CAVPO 378 41 -
NFSGRSVFSNGYSSPGMRPD GCR_TUPGB 382 41 -
NFPNRSVFSNGYSSPGIRSD GCR_XENLA 382 40 -