Swiss-Prot entry
ID ANDR_PIG STANDARD; PRT; 896 AA.
AC Q9GKL7; Q9GKN9;
DT 05-JUL-2004 (Rel. 44, Created)
DT 05-JUL-2004 (Rel. 44, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Androgen receptor (Dihydrotestosterone receptor).
GN Name=AR; Synonyms=NR3C4;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pituitary;
RA Song J.H., Fahrenkrug S.C., Rohrer G.A., Wise T.H., Ford J.J.;
RT "Sus scrofa androgen receptor (AR) coding sequence.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX MEDLINE=20539123; PubMed=11086548 [NCBI, ExPASy, EBI, Israel, Japan];
RA Trakooljul N., Ponsuksili S., Schellander K., Wimmers K.;
RT "A highly polymorphic repetitive polypyrimidine/polypurine (CCTTT)n
RT sequence in the 5' untranslated sequence of the porcine androgen
RT receptor gene.";
RL Anim. Genet. 31:288-289(2000).
CC -!- FUNCTION: The steroid hormones and their receptors are involved in
CC the regulation of eukaryotic gene expression and affect cellular
CC proliferation and differentiation in target tissues. Activated,
CC but not phosphorylated, by HIPK3 (By similarity).
CC -!- SUBUNIT: Binds DNA as a homodimer. The AR N-terminal poly-Gln
CC region binds Ran resulting in enhancement of AR-mediated
CC transactivation. Ran-binding decreases as the poly-Gln length
CC increases. Interacts with RANBP9. Interacts with HIPK3 in the
CC presence of androgen (By similarity).
CC -!- SUBCELLULAR LOCATION: Nuclear (By similarity).
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain,
CC a DNA-binding domain and a C-terminal steroid-binding domain.
CC Interaction with RANBP9 is mediated by both the N-terminal domain
CC and the DNA-binding domain (By similarity).
CC -!- MISCELLANEOUS: In the absence of ligand, steroid hormone receptors
CC are thought to be weakly associated with nuclear components;
CC hormone binding greatly increases receptor affinity. The hormone-
CC receptor complex appears to recognize discrete DNA sequences
CC upstream of transcriptional start sites.
CC -!- MISCELLANEOUS: Transcriptional activity is enhanced by binding to
CC RANBP9.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR3
CC subfamily.
CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; AF202775; AAG37994.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR EMBL; AF161717; AAG40566.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR HSSP; P10275; 1E3G. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; Q9GKL7; 532-605, 646-895.
DR InterPro; IPR001103; Andrgn_receptor.
DR InterPro; IPR000536; Hrmon_recept_lig.
DR InterPro; IPR008946; Str_ncl_receptor.
DR InterPro; IPR001628; Znf_C4steroid.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF02166; Androgen_recep; 1.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR00521; ANDROGENR.
DR PRINTS; PR00047; STROIDFINGER.
DR ProDom; PD000035; Znf_C4steroid; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q9GKL7.
DR ProtoNet; Q9GKL7.
DR ProtoMap; Q9GKL7.
DR PRESAGE; Q9GKL7.
DR DIP; Q9GKL7.
DR ModBase; Q9GKL7.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW DNA-binding; Nuclear protein; Receptor; Steroid-binding;
KW Transcription; Transcription regulation; Zinc-finger.
FT DOMAIN 1 534 Modulating (By similarity).
FT DNA_BIND 535 608 Nuclear receptor-type.
FT ZN_FING 536 556 C4-type.
FT DOMAIN 548 638 Interaction with HIPK3 (By similarity).
FT ZN_FING 572 596 C4-type.
FT DOMAIN 667 896 Ligand-binding.
FT DOMAIN 55 62 Poly-Gln.
FT DOMAIN 69 75 Poly-Gln.
FT DOMAIN 180 189 Poly-Gln.
FT DOMAIN 364 373 Poly-Pro.
FT DOMAIN 388 394 Poly-Ala.
FT DOMAIN 441 446 Poly-Gly.
FT CONFLICT 13 13 R -> W (in Ref. 2).
FT CONFLICT 75 75 Missing (in Ref. 2).
FT CONFLICT 256 256 D -> G (in Ref. 2).
FT CONFLICT 323 323 A -> E (in Ref. 2).
FT CONFLICT 352 352 R -> N (in Ref. 1).
FT CONFLICT 363 363 G -> R (in Ref. 2).
FT CONFLICT 410 410 P -> S (in Ref. 2).
FT CONFLICT 820 823 VMQE -> ACKR (in Ref. 1).
SQ SEQUENCE 896 AA; 97166 MW; 7C88B3E6765724CD CRC64;
MEVQLGLGRV YPRPPSKTFR GAFQNLFQSV REVIQNPGPR HPEAASAAPP GARLQQQQLQ
QQETSPRRQQ QQQQQPSEDG SPQVQSRGPT GYLALDEKQQ PSQQQSAPEC HPESGCTPEP
GAASAASKGL QQQPPAPPDE DDSAAPSTLS LLGPTFPGLS SCSTDLKDIL SEAGTMQLLQ
QQQQQQQQQE AVSEGNSSGR AREATGAPIS SKDSYLGGSS TISDSAKELC KAVSVSMGLG
VEALEHLSPG EQLRGDCMYA PLLTGPPSVR PTPCAPLAEC KGSLLDDGPG KSNEETAEYS
PFKAGYTKGL DSESLGCSSG GEAGGSGTLE LPSALSLYKS GALDDVAAYP SRDYYNFPLA
LAGPPPPPPP PHPHARIKLE NPLDYGSAWA AAAAQCRYGD LASLHGGGAP GPGSGSPSAT
SSSSWHTLFT AEESQLYGPC GGGGGGSAGE AGAVAPYGYT RPPQGLAGQE GDLAIPDIWY
PGGVVSRVPY PSPSCVKSEM GPWMESYSGP YGDMRLEPTR DHVLPIDYYF PPQKTCLICG
DEASGCHYGA LTCGSCKVFF KRAAEGKQKY LCASRNDCTI DKFRRKNCPS CRLRKCYEAG
MTLGARKLKK LGNLKLQEEG EASSATSPTE EPAQKLTVSH IEGYECQPIF LNVLEAIEPG
VVCAGHDNNQ PDSFAALLSS LNELGERQLV HVVKWAKALP GFRNLHVDDQ MAVIQYSWMG
LMVFAMGWRS FTNVNSRMLY FAPDLVFNEY RMHKSRMYSQ CVRMRHLSQE FGWLQITPQE
FLCMKALLLF SIIPVDGLKN QKFFDELRMN YIKELDRIIV MQEKNPTSCS RRFYQLTKLL
DSVQPIAREL HQFTFDLLIK SHMVSVDFPE MMAEIISVQV PKILSGKVKP IYFHTQ
//