Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Steroidogenic factor 1

Gene

NR5A1

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Transcriptional activator. Seems to be essential for sexual differentiation and formation of the primary steroidogenic tissues. Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional activity. Binds phosphatidylcholine and phospholipids with a phosphatidylinositol (PI) headgroup, in particular PI(3,4)P2 and PI(3,4,5)P3. Activated by the phosphorylation of NR5A1 by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei341Lipid headgroup; via amide nitrogenBy similarity1
Binding sitei436Lipid headgroupBy similarity1
Binding sitei440Lipid headgroupBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi10 – 85Nuclear receptorPROSITE-ProRule annotationAdd BLAST76
Zinc fingeri13 – 33NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri49 – 73NR C4-typePROSITE-ProRule annotationAdd BLAST25

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, DNA-binding, Receptor
Biological processTranscription, Transcription regulation
LigandLipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SSC-383280 Nuclear Receptor transcription pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Steroidogenic factor 1
Short name:
SF-1
Short name:
STF-1
Alternative name(s):
Adrenal 4-binding protein
Fushi tarazu factor homolog 1
Nuclear receptor subfamily 5 group A member 1
Steroid hormone receptor Ad4BP
Gene namesi
Name:NR5A1
Synonyms:FTZF1
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000537331 – 461Steroidogenic factor 1Add BLAST461

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei34N6-acetyllysineBy similarity1
Modified residuei38N6-acetyllysineBy similarity1
Modified residuei72N6-acetyllysineBy similarity1
Cross-linki119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei203Phosphoserine; by CDK7By similarity1

Post-translational modificationi

Acetylation stimulates the transcriptional activity.By similarity
Sumoylation reduces CDK7-mediated phosphorylation on Ser-203.By similarity
Phosphorylated on Ser-203 by CDK7. This phosphorylation promotes transcriptional activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP79387
PRIDEiP79387

Interactioni

Subunit structurei

Binds DNA as a monomer (By similarity). Part of a complex consisting of SFPQ, NONO and NR5A1. Interacts with NR0B2, NCOA2 and PPARGC1A. Interacts with DGKQ and CDK7. Binds to and activated by HIPK3 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000005989

Structurei

3D structure databases

ProteinModelPortaliP79387
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini222 – 459NR LBDPROSITE-ProRule annotationAdd BLAST238

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni230 – 461Important for dimerizationAdd BLAST232

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri13 – 33NR C4-typePROSITE-ProRule annotationAdd BLAST21
Zinc fingeri49 – 73NR C4-typePROSITE-ProRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4218 Eukaryota
ENOG410YWC2 LUCA
GeneTreeiENSGT00870000136388
HOGENOMiHOG000063718
HOVERGENiHBG106677
InParanoidiP79387
KOiK08560

Family and domain databases

Gene3Di3.30.50.10, 1 hit
InterProiView protein in InterPro
IPR035500 NHR_like_dom_sf
IPR016355 NR5_fam
IPR000536 Nucl_hrmn_rcpt_lig-bd
IPR001723 Nuclear_hrmn_rcpt
IPR001628 Znf_hrmn_rcpt
IPR013088 Znf_NHR/GATA
PANTHERiPTHR24086 PTHR24086, 1 hit
PfamiView protein in Pfam
PF00104 Hormone_recep, 1 hit
PF00105 zf-C4, 1 hit
PIRSFiPIRSF002530 Nuc_orph_FTZ-F1, 1 hit
PRINTSiPR00398 STRDHORMONER
PR00047 STROIDFINGER
SMARTiView protein in SMART
SM00430 HOLI, 1 hit
SM00399 ZnF_C4, 1 hit
SUPFAMiSSF48508 SSF48508, 2 hits
PROSITEiView protein in PROSITE
PS51843 NR_LBD, 1 hit
PS00031 NUCLEAR_REC_DBD_1, 1 hit
PS51030 NUCLEAR_REC_DBD_2, 1 hit

Sequencei

Sequence statusi: Complete.

P79387-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT
60 70 80 90 100
ESQSCKIDKT QRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK
110 120 130 140 150
RDRALKQQKK AQIRANGFKL ETGPPMGVAP PPPPPPDYML PPGLHAPEPK
160 170 180 190 200
GLAAGPPTGP LGDFGAPTLP MAVPSAHGPL AGYLYPAFPG RAIKSEYPEP
210 220 230 240 250
YASPPQPGPP YGYPEPFSGG PGVPELIVQL LQLEPDEDQV RARIVGCLQE
260 270 280 290 300
PAKGRPDQPA PFSLLCRMAD QTFISIVDWA RRCMVFKELE VADQMTLLQN
310 320 330 340 350
CWSELLVFDH IYRQIQHGKE GSILLVTGQE VELTTVAAQA GSLLHGLVLR
360 370 380 390 400
AQELVLQLHA LQLDRQEFVC LKFLILFSLD VKFLNNHSLV KDAQEKANAA
410 420 430 440 450
LLDYTLCHYP HCGDKFQQLL LCLVEVRALS MQAKEYLYHK HLGNEMPRNN
460
LLIEMLQAKQ T
Length:461
Mass (Da):51,575
Last modified:November 13, 2007 - v3
Checksum:i0F5051A722FF64B2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4S → W in AAC64209 (PubMed:9724033).Curated1
Sequence conflicti32S → T in AAC64209 (PubMed:9724033).Curated1
Sequence conflicti87R → G in AAC64209 (PubMed:9724033).Curated1
Sequence conflicti306L → H in AAC64209 (PubMed:9724033).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U84399 mRNA Translation: AAC64209.1
AP009124 Genomic DNA Translation: BAF45331.1
RefSeqiNP_999344.1, NM_214179.1
XP_013849311.1, XM_013993857.1
UniGeneiSsc.16099
Ssc.82462
Ssc.82473

Genome annotation databases

EnsembliENSSSCT00000034748; ENSSSCP00000047808; ENSSSCG00000005588
GeneIDi397368
KEGGissc:397368

Similar proteinsi

Entry informationi

Entry nameiSTF1_PIG
AccessioniPrimary (citable) accession number: P79387
Secondary accession number(s): A2BD07
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 13, 2007
Last modified: March 28, 2018
This is version 132 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health