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Entry version 185 (02 Dec 2020)
Sequence version 1 (01 Feb 1991)
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Protein

Follicle-stimulating hormone receptor

Gene

Fshr

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

G protein-coupled receptor for follitropin, the follicle-stimulating hormone. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways.By similarity

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionG-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-375281, Hormone ligand-binding receptors

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Follicle-stimulating hormone receptor
Short name:
FSH-R
Alternative name(s):
Follitropin receptor
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Fshr
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Rat genome database

More...
RGDi
2632, Fshr

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini18 – 365ExtracellularSequence analysisAdd BLAST348
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei366 – 386Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini387 – 397CytoplasmicSequence analysisAdd BLAST11
Transmembranei398 – 420Helical; Name=2Sequence analysisAdd BLAST23
Topological domaini421 – 442ExtracellularSequence analysisAdd BLAST22
Transmembranei443 – 464Helical; Name=3Sequence analysisAdd BLAST22
Topological domaini465 – 484CytoplasmicSequence analysisAdd BLAST20
Transmembranei485 – 507Helical; Name=4Sequence analysisAdd BLAST23
Topological domaini508 – 527ExtracellularSequence analysisAdd BLAST20
Transmembranei528 – 549Helical; Name=5Sequence analysisAdd BLAST22
Topological domaini550 – 572CytoplasmicSequence analysisAdd BLAST23
Transmembranei573 – 596Helical; Name=6Sequence analysisAdd BLAST24
Topological domaini597 – 607ExtracellularSequence analysisAdd BLAST11
Transmembranei608 – 629Helical; Name=7Sequence analysisAdd BLAST22
Topological domaini630 – 692CytoplasmicSequence analysisAdd BLAST63

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi191N → Q: Reduces N-glycosylation level. 1 Publication1
Mutagenesisi199N → Q: Does not affect N-glycosylation level. 1 Publication1
Mutagenesisi293N → Q: Reduces N-glycosylation level. 1 Publication1
Mutagenesisi387T → I: Reduces interaction with ARRB2; when associated with I-389 and N-394. 1 Publication1
Mutagenesisi389S → I: Reduces interaction with ARRB2; when associated with I-387 and N-394. 1 Publication1
Mutagenesisi394T → N: Reduces interaction with ARRB2; when associated with I-387 and I-389. 1 Publication1
Mutagenesisi407D → N: Reduces interaction with ARRB2. 1 Publication1
Mutagenesisi548Y → F: Reduces interaction with ARRB2. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL4288

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000001277518 – 692Follicle-stimulating hormone receptorAdd BLAST675

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi18 ↔ 25PROSITE-ProRule annotation
Disulfide bondi23 ↔ 32PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi191N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi199N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi275 ↔ 345By similarity
Disulfide bondi276 ↔ 355By similarity
Disulfide bondi276 ↔ 292By similarity
Disulfide bondi292 ↔ 337By similarity
Glycosylationi293N-linked (GlcNAc...) asparagine1 Publication1
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei334SulfotyrosineBy similarity1
Disulfide bondi441 ↔ 516PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

N-glycosylated; indirectly required for FSH-binding, possibly via a conformational change that allows high affinity binding of hormone.1 Publication
Sulfated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P20395

PRoteomics IDEntifications database

More...
PRIDEi
P20395

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P20395, 3 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P20395

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P20395

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Sertoli cells and ovarian granulosa cells.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000016783, Expressed in female gonad and 2 other tissues

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimer. Functions as a homotrimer binding the FSH hormone heterodimer composed of CGA and FSHB (By similarity).

Interacts with ARRB2 (PubMed:12850288).

Interacts with APPL2; interaction is independent of follicle stimulating hormone stimulation (By similarity).

By similarity1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000022802

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P20395

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P20395

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini18 – 46LRRNTAdd BLAST29
<p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati49 – 72LRR 1Add BLAST24
Repeati73 – 97LRR 2Add BLAST25
Repeati98 – 118LRR 3Add BLAST21
Repeati119 – 143LRR 4Add BLAST25
Repeati144 – 169LRR 5Add BLAST26
Repeati170 – 192LRR 6Add BLAST23
Repeati193 – 216LRR 7Add BLAST24
Repeati217 – 240LRR 8Add BLAST24
Repeati241 – 259LRR 9Add BLAST19

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family. FSH/LSH/TSH subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Leucine-rich repeat, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2087, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000158952

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_006130_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P20395

Identification of Orthologs from Complete Genome Data

More...
OMAi
HNFHTRN

Database of Orthologous Groups

More...
OrthoDBi
257031at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P20395

TreeFam database of animal gene trees

More...
TreeFami
TF316814

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002272, FSH_rcpt
IPR024635, GnHR_TM
IPR000276, GPCR_Rhodpsn
IPR017452, GPCR_Rhodpsn_7TM
IPR002131, Gphrmn_rcpt_fam
IPR001611, Leu-rich_rpt
IPR026906, LRR_5
IPR000372, LRRNT

The PANTHER Classification System

More...
PANTHERi
PTHR24372:SF5, PTHR24372:SF5, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00001, 7tm_1, 1 hit
PF12369, GnHR_trans, 1 hit
PF13306, LRR_5, 2 hits
PF01462, LRRNT, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01143, FSHRECEPTOR
PR00373, GLYCHORMONER
PR00237, GPCRRHODOPSN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00013, LRRNT, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00237, G_PROTEIN_RECEP_F1_1, 1 hit
PS50262, G_PROTEIN_RECEP_F1_2, 1 hit
PS51450, LRR, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P20395-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALLLVSLLA FLGTGSGCHH WLCHCSNRVF LCQDSKVTEI PTDLPRNAIE
60 70 80 90 100
LRFVLTKLRV IPKGSFAGFG DLEKIEISQN DVLEVIEADV FSNLPKLHEI
110 120 130 140 150
RIEKANNLLY INPEAFQNLP SLRYLLISNT GIKHLPAVHK IQSLQKVLLD
160 170 180 190 200
IQDNINIHIV ARNSFMGLSF ESVILWLSKN GIEEIHNCAF NGTQLDELNL
210 220 230 240 250
SDNNNLEELP NDVFQGASGP VILDISRTKV HSLPNHGLEN LKKLRARSTY
260 270 280 290 300
RLKKLPNLDK FVTLMEASLT YPSHCCAFAN LKRQISELHP ICNKSILRQD
310 320 330 340 350
IDDMTQIGDQ RVSLIDDEPS YGKGSDMMYN EFDYDLCNEV VDVTCSPKPD
360 370 380 390 400
AFNPCEDIMG YNILRVLIWF ISILAITGNT TVLVVLTTSQ YKLTVPRFLM
410 420 430 440 450
CNLAFADLCI GIYLLLIASV DIHTKSQYHN YAIDWQTGAG CDAAGFFTVF
460 470 480 490 500
ASELSVYTLT AITLERWHTI THAMQLECKV QLRHAASVMV LGWTFAFAAA
510 520 530 540 550
LFPIFGISSY MKVSICLPMD IDSPLSQLYV MALLVLNVLA FVVICGCYTH
560 570 580 590 600
IYLTVRNPTI VSSSSDTKIA KRMATLIFTD FLCMAPISFF AISASLKVPL
610 620 630 640 650
ITVSKAKILL VLFYPINSCA NPFLYAIFTK NFRRDFFILL SKFGCYEMQA
660 670 680 690
QIYRTETSSA THNFHARKSH CSSAPRVTNS YVLVPLNHSS QN
Length:692
Mass (Da):77,681
Last modified:February 1, 1991 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i267EA78C7CFD8EC6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti172 – 175Missing in AAB21415 (PubMed:1738373).Curated4
Sequence conflicti252L → W in AAB21415 (PubMed:1738373).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L02842 mRNA Translation: AAA41175.1
S81198 S81178 Genomic DNA Translation: AAB21415.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A34548

NCBI Reference Sequences

More...
RefSeqi
NP_954707.1, NM_199237.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000022802; ENSRNOP00000022802; ENSRNOG00000016783

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25449

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25449

UCSC genome browser

More...
UCSCi
RGD:2632, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Sequence-structure-function-analysis of glycoprotein hormone receptors

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02842 mRNA Translation: AAA41175.1
S81198 S81178 Genomic DNA Translation: AAB21415.2
PIRiA34548
RefSeqiNP_954707.1, NM_199237.1

3D structure databases

SMRiP20395
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022802

Chemistry databases

BindingDBiP20395
ChEMBLiCHEMBL4288

Protein family/group databases

Information system for G protein-coupled receptors (GPCRs)

More...
GPCRDBi
Search...

PTM databases

GlyGeniP20395, 3 sites
iPTMnetiP20395
PhosphoSitePlusiP20395

Proteomic databases

PaxDbiP20395
PRIDEiP20395

Genome annotation databases

EnsembliENSRNOT00000022802; ENSRNOP00000022802; ENSRNOG00000016783
GeneIDi25449
KEGGirno:25449
UCSCiRGD:2632, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2492
RGDi2632, Fshr

Phylogenomic databases

eggNOGiKOG2087, Eukaryota
GeneTreeiENSGT00940000158952
HOGENOMiCLU_006130_1_1_1
InParanoidiP20395
OMAiHNFHTRN
OrthoDBi257031at2759
PhylomeDBiP20395
TreeFamiTF316814

Enzyme and pathway databases

ReactomeiR-RNO-375281, Hormone ligand-binding receptors

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P20395

Gene expression databases

BgeeiENSRNOG00000016783, Expressed in female gonad and 2 other tissues

Family and domain databases

InterProiView protein in InterPro
IPR002272, FSH_rcpt
IPR024635, GnHR_TM
IPR000276, GPCR_Rhodpsn
IPR017452, GPCR_Rhodpsn_7TM
IPR002131, Gphrmn_rcpt_fam
IPR001611, Leu-rich_rpt
IPR026906, LRR_5
IPR000372, LRRNT
PANTHERiPTHR24372:SF5, PTHR24372:SF5, 1 hit
PfamiView protein in Pfam
PF00001, 7tm_1, 1 hit
PF12369, GnHR_trans, 1 hit
PF13306, LRR_5, 2 hits
PF01462, LRRNT, 1 hit
PRINTSiPR01143, FSHRECEPTOR
PR00373, GLYCHORMONER
PR00237, GPCRRHODOPSN
SMARTiView protein in SMART
SM00013, LRRNT, 1 hit
PROSITEiView protein in PROSITE
PS00237, G_PROTEIN_RECEP_F1_1, 1 hit
PS50262, G_PROTEIN_RECEP_F1_2, 1 hit
PS51450, LRR, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFSHR_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P20395
Secondary accession number(s): Q64183
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: December 2, 2020
This is version 185 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
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