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Protein

Adhesion G protein-coupled receptor F5

Gene

Adgrf5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor that plays a critical role in lung surfactant homeostasis. May play a role in controlling adipocyte function.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiR-RNO-5683826. Surfactant metabolism.

Protein family/group databases

MEROPSiP02.032.

Names & Taxonomyi

Protein namesi
Recommended name:
Adhesion G protein-coupled receptor F5
Alternative name(s):
G-protein coupled hepta-helical receptor Ig-hepta
G-protein coupled receptor 116
Gene namesi
Name:Adgrf5
Synonyms:Gpr116, Gprhep
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi621679. Adgrf5.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini25 – 1016ExtracellularCuratedAdd BLAST992
Transmembranei1017 – 1036Helical; Name=1Sequence analysisAdd BLAST20
Topological domaini1037 – 1055CytoplasmicCuratedAdd BLAST19
Transmembranei1056 – 1078Helical; Name=2Sequence analysisAdd BLAST23
Topological domaini1079 – 1097ExtracellularCuratedAdd BLAST19
Transmembranei1098 – 1120Helical; Name=3Sequence analysisAdd BLAST23
Topological domaini1121 – 1131CytoplasmicCuratedAdd BLAST11
Transmembranei1132 – 1154Helical; Name=4Sequence analysisAdd BLAST23
Topological domaini1155 – 1173ExtracellularCuratedAdd BLAST19
Transmembranei1174 – 1196Helical; Name=5Sequence analysisAdd BLAST23
Topological domaini1197 – 1216CytoplasmicCuratedAdd BLAST20
Transmembranei1217 – 1239Helical; Name=6Sequence analysisAdd BLAST23
Topological domaini1240 – 1248ExtracellularCurated9
Transmembranei1249 – 1271Helical; Name=7Sequence analysisAdd BLAST23
Topological domaini1272 – 1349CytoplasmicCuratedAdd BLAST78

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi994T → A: Abolishes cleavage. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000001289725 – 1349Adhesion G protein-coupled receptor F5Add BLAST1325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi73N-linked (GlcNAc...)Sequence analysis1
Glycosylationi94N-linked (GlcNAc...)Sequence analysis1
Glycosylationi185N-linked (GlcNAc...)Sequence analysis1
Glycosylationi254N-linked (GlcNAc...)Sequence analysis1
Glycosylationi270N-linked (GlcNAc...)Sequence analysis1
Glycosylationi286N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi291 ↔ 348PROSITE-ProRule annotation
Glycosylationi299N-linked (GlcNAc...)Sequence analysis1
Glycosylationi326N-linked (GlcNAc...)Sequence analysis1
Glycosylationi337N-linked (GlcNAc...)Sequence analysis1
Glycosylationi349N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi389 ↔ 447PROSITE-ProRule annotation
Glycosylationi396N-linked (GlcNAc...)Sequence analysis1
Glycosylationi470N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi490 ↔ 543PROSITE-ProRule annotation
Glycosylationi503N-linked (GlcNAc...)Sequence analysis1
Glycosylationi538N-linked (GlcNAc...)Sequence analysis1
Glycosylationi649N-linked (GlcNAc...)Sequence analysis1
Glycosylationi666N-linked (GlcNAc...)Sequence analysis1
Modified residuei819PhosphoserineCombined sources1
Glycosylationi820N-linked (GlcNAc...)Sequence analysis1
Glycosylationi958N-linked (GlcNAc...)Sequence analysis1
Glycosylationi963N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1085N-linked (GlcNAc...)Sequence analysis1
Modified residuei1303PhosphothreonineBy similarity1
Modified residuei1310PhosphoserineBy similarity1

Post-translational modificationi

Proteolytically cleaved at multiple sites: one in the GPS domain (S1 site) and the other in the SEA domain (S2 site). The proteolytic cleavage at S1 site generates an extracellular subunit and a seven-transmembrane subunit. The proteolytic cleavage at S2 site generates a fragment that undergoes proteolytic cleavage by the processing enzyme furin.2 Publications
Highly glycosylated.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei51 – 52Cleavage; by furin1 Publication2
Sitei223 – 224Cleavage1 Publication2
Sitei993 – 994Cleavage; by autolysis1 Publication2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ9WVT0.
PRIDEiQ9WVT0.

PTM databases

iPTMnetiQ9WVT0.
PhosphoSitePlusiQ9WVT0.

Expressioni

Tissue specificityi

Highly expressed in the lung and to a much lesser extent in the kidney and heart. Dense localization in alveolar walls of the lung and in the intercalated cells of the collecting duct of the kidney.1 Publication

Developmental stagei

Strongly induced postnatally.1 Publication

Gene expression databases

BgeeiENSRNOG00000011154.
ExpressionAtlasiQ9WVT0. baseline and differential.
GenevisibleiQ9WVT0. RN.

Interactioni

Subunit structurei

Homodimer; disulfide-linked (PubMed:10391944). Heterodimer of 2 chains generated by proteolytic processing; the large extracellular N-terminal fragment and the membrane-bound C-terminal fragment predominantly remain associated and non-covalently linked (PubMed:11973329). Fragment generates by the processing enzyme furin remains attached to the extracellular N-terminal fragment (PubMed:16882675). Interacts (via N-terminal extracellular domain) with SFTPD (By similarity).By similarity3 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015223.

Structurei

3D structure databases

ProteinModelPortaliQ9WVT0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini163 – 271SEAPROSITE-ProRule annotationAdd BLAST109
Domaini268 – 366Ig-like 1Add BLAST99
Domaini367 – 464Ig-like 2Add BLAST98
Domaini469 – 559Ig-like 3Add BLAST91
Domaini951 – 1005GPSPROSITE-ProRule annotationAdd BLAST55

Sequence similaritiesi

Contains 1 GPS domain.PROSITE-ProRule annotation
Contains 1 SEA domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4193. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00830000128272.
HOGENOMiHOG000112764.
HOVERGENiHBG051772.
InParanoidiQ9WVT0.
KOiK08458.
PhylomeDBiQ9WVT0.
TreeFamiTF316380.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
3.30.70.960. 1 hit.
InterProiIPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR008078. GPCR_2_Ig-hepta-like_rcpt.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR000082. SEA_dom.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF16489. GAIN. 1 hit.
PF01825. GPS. 1 hit.
PF00047. ig. 1 hit.
PF01390. SEA. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR01695. IGHEPTARCPTR.
SMARTiSM00303. GPS. 1 hit.
SM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
SSF82671. SSF82671. 1 hit.
PROSITEiPS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS50835. IG_LIKE. 3 hits.
PS50024. SEA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9WVT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKSSRTVTLY FVLIVICSSE ATWSRPAEPI VHPLILQEHE LAGEELLRPK
60 70 80 90 100
RAVAVGGPVA EEYTVDVEIS FENVSFLESI RAHLNSLRFP VQGNGTDILS
110 120 130 140 150
MAMTTVCTPT GNDLLCFCEK GYQWPEERCL SSLTCQEHDS ALPGRYCNCL
160 170 180 190 200
KGLPPQGPFC QLPETYITLK IKVRLNIGFQ EDLENTSSAL YRSYKTDLER
210 220 230 240 250
AFRAGYRTLP GFRSVTVTQF TKGSVVVDYI VEVASAPLPG SIHKANEQVI
260 270 280 290 300
QNLNQTYKMD YNSFQGTPSN ETKFTVTPEF IFEGDNVTLE CESEFVSSNT
310 320 330 340 350
SWFYGEKRSD IQNSDKFSIH TSIINNISLV TRLTIFNFTQ HDAGLYGCNV
360 370 380 390 400
TLDIFEYGTV RKLDVTPIRI LAKEERKVVC DNNPISLNCC SENIANWSRI
410 420 430 440 450
EWKQEGKINI EGTPETDLES SCSTYTLKAD GTQCPSGSSG TTVIYTCEFV
460 470 480 490 500
SVYGAKGSKN IAVTFTSVAN LTITPDPISV SEGQSFSITC LSDVSSFDEV
510 520 530 540 550
YWNTSAGIKI HPRFYTMRRY RDGAESVLTV KTSTREWNGT YHCIFRYKNS
560 570 580 590 600
YSIATKDVTV HPLPLESDIM MDPLEASGLC TSSHQFKCCI EENDGEEYIV
610 620 630 640 650
TFHVDSSSFP AEREVIGKQA CYTYSLPGKL PSRCPKDIDV FCHFTNAANS
660 670 680 690 700
SVRSPSMKLT LVPGKNITCQ DPIIGIGEPG KVIQKLCQFA GVSRSPGQTI
710 720 730 740 750
GGTVTYKCVG SQWKEETRAC ISAPINGLLQ LAKALIKSPS QDQKLPKYLR
760 770 780 790 800
DLSVSTGKEE QDIRSSPGSL GAIISILDLL STVPTQVNSE MMRDILATIN
810 820 830 840 850
VILDKSTLNS WEKLLQQQSN QSSQFLQSVE RFSKALELGD STPPFLFHPN
860 870 880 890 900
VQMKSMVIKR GHAQMYQQKF VFTDSDLWGD VAIDECQLGS LQPDSSIVTV
910 920 930 940 950
AFPTLKAILA QDGQRKTPSN SLVMTTTVSH NIVKPFRISM TFKNNHRSGG
960 970 980 990 1000
KPQCVFWNFS LANNTGGWDS SGCTVEDDGR DNRDRVFCKC NHLTSFSILM
1010 1020 1030 1040 1050
SPDSPDPGSL LKILLDIISY IGLGFSIVSL AACLVVEAMV WKSVTKNRTS
1060 1070 1080 1090 1100
YMRHICIVNI ALCLLIADIW FIVAGAIHDG HYPLNETACV AATFFIHFFY
1110 1120 1130 1140 1150
LSVFFWMLTL GLMLFYRLIF ILHDASKSTQ KAIAFSLGYG CPLIISSITV
1160 1170 1180 1190 1200
GVTQPQEVYM RKNACWLNWE DTRALLAFAI PALIIVVVNV SITVVVITKI
1210 1220 1230 1240 1250
LRPSVGDKPG KQEKSSLFQI SKSIGVLTPL LGLTWGFGLA TVIQGSNAVF
1260 1270 1280 1290 1300
HIIFTLLNAF QGLFILLFGC LWDQKVQEAL LHKFSLSRWS SQHSKSTSLG
1310 1320 1330 1340
SSTPVFSMSS PISRRFNNLF GKTGTYNVST PETTSSSVEN SSSAYSLLN
Length:1,349
Mass (Da):149,446
Last modified:November 1, 1999 - v1
Checksum:i104CF1D9A35B1409
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019120 mRNA. Translation: BAA82518.1.
RefSeqiNP_620810.1. NM_139110.1.
XP_006244659.1. XM_006244597.3.
UniGeneiRn.25073.

Genome annotation databases

EnsembliENSRNOT00000015223; ENSRNOP00000015223; ENSRNOG00000011154.
GeneIDi245977.
KEGGirno:245977.
UCSCiRGD:621679. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019120 mRNA. Translation: BAA82518.1.
RefSeqiNP_620810.1. NM_139110.1.
XP_006244659.1. XM_006244597.3.
UniGeneiRn.25073.

3D structure databases

ProteinModelPortaliQ9WVT0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000015223.

Protein family/group databases

MEROPSiP02.032.
GPCRDBiSearch...

PTM databases

iPTMnetiQ9WVT0.
PhosphoSitePlusiQ9WVT0.

Proteomic databases

PaxDbiQ9WVT0.
PRIDEiQ9WVT0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015223; ENSRNOP00000015223; ENSRNOG00000011154.
GeneIDi245977.
KEGGirno:245977.
UCSCiRGD:621679. rat.

Organism-specific databases

CTDi221395.
RGDi621679. Adgrf5.

Phylogenomic databases

eggNOGiKOG4193. Eukaryota.
ENOG410XSD2. LUCA.
GeneTreeiENSGT00830000128272.
HOGENOMiHOG000112764.
HOVERGENiHBG051772.
InParanoidiQ9WVT0.
KOiK08458.
PhylomeDBiQ9WVT0.
TreeFamiTF316380.

Enzyme and pathway databases

ReactomeiR-RNO-5683826. Surfactant metabolism.

Miscellaneous databases

PROiQ9WVT0.

Gene expression databases

BgeeiENSRNOG00000011154.
ExpressionAtlasiQ9WVT0. baseline and differential.
GenevisibleiQ9WVT0. RN.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
3.30.70.960. 1 hit.
InterProiIPR032471. GAIN_dom_N.
IPR017981. GPCR_2-like.
IPR008078. GPCR_2_Ig-hepta-like_rcpt.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
IPR000203. GPS.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR000082. SEA_dom.
[Graphical view]
PfamiPF00002. 7tm_2. 1 hit.
PF16489. GAIN. 1 hit.
PF01825. GPS. 1 hit.
PF00047. ig. 1 hit.
PF01390. SEA. 1 hit.
[Graphical view]
PRINTSiPR00249. GPCRSECRETIN.
PR01695. IGHEPTARCPTR.
SMARTiSM00303. GPS. 1 hit.
SM00409. IG. 2 hits.
SM00408. IGc2. 2 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 2 hits.
SSF82671. SSF82671. 1 hit.
PROSITEiPS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
PS50221. GPS. 1 hit.
PS50835. IG_LIKE. 3 hits.
PS50024. SEA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAGRF5_RAT
AccessioniPrimary (citable) accession number: Q9WVT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.