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Protein

Adhesion G protein-coupled receptor F5

Gene

Adgrf5

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

Keywordsi

Molecular functionG-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi621679 Adgrf5

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

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

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...) asparagineSequence analysis1
Glycosylationi94N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi185N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi254N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi270N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi286N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi291 ↔ 348PROSITE-ProRule annotation
Glycosylationi299N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi326N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi337N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi349N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi389 ↔ 447PROSITE-ProRule annotation
Glycosylationi396N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi470N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi490 ↔ 543PROSITE-ProRule annotation
Glycosylationi503N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi538N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi649N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi666N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei819PhosphoserineCombined sources1
Glycosylationi820N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi958N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi963N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1085N-linked (GlcNAc...) asparagineSequence 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

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG4193 Eukaryota
ENOG410XSD2 LUCA
GeneTreeiENSGT00920000148969
HOGENOMiHOG000112764
HOVERGENiHBG051772
InParanoidiQ9WVT0
KOiK08458
PhylomeDBiQ9WVT0
TreeFamiTF316380

Family and domain databases

Gene3Di2.60.40.10, 2 hits
InterProiView protein in InterPro
IPR032471 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
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013151 Immunoglobulin
IPR000082 SEA_dom
IPR036364 SEA_dom_sf
PfamiView protein in Pfam
PF00002 7tm_2, 1 hit
PF16489 GAIN, 1 hit
PF01825 GPS, 1 hit
PF00047 ig, 1 hit
PF01390 SEA, 1 hit
PRINTSiPR00249 GPCRSECRETIN
PR01695 IGHEPTARCPTR
SMARTiView protein in SMART
SM00303 GPS, 1 hit
SM00409 IG, 2 hits
SM00408 IGc2, 2 hits
SUPFAMiSSF48726 SSF48726, 2 hits
SSF82671 SSF82671, 1 hit
PROSITEiView protein in PROSITE
PS00650 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

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

Similar proteinsi

Entry informationi

Entry nameiAGRF5_RAT
AccessioniPrimary (citable) accession number: Q9WVT0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1999
Last modified: June 20, 2018
This is version 132 of the entry and version 1 of the sequence. See 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

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