PAQR3_HUMAN
ID PAQR3_HUMAN Reviewed; 311 AA.
AC Q6TCH7; A8K5B7; B3KP59; Q6PIQ1; Q86X05; Q8NCP9;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Progestin and adipoQ receptor family member 3 {ECO:0000303|PubMed:16044242};
DE AltName: Full=Progestin and adipoQ receptor family member III;
DE AltName: Full=Raf kinase trapping to Golgi {ECO:0000303|PubMed:18547165};
DE Short=RKTG {ECO:0000303|PubMed:18547165};
GN Name=PAQR3 {ECO:0000312|HGNC:HGNC:30130};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=16044242; DOI=10.1007/s00239-004-0375-2;
RA Tang Y.T., Hu T., Arterburn M., Boyle B., Bright J.M., Emtage P.C.,
RA Funk W.D.;
RT "PAQR proteins: a novel membrane receptor family defined by an ancient 7-
RT transmembrane pass motif.";
RL J. Mol. Evol. 61:372-380(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=18547165; DOI=10.1042/bj20080948;
RA Luo X., Feng L., Jiang X., Xiao F., Wang Z., Feng G.S., Chen Y.;
RT "Characterization of the topology and functional domains of RKTG.";
RL Biochem. J. 414:399-406(2008).
CC -!- FUNCTION: Functions as a spatial regulator of RAF1 kinase by
CC sequestrating it to the Golgi. {ECO:0000269|PubMed:18547165}.
CC -!- INTERACTION:
CC Q6TCH7; P04049: RAF1; NbExp=3; IntAct=EBI-15654365, EBI-365996;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:18547165}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18547165}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6TCH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6TCH7-2; Sequence=VSP_011479;
CC Name=3;
CC IsoId=Q6TCH7-3; Sequence=VSP_011480;
CC Name=4;
CC IsoId=Q6TCH7-4; Sequence=VSP_011477, VSP_011478;
CC -!- TISSUE SPECIFICITY: Widely expressed in a range of tissues.
CC {ECO:0000269|PubMed:16044242}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ADIPOR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG51571.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY424281; AAR08369.1; -; mRNA.
DR EMBL; AK055774; BAG51571.1; ALT_INIT; mRNA.
DR EMBL; AK291232; BAF83921.1; -; mRNA.
DR EMBL; BC029604; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC031256; AAH31256.1; -; mRNA.
DR EMBL; BC047510; AAH47510.1; -; mRNA.
DR CCDS; CCDS34020.1; -. [Q6TCH7-1]
DR RefSeq; NP_001035292.1; NM_001040202.1. [Q6TCH7-1]
DR AlphaFoldDB; Q6TCH7; -.
DR SMR; Q6TCH7; -.
DR BioGRID; 127451; 22.
DR CORUM; Q6TCH7; -.
DR DIP; DIP-46464N; -.
DR IntAct; Q6TCH7; 1.
DR STRING; 9606.ENSP00000421981; -.
DR iPTMnet; Q6TCH7; -.
DR PhosphoSitePlus; Q6TCH7; -.
DR BioMuta; PAQR3; -.
DR DMDM; 51701774; -.
DR EPD; Q6TCH7; -.
DR jPOST; Q6TCH7; -.
DR MassIVE; Q6TCH7; -.
DR MaxQB; Q6TCH7; -.
DR PaxDb; Q6TCH7; -.
DR PeptideAtlas; Q6TCH7; -.
DR PRIDE; Q6TCH7; -.
DR ProteomicsDB; 67380; -. [Q6TCH7-1]
DR ProteomicsDB; 67381; -. [Q6TCH7-2]
DR ProteomicsDB; 67382; -. [Q6TCH7-3]
DR ProteomicsDB; 67383; -. [Q6TCH7-4]
DR Antibodypedia; 55228; 53 antibodies from 10 providers.
DR DNASU; 152559; -.
DR Ensembl; ENST00000395594.2; ENSP00000378959.2; ENSG00000163291.14. [Q6TCH7-3]
DR Ensembl; ENST00000511594.5; ENSP00000425080.1; ENSG00000163291.14. [Q6TCH7-1]
DR Ensembl; ENST00000512733.5; ENSP00000421981.1; ENSG00000163291.14. [Q6TCH7-1]
DR Ensembl; ENST00000512760.5; ENSP00000426875.1; ENSG00000163291.14. [Q6TCH7-4]
DR Ensembl; ENST00000515853.5; ENSP00000422357.1; ENSG00000163291.14. [Q6TCH7-4]
DR GeneID; 152559; -.
DR KEGG; hsa:152559; -.
DR MANE-Select; ENST00000512733.5; ENSP00000421981.1; NM_001040202.2; NP_001035292.1.
DR UCSC; uc003hlp.2; human. [Q6TCH7-1]
DR CTD; 152559; -.
DR DisGeNET; 152559; -.
DR GeneCards; PAQR3; -.
DR HGNC; HGNC:30130; PAQR3.
DR HPA; ENSG00000163291; Low tissue specificity.
DR MIM; 614577; gene.
DR neXtProt; NX_Q6TCH7; -.
DR OpenTargets; ENSG00000163291; -.
DR PharmGKB; PA134952039; -.
DR VEuPathDB; HostDB:ENSG00000163291; -.
DR eggNOG; KOG0748; Eukaryota.
DR GeneTree; ENSGT00940000155291; -.
DR HOGENOM; CLU_190093_0_0_1; -.
DR InParanoid; Q6TCH7; -.
DR OMA; CLESIFW; -.
DR OrthoDB; 1524940at2759; -.
DR PhylomeDB; Q6TCH7; -.
DR TreeFam; TF313640; -.
DR PathwayCommons; Q6TCH7; -.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR SignaLink; Q6TCH7; -.
DR BioGRID-ORCS; 152559; 18 hits in 1081 CRISPR screens.
DR ChiTaRS; PAQR3; human.
DR GenomeRNAi; 152559; -.
DR Pharos; Q6TCH7; Tbio.
DR PRO; PR:Q6TCH7; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q6TCH7; protein.
DR Bgee; ENSG00000163291; Expressed in sperm and 183 other tissues.
DR ExpressionAtlas; Q6TCH7; baseline and differential.
DR Genevisible; Q6TCH7; HS.
DR GO; GO:0005794; C:Golgi apparatus; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:MGI.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IDA:MGI.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IDA:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:MGI.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IPI:MGI.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR InterPro; IPR004254; AdipoR/HlyIII-related.
DR PANTHER; PTHR20855; PTHR20855; 1.
DR Pfam; PF03006; HlyIII; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Golgi apparatus; Membrane; Receptor;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..311
FT /note="Progestin and adipoQ receptor family member 3"
FT /id="PRO_0000218846"
FT TOPO_DOM 1..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 97..105
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..140
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..172
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..201
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..238
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..298
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..311
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 61..71
FT /note="Golgi targeting"
FT REGION 299..303
FT /note="Golgi targeting"
FT VAR_SEQ 62..88
FT /note="SLFILSNETVNIWSHLLGFFLFFTLGI -> RSVCFALWAIIFFPAIGQKKH
FT VEDGWH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011477"
FT VAR_SEQ 89..311
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011478"
FT VAR_SEQ 265..311
FT /note="GQLNYLGSSHQIWHILAVVMLYWWHQSTVYVMQYRHSKPCPDYVSHL -> E
FT NIFRWEITKRTLGGVNNSLQNLYLLV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011479"
FT VAR_SEQ 265..311
FT /note="GQLNYLGSSHQIWHILAVVMLYWWHQSTVYVMQYRHSKPCPDYVSHL -> E
FT SLPR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011480"
FT CONFLICT 30
FT /note="L -> Q (in Ref. 2; BAF83921)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="V -> A (in Ref. 1; AAR08369)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 36217 MW; 8C629920D0F8D785 CRC64;
MHQKLLKSAH YIELGSYQYW PVLVPRGIRL YTYEQIPGSL KDNPYITDGY RAYLPSRLCI
KSLFILSNET VNIWSHLLGF FLFFTLGIYD MTSVLPSASA SREDFVICSI CLFCFQVCML
CSVGYHLFSC HRSEKTCRRW MALDYAGISI GILGCYVSGV FYAFYCNNYW RQVYLITVLA
MILAVFFAQI HPNYLTQQWQ RLRSIIFCSV SGYGVIPTLH WVWLNGGIGA PIVQDFAPRV
IVMYMIALLA FLFYISKVPE RYFPGQLNYL GSSHQIWHIL AVVMLYWWHQ STVYVMQYRH
SKPCPDYVSH L
