GP107_HUMAN
ID GP107_HUMAN Reviewed; 600 AA.
AC Q5VW38; A6NJ53; Q2TB81; Q5JPA3; Q5VW39; Q96T26; Q9H658; Q9HCE8;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Protein GPR107;
DE AltName: Full=Lung seven transmembrane receptor 1;
DE Flags: Precursor;
GN Name=GPR107; Synonyms=KIAA1624, LUSTR1;
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 2).
RA Edgar A.J., Polak J.M.;
RT "Novel putative G protein-coupled receptors cloned from lung.";
RL J. Anat. 200:202-202(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Small intestine;
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 GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-600 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-600 (ISOFORM 2).
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP FUNCTION.
RX PubMed=22933024; DOI=10.1152/ajpregu.00336.2012;
RA Yosten G.L., Redlinger L.J., Samson W.K.;
RT "Evidence for an interaction of neuronostatin with the orphan G protein-
RT coupled receptor, GPR107.";
RL Am. J. Physiol. 303:R941-R949(2012).
RN [10]
RP FUNCTION, CLEAVAGE BY FURIN, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-182,
RP AND DISULFIDE BOND.
RX PubMed=25031321; DOI=10.1074/jbc.m114.589275;
RA Tafesse F.G., Guimaraes C.P., Maruyama T., Carette J.E., Lory S.,
RA Brummelkamp T.R., Ploegh H.L.;
RT "GPR107, a G-protein-coupled receptor essential for intoxication by
RT Pseudomonas aeruginosa exotoxin A, localizes to the Golgi and is cleaved by
RT furin.";
RL J. Biol. Chem. 289:24005-24018(2014).
CC -!- FUNCTION: Has been proposed to act as a receptor for neuronostatin, a
CC peptide derived from the somatostatin/SST precursor (PubMed:22933024).
CC Involved in blood sugar regulation through the induction of glucagon in
CC response to low glucose (By similarity). {ECO:0000250|UniProtKB:D3ZWZ9,
CC ECO:0000269|PubMed:22933024}.
CC -!- FUNCTION: (Microbial infection) Required for intoxication by
CC Pseudomonas aeruginosa exotoxin A and Campylobacter jejuni CDT. May
CC contribute to the retrograde transport of bacterial toxins, including
CC cholera toxin, from the trans-Golgi network to the endoplasmic
CC reticulum. {ECO:0000269|PubMed:25031321}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:D3ZWZ9};
CC Multi-pass membrane protein {ECO:0000305}. Golgi apparatus, trans-Golgi
CC network membrane {ECO:0000269|PubMed:25031321}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5VW38-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VW38-2; Sequence=VSP_014436;
CC Name=3;
CC IsoId=Q5VW38-3; Sequence=VSP_014434, VSP_014435;
CC -!- PTM: Cleaved by FURIN to yield two fragments of 17 and 35 kDa that
CC remain associated via a disulfide bond. {ECO:0000269|PubMed:25031321}.
CC -!- SIMILARITY: Belongs to the LU7TM family. {ECO:0000305}.
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DR EMBL; AF376725; AAK57695.1; -; mRNA.
DR EMBL; AK026244; BAB15408.1; -; mRNA.
DR EMBL; AL136141; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL360004; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL392105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87924.1; -; Genomic_DNA.
DR EMBL; BC110518; AAI10519.1; -; mRNA.
DR EMBL; AB046844; BAB13450.1; -; mRNA.
DR EMBL; AL834359; CAI46205.1; -; mRNA.
DR CCDS; CCDS35162.1; -. [Q5VW38-2]
DR CCDS; CCDS48041.1; -. [Q5VW38-1]
DR RefSeq; NP_001130029.1; NM_001136557.1. [Q5VW38-1]
DR RefSeq; NP_001130030.1; NM_001136558.1.
DR RefSeq; NP_066011.2; NM_020960.4. [Q5VW38-2]
DR AlphaFoldDB; Q5VW38; -.
DR BioGRID; 121743; 71.
DR IntAct; Q5VW38; 10.
DR MINT; Q5VW38; -.
DR STRING; 9606.ENSP00000361483; -.
DR ChEMBL; CHEMBL4630835; -.
DR TCDB; 9.A.14.22.2; the g-protein-coupled receptor (gpcr) family.
DR GlyConnect; 1660; 2 N-Linked glycans (1 site).
DR GlyGen; Q5VW38; 3 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q5VW38; -.
DR PhosphoSitePlus; Q5VW38; -.
DR BioMuta; GPR107; -.
DR DMDM; 68565572; -.
DR EPD; Q5VW38; -.
DR jPOST; Q5VW38; -.
DR MassIVE; Q5VW38; -.
DR MaxQB; Q5VW38; -.
DR PaxDb; Q5VW38; -.
DR PeptideAtlas; Q5VW38; -.
DR PRIDE; Q5VW38; -.
DR ProteomicsDB; 65517; -. [Q5VW38-1]
DR ProteomicsDB; 65518; -. [Q5VW38-2]
DR ProteomicsDB; 65519; -. [Q5VW38-3]
DR Antibodypedia; 31467; 153 antibodies from 26 providers.
DR DNASU; 57720; -.
DR Ensembl; ENST00000347136.11; ENSP00000336988.7; ENSG00000148358.20. [Q5VW38-2]
DR Ensembl; ENST00000372406.5; ENSP00000361483.1; ENSG00000148358.20. [Q5VW38-1]
DR Ensembl; ENST00000610997.1; ENSP00000483750.1; ENSG00000148358.20. [Q5VW38-1]
DR GeneID; 57720; -.
DR KEGG; hsa:57720; -.
DR MANE-Select; ENST00000347136.11; ENSP00000336988.7; NM_020960.5; NP_066011.2. [Q5VW38-2]
DR UCSC; uc004bzd.3; human. [Q5VW38-1]
DR CTD; 57720; -.
DR DisGeNET; 57720; -.
DR GeneCards; GPR107; -.
DR HGNC; HGNC:17830; GPR107.
DR HPA; ENSG00000148358; Low tissue specificity.
DR MIM; 618490; gene.
DR neXtProt; NX_Q5VW38; -.
DR OpenTargets; ENSG00000148358; -.
DR PharmGKB; PA28854; -.
DR VEuPathDB; HostDB:ENSG00000148358; -.
DR eggNOG; KOG2569; Eukaryota.
DR GeneTree; ENSGT00940000160451; -.
DR HOGENOM; CLU_020277_4_1_1; -.
DR InParanoid; Q5VW38; -.
DR OMA; PQGEWES; -.
DR OrthoDB; 1427067at2759; -.
DR PhylomeDB; Q5VW38; -.
DR TreeFam; TF314804; -.
DR PathwayCommons; Q5VW38; -.
DR SignaLink; Q5VW38; -.
DR BioGRID-ORCS; 57720; 16 hits in 1080 CRISPR screens.
DR ChiTaRS; GPR107; human.
DR GeneWiki; GPR107; -.
DR GenomeRNAi; 57720; -.
DR Pharos; Q5VW38; Tbio.
DR PRO; PR:Q5VW38; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5VW38; protein.
DR Bgee; ENSG00000148358; Expressed in endometrium epithelium and 209 other tissues.
DR ExpressionAtlas; Q5VW38; baseline and differential.
DR Genevisible; Q5VW38; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032050; F:clathrin heavy chain binding; IBA:GO_Central.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IBA:GO_Central.
DR InterPro; IPR009637; GPR107/GPR108-like.
DR PANTHER; PTHR21229; PTHR21229; 1.
DR Pfam; PF06814; Lung_7-TM_R; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW Golgi apparatus; Membrane; Reference proteome; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..39
FT /evidence="ECO:0000255"
FT CHAIN 40..600
FT /note="Protein GPR107"
FT /id="PRO_0000021340"
FT TOPO_DOM 40..263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..293
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 294..314
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 315..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..368
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..498
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 499..519
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 520..524
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 525..544
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..600
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 157..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 109..228
FT /evidence="ECO:0000269|PubMed:25031321"
FT VAR_SEQ 298..300
FT /note="MAA -> GFH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014434"
FT VAR_SEQ 301..600
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_014435"
FT VAR_SEQ 436..483
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.1"
FT /id="VSP_014436"
FT VARIANT 189
FT /note="A -> P (in dbSNP:rs640343)"
FT /id="VAR_030863"
FT MUTAGEN 182
FT /note="R->A: Loss of furin cleavage."
FT /evidence="ECO:0000269|PubMed:25031321"
FT CONFLICT 250
FT /note="N -> D (in Ref. 2; BAB15408)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="H -> R (in Ref. 6; BAB13450)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="Q -> R (in Ref. 6; BAB13450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 600 AA; 66990 MW; 679D414C0EB9F205 CRC64;
MAALAPVGSP ASRGPRLAAG LRLLPMLGLL QLLAEPGLGR VHHLALKDDV RHKVHLNTFG
FFKDGYMVVN VSSLSLNEPE DKDVTIGFSL DRTKNDGFSS YLDEDVNYCI LKKQSVSVTL
LILDISRSEV RVKSPPEAGT QLPKIIFSRD EKVLGQSQEP NVNPASAGNQ TQKTQDGGKS
KRSTVDSKAM GEKSFSVHNN GGAVSFQFFF NISTDDQEGL YSLYFHKCLG KELPSDKFTF
SLDIEITEKN PDSYLSAGEI PLPKLYISMA FFFFLSGTIW IHILRKRRND VFKIHWLMAA
LPFTKSLSLV FHAIDYHYIS SQGFPIEGWA VVYYITHLLK GALLFITIAL IGTGWAFIKH
ILSDKDKKIF MIVIPLQVLA NVAYIIIEST EEGTTEYGLW KDSLFLVDLL CCGAILFPVV
WSIRHLQEAS ATDGKGDSMG PLQQRANLRA GSRIESHHFA QADLELLASS CPPASVSQRA
GITAAINLAK LKLFRHYYVL IVCYIYFTRI IAFLLKLAVP FQWKWLYQLL DETATLVFFV
LTGYKFRPAS DNPYLQLSQE EEDLEMESVV TTSGVMESMK KVKKVTNGSV EPQGEWEGAV
