ALEX_MOUSE
ID ALEX_MOUSE Reviewed; 725 AA.
AC Q6R0H6; A6PW72; Q8BIR3;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Protein ALEX;
DE AltName: Full=Alternative gene product encoded by XL-exon;
GN Name=Gnas {ECO:0000312|MGI:MGI:95777};
GN Synonyms=Gnas1 {ECO:0000312|MGI:MGI:95777};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000312|EMBL:AAS00602.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAS00602.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAS00602.1};
RX PubMed=15148396; DOI=10.1073/pnas.0308758101;
RA Abramowitz J., Grenet D., Birnbaumer M., Torres H.N., Birnbaumer L.;
RT "XL alpha-s, the extra-long form of the alpha subunit of the Gs G protein,
RT is significantly longer than suspected, and so is its companion Alex.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8366-8371(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC26987.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 297-725.
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26987.1};
RC TISSUE=Pituitary {ECO:0000312|EMBL:BAC26987.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: May inhibit the adenylyl cyclase-stimulating activity of
CC guanine nucleotide-binding protein G(s) subunit alpha which is produced
CC from the same locus in a different open reading frame.
CC {ECO:0000250|UniProtKB:P84996}.
CC -!- SUBUNIT: Interacts with the N-terminal region of the XLas isoforms of
CC guanine nucleotide-binding protein G(s) subunit alpha. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell
CC projection, ruffle {ECO:0000250}. Note=Predominantly associated with
CC cell membrane ruffles. {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces guanine nucleotide-binding protein G(s) subunit alpha
CC from an overlapping reading frame. {ECO:0000250|UniProtKB:Q9Z213}.
CC -!- SIMILARITY: Belongs to the ALEX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC26987.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY519502; AAS00602.1; -; mRNA.
DR EMBL; AL593857; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK030489; BAC26987.1; ALT_INIT; mRNA.
DR CCDS; CCDS50817.1; -.
DR RefSeq; NP_001070975.1; NM_001077507.2.
DR RefSeq; NP_001297014.1; NM_001310085.1.
DR RefSeq; NP_963911.1; NM_201617.2.
DR RefSeq; NP_963912.1; NM_201618.2.
DR AlphaFoldDB; Q6R0H6; -.
DR BioGRID; 199972; 37.
DR iPTMnet; Q6R0H6; -.
DR SwissPalm; Q6R0H6; -.
DR REPRODUCTION-2DPAGE; IPI00471141; -.
DR PRIDE; Q6R0H6; -.
DR ProteomicsDB; 296394; -.
DR Antibodypedia; 4152; 809 antibodies from 44 providers.
DR DNASU; 14683; -.
DR Ensembl; ENSMUST00000109088; ENSMUSP00000104716; ENSMUSG00000027523.
DR Ensembl; ENSMUST00000186907; ENSMUSP00000139839; ENSMUSG00000027523.
DR GeneID; 14683; -.
DR UCSC; uc008oeu.2; mouse.
DR CTD; 2778; -.
DR MGI; MGI:95777; Gnas.
DR VEuPathDB; HostDB:ENSMUSG00000027523; -.
DR GeneTree; ENSGT00940000156300; -.
DR HOGENOM; CLU_437395_0_0_1; -.
DR BioGRID-ORCS; 14683; 12 hits in 74 CRISPR screens.
DR ChiTaRS; Gnas; mouse.
DR Proteomes; UP000000589; Chromosome 2.
DR Bgee; ENSMUSG00000027523; Expressed in superior cervical ganglion and 269 other tissues.
DR ExpressionAtlas; Q6R0H6; baseline and differential.
DR Genevisible; Q6R0H6; MM.
DR GO; GO:0030142; C:COPI-coated Golgi to ER transport vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; ISO:MGI.
DR GO; GO:0031224; C:intrinsic component of membrane; ISO:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0001726; C:ruffle; ISO:MGI.
DR GO; GO:0042383; C:sarcolemma; ISO:MGI.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:MGI.
DR GO; GO:0010856; F:adenylate cyclase activator activity; ISO:MGI.
DR GO; GO:0047391; F:alkylglycerophosphoethanolamine phosphodiesterase activity; ISO:MGI.
DR GO; GO:0043014; F:alpha-tubulin binding; ISO:MGI.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; ISO:MGI.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; ISO:MGI.
DR GO; GO:0031748; F:D1 dopamine receptor binding; ISO:MGI.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:0031681; F:G-protein beta-subunit binding; ISO:MGI.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; ISO:MGI.
DR GO; GO:0003924; F:GTPase activity; ISO:MGI.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; ISO:MGI.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISO:MGI.
DR GO; GO:0031852; F:mu-type opioid receptor binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISO:MGI.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; IGI:MGI.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0007188; P:adenylate cyclase-modulating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; ISO:MGI.
DR GO; GO:0055074; P:calcium ion homeostasis; ISO:MGI.
DR GO; GO:0051216; P:cartilage development; IMP:MGI.
DR GO; GO:0071870; P:cellular response to catecholamine stimulus; ISO:MGI.
DR GO; GO:0071380; P:cellular response to prostaglandin E stimulus; ISO:MGI.
DR GO; GO:0050890; P:cognition; ISO:MGI.
DR GO; GO:0048589; P:developmental growth; ISO:MGI.
DR GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR GO; GO:0006112; P:energy reserve metabolic process; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0071514; P:genomic imprinting; IMP:MGI.
DR GO; GO:0060789; P:hair follicle placode formation; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; ISO:MGI.
DR GO; GO:0070527; P:platelet aggregation; ISO:MGI.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:MGI.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IMP:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISO:MGI.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; IMP:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:2000828; P:regulation of parathyroid hormone secretion; IMP:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0071107; P:response to parathyroid hormone; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0043588; P:skin development; IMP:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Membrane; Reference proteome.
FT CHAIN 1..725
FT /note="Protein ALEX"
FT /id="PRO_0000253965"
FT REGION 1..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 638..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..480
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 297
FT /note="Q -> E (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 725 AA; 79084 MW; 273F2244509B1573 CRC64;
MSPSPTRLAV RSVDPQKTPN LTSKAPARPS RKSEWVETTA HLRRKPCHSR HNSPAWEISG
PPWSSQDHLG PHQASKPSTQ RFWSPGPPLA RAQAWEPIPP HQKKLCHLSS TSLPRETIAS
LPCKSQTLRQ EVRKHWSPEL FPRSPGTSDL KTLASEKTTA LPLKNLCHFR SVEKNSGAIA
HPQDSRESSH KSALAASSRQ SRSRVRSASL PPRTRLPSGS EAPLTDHSAR LSDLLLTSHA
TAPRWRSPDP CLRLAEPPLG STTTPLSIWT APQSQVMARP SKSREPQIRA SAQRDPQLSE
KQPRWKEALP PPLRWKEKSP LRREGTDLPP SLKQWMPSQP LLPKPSLPDL MLELLRIPRC
SQIARAMPEK TGQPQERLQI SSRILKNSKK PQLSAPILTE GQPQSPQPLL PSPSLKAAEI
QPPSQPPRQS LPPRPSLPPG QPLSPRWSPQ PRQSLPPWRS LPPGQPLSPP RSPLPGQSPL
LEPIRPLEQS LAPQQCQPLL GQLPLGQPMQ VHWSGEPGHS QLLPPLGHPF LPAQQLPPGQ
PLLPAQSLLA GQPLPPPAGP ILDPPAPRSR LLTRLLRGLL RGRLPGLTST SGAEAAAGTR
HRLASARSSP PVMSRKKGPP AASSGFCGET AALACPGATR SGATQSATSS PEPSEAASVY
PSVPDHDPSA PGRPRILWRR GANRCAKKPL RCESRSAQIR NAASSSTSNW RRRRWTTCVH
TACCF
