ALEX_RAT
ID ALEX_RAT Reviewed; 738 AA.
AC Q9Z213; Q924W1;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Protein ALEX;
DE AltName: Full=Alternative gene product encoded by XL-exon;
GN Name=Gnas {ECO:0000312|RGD:2716}; Synonyms=Gnas1 {ECO:0000312|RGD:2716};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAD03033.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Wistar {ECO:0000312|EMBL:AAD03033.1};
RA Wang Y.Z., Kehlenbach R.H., Huttner W.B.;
RT "The XL-domain of rat XLas is encoded by a single exon.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAC39212.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 227-738, INTERACTION WITH GNAS XLAS ISOFORMS,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=Wistar {ECO:0000312|EMBL:AAD03033.1};
RX PubMed=11447126; DOI=10.1093/emboj/20.14.3849;
RA Klemke M., Kehlenbach R.H., Huttner W.B.;
RT "Two overlapping reading frames in a single exon encode interacting
RT proteins -- a novel way of gene usage.";
RL EMBO J. 20:3849-3860(2001).
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.
CC {ECO:0000269|PubMed:11447126}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11447126};
CC Peripheral membrane protein {ECO:0000269|PubMed:11447126}. Cell
CC projection, ruffle {ECO:0000269|PubMed:11447126}. Note=Predominantly
CC associated with cell membrane ruffles.
CC -!- MISCELLANEOUS: This protein is produced by a bicistronic gene which
CC also produces the guanine nucleotide-binding protein G(s) subunit alpha
CC from an overlapping reading frame. {ECO:0000269|PubMed:11447126}.
CC -!- SIMILARITY: Belongs to the ALEX family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC39212.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF093569; AAD03033.1; -; Genomic_DNA.
DR EMBL; X84047; CAC39212.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q9Z213; -.
DR PRIDE; Q9Z213; -.
DR RGD; 2716; Gnas.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030142; C:COPI-coated Golgi to ER transport vesicle; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0005834; C:heterotrimeric G-protein complex; IDA:RGD.
DR GO; GO:0031224; C:intrinsic component of membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0055037; C:recycling endosome; IDA:RGD.
DR GO; GO:0001726; C:ruffle; IDA:RGD.
DR GO; GO:0032588; C:trans-Golgi network membrane; ISO:RGD.
DR GO; GO:0043014; F:alpha-tubulin binding; IDA:RGD.
DR GO; GO:0031698; F:beta-2 adrenergic receptor binding; IPI:RGD.
DR GO; GO:0051430; F:corticotropin-releasing hormone receptor 1 binding; IPI:RGD.
DR GO; GO:0031748; F:D1 dopamine receptor binding; IPI:RGD.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:RGD.
DR GO; GO:0031681; F:G-protein beta-subunit binding; IDA:RGD.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IDA:RGD.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0005159; F:insulin-like growth factor receptor binding; IPI:RGD.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:RGD.
DR GO; GO:0031852; F:mu-type opioid receptor binding; IDA:RGD.
DR GO; GO:0019904; F:protein domain specific binding; IPI:RGD.
DR GO; GO:0071880; P:adenylate cyclase-activating adrenergic receptor signaling pathway; ISO:RGD.
DR GO; GO:0007191; P:adenylate cyclase-activating dopamine receptor signaling pathway; ISO:RGD.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:RGD.
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:RGD.
DR GO; GO:0055074; P:calcium ion homeostasis; IMP:RGD.
DR GO; GO:0051216; P:cartilage development; ISO:RGD.
DR GO; GO:0050890; P:cognition; ISO:RGD.
DR GO; GO:0048589; P:developmental growth; ISO:RGD.
DR GO; GO:0006306; P:DNA methylation; ISO:RGD.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; ISO:RGD.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; ISO:RGD.
DR GO; GO:0001958; P:endochondral ossification; ISO:RGD.
DR GO; GO:0006112; P:energy reserve metabolic process; ISO:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:RGD.
DR GO; GO:0071514; P:genomic imprinting; ISO:RGD.
DR GO; GO:0060789; P:hair follicle placode formation; ISO:RGD.
DR GO; GO:0035264; P:multicellular organism growth; ISO:RGD.
DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD.
DR GO; GO:0040015; P:negative regulation of multicellular organism growth; ISO:RGD.
DR GO; GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD.
DR GO; GO:0070527; P:platelet aggregation; ISO:RGD.
DR GO; GO:0043950; P:positive regulation of cAMP-mediated signaling; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0043547; P:positive regulation of GTPase activity; ISO:RGD.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IMP:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; IMP:RGD.
DR GO; GO:0040032; P:post-embryonic body morphogenesis; ISO:RGD.
DR GO; GO:0009791; P:post-embryonic development; ISO:RGD.
DR GO; GO:2000828; P:regulation of parathyroid hormone secretion; ISO:RGD.
DR GO; GO:0009966; P:regulation of signal transduction; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:RGD.
DR GO; GO:0071107; P:response to parathyroid hormone; ISO:RGD.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD.
DR GO; GO:0007606; P:sensory perception of chemical stimulus; IBA:GO_Central.
DR GO; GO:0001501; P:skeletal system development; ISO:RGD.
DR GO; GO:0043588; P:skin development; ISO:RGD.
DR GO; GO:0001894; P:tissue homeostasis; ISO:RGD.
DR InterPro; IPR001019; Gprotein_alpha_su.
DR PANTHER; PTHR10218; PTHR10218; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Membrane; Reference proteome.
FT CHAIN 1..738
FT /note="Protein ALEX"
FT /id="PRO_0000253966"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..689
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 30..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..501
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..575
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..669
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 80341 MW; 51EA2B3A7D9D018A CRC64;
MSPSPTRLTV RSVDPLKTPN LTSRAPVRPS RKSKWAETTA HLQRKPCHSR SNSPAWEISG
PPWSSLDHLD PIRHQSLQPS DFGARTPTGA HPGLGAYSPP PEEAMPFEFN EPAQEDRCQP
PLQVPDLAPG GPEAWVSRAL PAEPGNLGFE NTGFREDYSP PPEESVPFQL DGEEFGGDSP
PPDSASHATN RHWRFEFPTV AVPSTLCLRP ARTRLPSGSR APLADHARLS DLLTSHTTFP
QWRSPDPCLR LAEPPLGSTT TPLSIWTAPQ SQVMARPSKS REPQLRASTQ RDPHLSDKQP
RQETALSAAP LQRRQKSPPS SEEKDPPPNL KQCISSQLLL RSPERTLPKP IRTQLHTQFF
RSVLRKSEES QPCPPIFRLL LKMRAQMSGQ NQTEGQPQPP LPSPKTTENQ PPPPPPSQPP
SQPLSQPPSQ PPSQPPSQLP RQSLTPKPSL PPGQSPTPKR SPQPRQPLPR RRSLPPGQPP
SPLRSPLPGL SLLPEPIQPP GLSLEPQRCQ PLLGQPPLEQ PMQVLWSGEP GHSRLLQPLG
HPSLPAQQLP PEQPLLPAQS LPAGQPLPPQ AGPILDPPAR RSRLLTRLLR GLLRGRVPGL
TNTNVAEAAA GMRLRPASAR SSPPAMSRKK GPLAASSGFC GETAALASPG ATQSGATRSA
TSSPEPSEAA SVYLSVPDHD PSAPGRPRIL WKRGANRCAK KPWRCESRSA QIRNAASSST
SNWRRRRWTT CVHTACCF
