GA2L2_RAT
ID GA2L2_RAT Reviewed; 857 AA.
AC D3ZUE1;
DT 16-OCT-2019, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=GAS2-like protein 2;
GN Name=Gas2l2 {ECO:0000312|RGD:1307868};
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|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0000305}
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ADORA2A, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=23994616; DOI=10.1016/j.bbamcr.2013.08.009;
RA Wu Y.C., Lai H.L., Chang W.C., Lin J.T., Liu Y.J., Chern Y.;
RT "A novel Galphas-binding protein, Gas-2 like 2, facilitates the signaling
RT of the A2A adenosine receptor.";
RL Biochim. Biophys. Acta 1833:3145-3154(2013).
CC -!- FUNCTION: Involved in the cross-linking of microtubules and
CC microfilaments (By similarity). Regulates microtubule dynamics and
CC stability by interacting with microtubule plus-end tracking proteins,
CC such as MAPRE1, to regulate microtubule growth along actin stress
CC fibers (By similarity). Enhances ADORA2-mediated adenylyl cyclase
CC activation by acting as a scaffold to recruit trimeric G-protein
CC complexes to ADORA2A (By similarity). {ECO:0000250|UniProtKB:Q5SSG4,
CC ECO:0000250|UniProtKB:Q8NHY3}.
CC -!- SUBUNIT: Interacts with ADORA2A (via its cytoplasmic C-terminal domain)
CC (PubMed:23994616). Interacts with GNAS, GNAL, GNAQ, and GNA13 (By
CC similarity). Interacts with MAPRE1 (By similarity).
CC {ECO:0000250|UniProtKB:Q5SSG4, ECO:0000250|UniProtKB:Q8NHY3,
CC ECO:0000269|PubMed:23994616}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:23994616}. Cell membrane
CC {ECO:0000269|PubMed:23994616}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q8NHY3}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q8NHY3}. Note=Colocalizes with ADORA2A at
CC neuronal processes (PubMed:23994616). Colocalizes with and tracks the
CC tips of microtubule plus ends (By similarity).
CC {ECO:0000250|UniProtKB:Q8NHY3, ECO:0000269|PubMed:23994616}.
CC -!- TISSUE SPECIFICITY: Expressed in the cortical tissue (at protein
CC level). {ECO:0000269|PubMed:23994616}.
CC -!- SIMILARITY: Belongs to the GAS2 family. {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; AC119615; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001099293.2; NM_001105823.2.
DR RefSeq; XP_008772026.1; XM_008773804.2.
DR AlphaFoldDB; D3ZUE1; -.
DR STRING; 10116.ENSRNOP00000067565; -.
DR jPOST; D3ZUE1; -.
DR PaxDb; D3ZUE1; -.
DR Ensembl; ENSRNOT00000071218; ENSRNOP00000067565; ENSRNOG00000047546.
DR GeneID; 287570; -.
DR KEGG; rno:287570; -.
DR CTD; 246176; -.
DR RGD; 1307868; Gas2l2.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000162866; -.
DR HOGENOM; CLU_015447_1_0_1; -.
DR InParanoid; D3ZUE1; -.
DR OMA; QPCHFRN; -.
DR OrthoDB; 1343422at2759; -.
DR PhylomeDB; D3ZUE1; -.
DR TreeFam; TF323754; -.
DR PRO; PR:D3ZUE1; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000047546; Expressed in lung and 4 other tissues.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0035371; C:microtubule plus-end; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; ISS:UniProtKB.
DR GO; GO:0008093; F:cytoskeletal anchor activity; ISS:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:0045745; P:positive regulation of G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:1904825; P:protein localization to microtubule plus-end; ISO:RGD.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; ISO:RGD.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:RGD.
DR CDD; cd00014; CH; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 3.30.920.20; -; 1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR003108; GAR_dom.
DR InterPro; IPR036534; GAR_dom_sf.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF02187; GAS2; 1.
DR SMART; SM00033; CH; 1.
DR SMART; SM00243; GAS2; 1.
DR SUPFAM; SSF143575; SSF143575; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51460; GAR; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Membrane;
KW Reference proteome.
FT CHAIN 1..857
FT /note="GAS2-like protein 2"
FT /id="PRO_0000448438"
FT DOMAIN 32..159
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 201..273
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..857
FT /note="Interaction with ADORA2A"
FT /evidence="ECO:0000250|UniProtKB:Q5SSG4"
FT REGION 670..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 759..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 857 AA; 94280 MW; D9066B87C67DFCAA CRC64;
MSQHVGHGRK PRTPGPPVRS IRPFKSSEQY LEVMKEDLAE WLRDLYGLDI DAANFLRVLE
TGLVLCRHAN TVTEAALAFL AEAPERVQKI PMPQVGVFCN GAAQPGTFQA RDNISNFIQW
CRKEMGIQEV LMFETEDLVL RKNVKSVVLC LLELGRRAWR FGVAAPSLVY LEEEIEEELR
RDLDLPSPDP PPPVPPARRP CHFHNLDQMV QSLVSHCTCP VQFSMVKISD GKYRVGDSNT
LIFIRILRSH VMVRVGGGWD TLGHYLDKHD PCRCTSLSHK PGSFLKPPGP PVQHEVKVQD
GPSQPQPLMT ISRSQSPLPP VDWKTYTSSS RKLRPPTPSS SGPRSEFPAR ARTPREMAPF
LRSQEKPTLS QRMSSPGPQL SSPCRGPDLQ STLSERRVNR SPGELPRGRT PTSWVPKEAD
SQGAHTKAPI PQRLQIPETT SKKTPARGPS PPPRSSSLAS PHTIWLPDQG ASPEISEPMS
AQSSSPGKGL TKIPIRLSPA RPPTPGRGSL GTEGGGSMQR GSLSSRALAG NLDRSTHGHH
SVDVSKDHQK VIQISSGTED PRSLGTQERK ERYTSLPLGR TREPALYDNL KEELVANMKL
LEVGAACTQG TRSQAIPRSG VYVPSLGGMW PEPRGPYDKV IQELVQGPPR LLKVDLKAWK
VGSECLPRPI VNPGSPKEEQ VSRERGTRRK ARPSAQGTTV KTTSPARGQD CSTLPVSANL
KAPTHSCSDP SSDKAKVCLG KGKRTLRKPQ KVPSIYKLKL RPRIRPRRDH RPEKRPSRIP
KPLVYPFLGP ARTAPGSRLL KATLGGTGGD VNGVGKKEEE KKKETSISLE SSIQPSESRE
PMQLDGTPLP PEEESWV
