GA2L1_MOUSE
ID GA2L1_MOUSE Reviewed; 678 AA.
AC Q8JZP9; Q5SVG0; Q8K573;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=GAS2-like protein 1;
DE AltName: Full=Growth arrest-specific protein 2-like 1;
GN Name=Gas2l1;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=12584248; DOI=10.1242/jcs.00272;
RA Goriounov D., Leung C.L., Liem R.K.;
RT "Protein products of human Gas2-related genes on chromosomes 17 and 22
RT (hGAR17 and hGAR22) associate with both microfilaments and microtubules.";
RL J. Cell Sci. 116:1045-1058(2003).
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Liver;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-352; SER-355;
RP SER-493 AND SER-654, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP INTERACTION WITH MAPRE1.
RX PubMed=24706950; DOI=10.1242/jcs.140558;
RA Stroud M.J., Nazgiewicz A., McKenzie E.A., Wang Y., Kammerer R.A.,
RA Ballestrem C.;
RT "GAS2-like proteins mediate communication between microtubules and actin
RT through interactions with end-binding proteins.";
RL J. Cell Sci. 127:2672-2682(2014).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-490; ARG-507 AND ARG-630, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Seems to be 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). {ECO:0000250|UniProtKB:Q99501}.
CC -!- SUBUNIT: Interacts with MAPRE1. {ECO:0000269|PubMed:24706950}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q99501}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:Q99501}. Note=Colocalizes with the tips of
CC microtubule plus ends. {ECO:0000250|UniProtKB:Q99501}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Beta;
CC IsoId=Q8JZP9-1; Sequence=Displayed;
CC Name=2; Synonyms=Alpha;
CC IsoId=Q8JZP9-2; Sequence=VSP_015496;
CC -!- SIMILARITY: Belongs to the GAS2 family. {ECO:0000305}.
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DR EMBL; AF508323; AAM34262.1; -; mRNA.
DR EMBL; AF508324; AAM34263.1; -; mRNA.
DR EMBL; AL645522; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031785; AAH31785.1; -; mRNA.
DR CCDS; CCDS36101.1; -. [Q8JZP9-1]
DR RefSeq; NP_001177337.1; NM_001190408.1. [Q8JZP9-1]
DR RefSeq; NP_653146.1; NM_144560.3. [Q8JZP9-1]
DR AlphaFoldDB; Q8JZP9; -.
DR SMR; Q8JZP9; -.
DR STRING; 10090.ENSMUSP00000050275; -.
DR iPTMnet; Q8JZP9; -.
DR PhosphoSitePlus; Q8JZP9; -.
DR jPOST; Q8JZP9; -.
DR MaxQB; Q8JZP9; -.
DR PaxDb; Q8JZP9; -.
DR PeptideAtlas; Q8JZP9; -.
DR PRIDE; Q8JZP9; -.
DR ProteomicsDB; 271630; -. [Q8JZP9-1]
DR ProteomicsDB; 271631; -. [Q8JZP9-2]
DR Antibodypedia; 10326; 209 antibodies from 24 providers.
DR Ensembl; ENSMUST00000056649; ENSMUSP00000050275; ENSMUSG00000034201. [Q8JZP9-1]
DR Ensembl; ENSMUST00000109895; ENSMUSP00000105521; ENSMUSG00000034201. [Q8JZP9-1]
DR GeneID; 78926; -.
DR KEGG; mmu:78926; -.
DR UCSC; uc007hvr.2; mouse. [Q8JZP9-2]
DR UCSC; uc007hvu.2; mouse. [Q8JZP9-1]
DR CTD; 10634; -.
DR MGI; MGI:1926176; Gas2l1.
DR VEuPathDB; HostDB:ENSMUSG00000034201; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000154849; -.
DR HOGENOM; CLU_015447_0_0_1; -.
DR InParanoid; Q8JZP9; -.
DR OMA; ACKPASV; -.
DR OrthoDB; 1343422at2759; -.
DR PhylomeDB; Q8JZP9; -.
DR TreeFam; TF323754; -.
DR BioGRID-ORCS; 78926; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Gas2l1; mouse.
DR PRO; PR:Q8JZP9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8JZP9; protein.
DR Bgee; ENSMUSG00000034201; Expressed in ear vesicle and 223 other tissues.
DR ExpressionAtlas; Q8JZP9; baseline and differential.
DR Genevisible; Q8JZP9; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0035371; C:microtubule plus-end; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008093; F:cytoskeletal anchor activity; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0046966; F:nuclear thyroid hormone receptor binding; ISS:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
DR GO; GO:0097067; P:cellular response to thyroid hormone stimulus; ISS:UniProtKB.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
DR GO; GO:1904825; P:protein localization to microtubule plus-end; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; ISO:MGI.
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 InterPro; IPR029931; GAS2L1.
DR PANTHER; PTHR46756:SF16; PTHR46756:SF16; 1.
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 Acetylation; Alternative splicing; Cytoplasm; Cytoskeleton; Methylation;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q99501"
FT CHAIN 2..678
FT /note="GAS2-like protein 1"
FT /id="PRO_0000190443"
FT DOMAIN 27..148
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 203..275
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 276..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..371
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..495
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q99501"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99501"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99501"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 355
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99501"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99501"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99501"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99501"
FT MOD_RES 489
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99501"
FT MOD_RES 490
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 501
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q99501"
FT MOD_RES 507
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 630
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 654
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 338..678
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12584248"
FT /id="VSP_015496"
SQ SEQUENCE 678 AA; 72411 MW; 067DCB47F5F1A3A7 CRC64;
MANPVAGIAG SAAKSVRPFR SSEAYVEAMK EDLADWLNAL YSLGLPGSGD GFLTGLATGT
TLCQHANAVT EAARALAAAR PTRGVAFQAH SVAPGSFMAR DNVASFIGWC RAELGVPEVL
MFETEDLVLR KNEKSVVLCL LEVARRGARL GLLAPRLVQF EQEIERELRA TPQVSSVPAA
EEDVTEIATV PGVPTRTPRM TPNDLRNLDE LVREILGRCT CPDQFPMIKV SEGKYRVGDS
SLLIFVRVLR SHVMVRVGGG WDTLEHYLDK HDPCRCSSST HRLPQQRTGT FSPQRGSPTP
SPRPGSPVPG SERRSSRPEV TPISLRGTKE GPETPLRPRD QLPPLPRSRR YSGDSDSSAS
SAQSGPMGAR SDDSATGSRR ERPSHRPTSC LPASPRRPTA PRSQSRDRLD RGRPRVAPGG
RGAQLSTSSP ARRTRSQSRE EQAVLMVRRD RDGQHSWVAR GRGGGGSGGS GRSTPQTPRA
LSPAAPRPSR GPSPGPELAA TPASIFRTPL QLDPQQEQQL FRRLEEEFLA NARALEAAAS
HTPMGSAPDP PAPDSAYCSS SSSSSSLSVL GGKCGQPGES GRTANGLPGP RSQALSSSSD
EGSPYLAVGG ALDATRSSLA GPEPSLTWAR GRMDTQPDRK PSRIPTPRGP RRPSGPIELG
AWHAQHSVTP RTEPDSSM
