GA2L3_MOUSE
ID GA2L3_MOUSE Reviewed; 683 AA.
AC Q3UWW6; Q3TCF5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=GAS2-like protein 3;
DE AltName: Full=Growth arrest-specific protein 2-like 3;
GN Name=Gas2l3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
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).
RN [2]
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).
CC -!- FUNCTION: Cytoskeletal linker protein. May promote and stabilize the
CC formation of the actin and microtubule network (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via CH domain) with F-actin (By similarity).
CC Interacts (via C terminus) with microtubules (By similarity). Interacts
CC with MAPRE1 (PubMed:24706950). {ECO:0000250|UniProtKB:Q86XJ1,
CC ECO:0000269|PubMed:24706950}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q86XJ1}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q86XJ1}. Note=Localizes
CC to microtubule and actin cytoskeletons. {ECO:0000250|UniProtKB:Q86XJ1}.
CC -!- DOMAIN: The GAR domain modulates the binding strength to each
CC cytoskeletal network. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GAS2 family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AK136054; BAE22798.1; -; mRNA.
DR EMBL; AK170750; BAE42001.1; -; mRNA.
DR CCDS; CCDS24115.1; -.
DR RefSeq; NP_001028503.2; NM_001033331.2.
DR RefSeq; NP_001073345.1; NM_001079876.1.
DR RefSeq; NP_001271273.1; NM_001284344.1.
DR RefSeq; XP_011241747.1; XM_011243445.1.
DR AlphaFoldDB; Q3UWW6; -.
DR SMR; Q3UWW6; -.
DR BioGRID; 231879; 2.
DR IntAct; Q3UWW6; 1.
DR STRING; 10090.ENSMUSP00000096973; -.
DR iPTMnet; Q3UWW6; -.
DR PhosphoSitePlus; Q3UWW6; -.
DR MaxQB; Q3UWW6; -.
DR PaxDb; Q3UWW6; -.
DR PeptideAtlas; Q3UWW6; -.
DR PRIDE; Q3UWW6; -.
DR ProteomicsDB; 265725; -.
DR DNASU; 237436; -.
DR GeneID; 237436; -.
DR KEGG; mmu:237436; -.
DR UCSC; uc007gsd.1; mouse.
DR CTD; 283431; -.
DR MGI; MGI:1918780; Gas2l3.
DR eggNOG; KOG0516; Eukaryota.
DR InParanoid; Q3UWW6; -.
DR OrthoDB; 1343422at2759; -.
DR PhylomeDB; Q3UWW6; -.
DR TreeFam; TF323754; -.
DR BioGRID-ORCS; 237436; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q3UWW6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q3UWW6; protein.
DR GO; GO:0015629; C:actin cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0008093; F:cytoskeletal anchor activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051764; P:actin crosslink formation; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP: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; IPR029932; GAS2L3.
DR PANTHER; PTHR46756:SF7; PTHR46756:SF7; 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 Actin-binding; Cytoplasm; Cytoskeleton; Microtubule; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..683
FT /note="GAS2-like protein 3"
FT /id="PRO_0000322985"
FT DOMAIN 50..170
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 210..283
FT /note="GAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00792"
FT REGION 301..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..483
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 435
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86XJ1"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86XJ1"
FT CONFLICT 315
FT /note="K -> Q (in Ref. 1; BAE42001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 683 AA; 74235 MW; C526B8912AA0960F CRC64;
MTMQPAIQVW FGEDLPLSPR CPLTPRHGPG LADVCQYDEW IAVRHEATLL PMQEDLSIWL
SGLLGVDIKA ERLLEELDNG VLLCQLINVL QNMVKGCHSD EPGNFPMRKV PCKKDAASGS
FFARDNTANF LHWCRHIGVD ETYLFESEGL VLHKDPRQVY LCLLEIGRIV SRYGVEPPVL
VKLEKEIELE ETLLNASGLE ESISIPKSCC QQEELHEAVK HIAEDPPCSC SHRFSIEYLS
EGRYRLGEKI LFIRMLHGKH VMVRVGGGWD TLQGFLLKYD PCRILQFATL EQKILAFQKG
VSNESVPDSP ARTPKPPEMN PLSAVNMFQK QNLRPGTPVS VPKNKEKQVR LPGARLPASS
VKGNLASPST RAKRPDSPAS FPHPKVTSLK DAAKKTTAPS NSVSQSLASP NPGSKPSTAQ
CASESSRKCV TFPKTAQTKA IPAQNSRDLS KSRLLPSKSP GKMEPKHLKH NHLSSRDESR
INLSSKSPKL PKGAMHGRPN PSPFQPPAKV TKPSSKTGAI GLGTQSQPPT RTPRSGAVSA
QRLQSTLNLN SPASVCSGSS AKATQGSKGK NTVSVAKKQP QSKGVCRNPG PGSSKSPGRT
PLSIVTVPQS ATKTETVSKS AKTAMKGQYS AKGPPKSSKP PTSFRDPPSS GKGADSGDKM
PTARKKEEDD HYFVMTGNKK LRK
