MRP_MOUSE
ID MRP_MOUSE Reviewed; 200 AA.
AC P28667; Q3TEZ4; Q91W07;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=MARCKS-related protein;
DE AltName: Full=Brain protein F52;
DE AltName: Full=MARCKS-like protein 1;
DE AltName: Full=Macrophage myristoylated alanine-rich C kinase substrate;
DE Short=Mac-MARCKS;
DE Short=MacMARCKS;
GN Name=Marcksl1; Synonyms=Mlp, Mrp;
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], AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=1864362; DOI=10.1016/0014-5793(91)80961-2;
RA Umekage T., Kato K.;
RT "A mouse brain cDNA encodes a novel protein with the protein kinase C
RT phosphorylation site domain common to MARCKS.";
RL FEBS Lett. 286:147-151(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=1516135; DOI=10.1016/0092-8674(92)90312-z;
RA Li J., Aderem A.;
RT "MacMARCKS, a novel member of the MARCKS family of protein kinase C
RT substrates.";
RL Cell 70:791-801(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RX PubMed=8406449; DOI=10.1006/geno.1993.1301;
RA Lobach D.F., Rochelle J.M., Watson M.L., Seldin M.F., Blackshear P.J.;
RT "Nucleotide sequence, expression, and chromosomal mapping of Mrp and
RT mapping of five related sequences.";
RL Genomics 17:194-204(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Cerebellum, Kidney, and Spinal ganglion;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary gland;
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 [6]
RP FUNCTION, INTERACTION WITH CALMODULIN, SUBCELLULAR LOCATION,
RP PHOSPHORYLATION, AND MYRISTOYLATION AT GLY-2.
RX PubMed=1618855; DOI=10.1016/s0021-9258(18)42245-4;
RA Blackshear P.J., Verghese G.M., Johnson J.D., Haupt D.M., Stumpo D.J.;
RT "Characteristics of the F52 protein, a MARCKS homologue.";
RL J. Biol. Chem. 267:13540-13546(1992).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=9819217; DOI=10.1021/bi981765a;
RA Bahr G., Diederich A., Vergeres G., Winterhalter M.;
RT "Interaction of the effector domain of MARCKS and MARCKS-related protein
RT with lipid membranes revealed by electric potential measurements.";
RL Biochemistry 37:16252-16261(1998).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9598313; DOI=10.1006/geno.1998.5247;
RA Stumpo D.J., Eddy R.L. Jr., Haley L.L., Sait S., Shows T.B., Lai W.S.,
RA Young W.S. III, Speer M.C., Dehejia A., Polymeropoulos M., Blackshear P.J.;
RT "Promoter sequence, expression, and fine chromosomal mapping of the human
RT gene (MLP) encoding the MARCKS-like protein: identification of neighboring
RT and linked polymorphic loci for MLP and MACS and use in the evaluation of
RT human neural tube defects.";
RL Genomics 49:253-264(1998).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; SER-48; SER-71; SER-135;
RP THR-148; SER-162; SER-165; THR-170 AND THR-192, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22; THR-85 AND THR-148, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-22; THR-85; SER-119;
RP SER-120; SER-132; SER-135; THR-148; THR-170 AND THR-183, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, 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 [12]
RP FUNCTION, INTERACTION WITH F-ACTIN, SUBCELLULAR LOCATION, PHOSPHORYLATION
RP AT SER-120; THR-148 AND THR-183, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP SER-120; THR-148 AND THR-183.
RX PubMed=22751924; DOI=10.1128/mcb.00713-12;
RA Bjorkblom B., Padzik A., Mohammad H., Westerlund N., Komulainen E.,
RA Hollos P., Parviainen L., Papageorgiou A.C., Iljin K., Kallioniemi O.,
RA Kallajoki M., Courtney M.J., Magard M., James P., Coffey E.T.;
RT "c-Jun N-terminal kinase phosphorylation of MARCKSL1 determines actin
RT stability and migration in neurons and in cancer cells.";
RL Mol. Cell. Biol. 32:3513-3526(2012).
CC -!- FUNCTION: Involved in the control of cell movement by regulating actin
CC cytoskeleton homeostasis and filopodium and lamellipodium formation
CC (PubMed:22751924). When unphosphorylated, induces cell migration
CC (PubMed:22751924). When phosphorylated by MAPK8, induces actin bundles
CC formation and stabilization, thereby reducing actin plasticity, hence
CC restricting cell movement, including neuronal migration
CC (PubMed:22751924). May be involved in coupling the protein kinase C and
CC calmodulin signal transduction systems (Probable).
CC {ECO:0000269|PubMed:22751924, ECO:0000305|PubMed:1618855}.
CC -!- SUBUNIT: Binds to filamentous actin (F-actin), but not to monomeric G-
CC actin, independently of its phosphorylation status (PubMed:22751924).
CC Interacts with calmodulin (PubMed:1618855).
CC {ECO:0000269|PubMed:1618855, ECO:0000269|PubMed:22751924}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:22751924}. Cell membrane
CC {ECO:0000305|PubMed:1618855, ECO:0000305|PubMed:9819217}; Lipid-anchor
CC {ECO:0000305|PubMed:1618855}. Note=Associates with the membrane via the
CC insertion of the N-terminal N-myristoyl chain and the partial insertion
CC of the effector domain (Probable). Association of the effector domain
CC with membranes may be regulated by Ca(2+)/calmodulin (By similarity).
CC Colocalizes with F-actin at the leading edge of migrating cells
CC (PubMed:22751924). {ECO:0000250|UniProtKB:P49006,
CC ECO:0000269|PubMed:22751924, ECO:0000305|PubMed:1618855,
CC ECO:0000305|PubMed:9819217}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in brain cortex and
CC hippocampus, including dentate gyrus, anterior olfactory nucleus,
CC primary olfactory cortex, entorhinal cortex, medial preoptic area and
CC dorsomedial hypothalamic nucleus (at protein level) (PubMed:1864362,
CC PubMed:8406449, PubMed:9598313, PubMed:22751924). Expressed in neuronal
CC cells (at protein level) (PubMed:22751924). Detected in the retina
CC (PubMed:9598313). Strongly expressed in testis and uterus; expressed at
CC lower levels in cerebellum, cerebrum, adipose tissue, spleen, kidney,
CC thyroid, liver, lung, skeletal muscle and heart (PubMed:8406449).
CC Detected in T-cells and B-cells (PubMed:8406449).
CC {ECO:0000269|PubMed:1864362, ECO:0000269|PubMed:22751924,
CC ECO:0000269|PubMed:8406449, ECO:0000269|PubMed:9598313}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the developing neural tube as early
CC as 8.5 dpc. Remains most highly expressed in the developing brain and
CC spinal cord during later development at least until 14.5 dpc. Also
CC detected in the lung, adrenal gland, gut and kidney, particularly the
CC kidney cortex. Undetectable in the liver. {ECO:0000269|PubMed:9598313}.
CC -!- INDUCTION: Up-regulated in peritoneal macrophages in response to
CC bacterial lipopolysaccharide (LPS). {ECO:0000269|PubMed:1516135}.
CC -!- PTM: Phosphorylated (PubMed:1618855, PubMed:22751924). Phosphorylation
CC at Ser-120 and Thr-183 is non-redundantly catalyzed by MAPK8 in vivo
CC (PubMed:22751924). Phosphorylation at Thr-148 is preferentially
CC catalyzed by MAPK8 in vivo, but this modification can also be catalyzed
CC by other kinases in the absence of MAPK8 (PubMed:22751924). May be
CC phosphorylated by protein kinase C, which disrupts the interaction with
CC calmodulin (PubMed:1618855). {ECO:0000269|PubMed:1618855,
CC ECO:0000269|PubMed:22751924}.
CC -!- SIMILARITY: Belongs to the MARCKS family. {ECO:0000305}.
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DR EMBL; X61399; CAA43671.1; -; mRNA.
DR EMBL; S65597; AAP13962.1; -; Genomic_DNA.
DR EMBL; AK079390; BAC37630.1; -; mRNA.
DR EMBL; AK083913; BAC39058.1; -; mRNA.
DR EMBL; AK152990; BAE31636.1; -; mRNA.
DR EMBL; AK169355; BAE41104.1; -; mRNA.
DR EMBL; BC006757; AAH06757.1; -; mRNA.
DR CCDS; CCDS18695.1; -.
DR PIR; S17185; S17185.
DR RefSeq; NP_034937.1; NM_010807.4.
DR AlphaFoldDB; P28667; -.
DR BioGRID; 201439; 5.
DR STRING; 10090.ENSMUSP00000055637; -.
DR iPTMnet; P28667; -.
DR PhosphoSitePlus; P28667; -.
DR SwissPalm; P28667; -.
DR EPD; P28667; -.
DR jPOST; P28667; -.
DR MaxQB; P28667; -.
DR PaxDb; P28667; -.
DR PeptideAtlas; P28667; -.
DR PRIDE; P28667; -.
DR ProteomicsDB; 291416; -.
DR Antibodypedia; 31303; 242 antibodies from 34 providers.
DR DNASU; 17357; -.
DR Ensembl; ENSMUST00000062356; ENSMUSP00000055637; ENSMUSG00000047945.
DR GeneID; 17357; -.
DR KEGG; mmu:17357; -.
DR UCSC; uc008uxf.2; mouse.
DR CTD; 65108; -.
DR MGI; MGI:97143; Marcksl1.
DR VEuPathDB; HostDB:ENSMUSG00000047945; -.
DR eggNOG; ENOG502RYXK; Eukaryota.
DR GeneTree; ENSGT00730000111349; -.
DR HOGENOM; CLU_073091_1_0_1; -.
DR InParanoid; P28667; -.
DR OMA; ANCQENG; -.
DR OrthoDB; 1511774at2759; -.
DR PhylomeDB; P28667; -.
DR TreeFam; TF332815; -.
DR BioGRID-ORCS; 17357; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Marcksl1; mouse.
DR PRO; PR:P28667; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P28667; protein.
DR Bgee; ENSMUSG00000047945; Expressed in neural tube and 270 other tissues.
DR Genevisible; P28667; MM.
DR GO; GO:0099026; C:anchored component of presynaptic membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0099523; C:presynaptic cytosol; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0099626; F:voltage-gated calcium channel activity involved in regulation of presynaptic cytosolic calcium levels; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IDA:MGI.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR InterPro; IPR002101; MARCKS.
DR PANTHER; PTHR14353; PTHR14353; 1.
DR Pfam; PF02063; MARCKS; 2.
DR PRINTS; PR00963; MARCKS.
DR PROSITE; PS00826; MARCKS_1; 1.
DR PROSITE; PS00827; MARCKS_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Calmodulin-binding; Cell membrane; Cytoplasm; Cytoskeleton;
KW Lipoprotein; Membrane; Myristate; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1618855"
FT CHAIN 2..200
FT /note="MARCKS-related protein"
FT /id="PRO_0000157153"
FT REGION 1..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..110
FT /note="Effector domain involved in lipid-binding and
FT calmodulin-binding"
FT /evidence="ECO:0000269|PubMed:1618855,
FT ECO:0000269|PubMed:9819217"
FT COMPBIAS 114..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49006"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 85
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 93
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P49006"
FT MOD_RES 101
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P49006"
FT MOD_RES 104
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250|UniProtKB:P49006"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 120
FT /note="Phosphoserine; by MAPK8"
FT /evidence="ECO:0000269|PubMed:22751924,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 148
FT /note="Phosphothreonine; by MAPK8"
FT /evidence="ECO:0000269|PubMed:22751924,
FT ECO:0007744|PubMed:15345747, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P49006"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 183
FT /note="Phosphothreonine; by MAPK8"
FT /evidence="ECO:0000269|PubMed:22751924,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 192
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:1618855"
FT MUTAGEN 120
FT /note="S->A: Complete loss of MAPK-mediated
FT phosphorylation; when associated with A-148 and A-183. In
FT neurons, induces the generation of large, flat
FT lamellipodial protrusions; when associated with A-148 and
FT A-183."
FT /evidence="ECO:0000269|PubMed:22751924"
FT MUTAGEN 120
FT /note="S->D: Induction of F-actin-bundling; when associated
FT with D-148 and D-183. In neurons, induces the generation of
FT long and prominent filopodia; when associated with D-148
FT and D-183."
FT /evidence="ECO:0000269|PubMed:22751924"
FT MUTAGEN 148
FT /note="T->A: Complete loss of MAPK-mediated
FT phosphorylation; when associated with A-120 and A-183. In
FT neurons, induces the generation of large, flat
FT lamellipodial protrusions; when associated with A-120 and
FT A-183."
FT /evidence="ECO:0000269|PubMed:22751924"
FT MUTAGEN 148
FT /note="T->D: Induction of F-actin-bundling; when associated
FT with D-120 and D-183. In neurons, induces the generation of
FT long and prominent filopodia; when associated with D-120
FT and D-183."
FT /evidence="ECO:0000269|PubMed:22751924"
FT MUTAGEN 183
FT /note="T->A: Complete loss of MAPK-mediated
FT phosphorylation; when associated with A-120 and A-148. In
FT neurons, induces the generation of large, flat
FT lamellipodial protrusions; when associated with A-120 and
FT A-148."
FT /evidence="ECO:0000269|PubMed:22751924"
FT MUTAGEN 183
FT /note="T->D: Induction of F-actin-bundling; when associated
FT with D-120 and D-148. In neurons, induces the generation of
FT long and prominent filopodia; when associated with D-120
FT and D-148."
FT /evidence="ECO:0000269|PubMed:22751924"
FT CONFLICT 134
FT /note="C -> S (in Ref. 5; AAH06757)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 200 AA; 20165 MW; AA50A0E2029921AF CRC64;
MGSQSSKAPR GDVTAEEAAG ASPAKANGQE NGHVRSNGDL TPKGEGESPP VNGTDEAAGA
TGDAIEPAPP SQEAEAKGEV APKETPKKKK KFSFKKPFKL SGLSFKRNRK EGGGDSSASS
PTEEEQEQGE MSACSDEGTA QEGKAAATPE SQEPQAKGAE ASAASKEGDT EEEAGPQAAE
PSTPSGPESG PTPASAEQNE
