CARL1_MOUSE
ID CARL1_MOUSE Reviewed; 1374 AA.
AC Q6EDY6; Q5NCM0; Q8BQ45; Q8BRS5; Q91YZ6;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=F-actin-uncapping protein LRRC16A {ECO:0000250|UniProtKB:Q5VZK9};
DE AltName: Full=CARMIL homolog {ECO:0000250|UniProtKB:Q95VZ3};
DE AltName: Full=Capping protein regulator and myosin 1 linker protein 1 {ECO:0000250|UniProtKB:Q5VZK9};
DE AltName: Full=Capping protein, Arp2/3 and myosin-I linker homolog 1 {ECO:0000250|UniProtKB:Q95VZ3};
DE AltName: Full=Capping protein, Arp2/3 and myosin-I linker protein 1 {ECO:0000303|PubMed:16054028};
DE Short=CARML1 {ECO:0000303|PubMed:16054028};
DE AltName: Full=Leucine-rich repeat-containing protein 16A {ECO:0000312|MGI:MGI:1915982};
GN Name=Carmil1 {ECO:0000250|UniProtKB:Q5VZK9};
GN Synonyms=Carmil {ECO:0000250|UniProtKB:Q95VZ3}, Lrrc16,
GN Lrrc16a {ECO:0000312|MGI:MGI:1915982};
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INTERACTION WITH F-ACTIN-CAPPING PROTEIN, AND MUTAGENESIS OF LYS-991 AND
RP ARG-993.
RC STRAIN=C57BL/6J;
RX PubMed=16054028; DOI=10.1016/j.devcel.2005.06.008;
RA Yang C., Pring M., Wear M.A., Huang M., Cooper J.A., Svitkina T.M.,
RA Zigmond S.H.;
RT "Mammalian CARMIL inhibits actin filament capping by capping protein.";
RL Dev. Cell 9:209-221(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 410-1374 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, 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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 595-1374 (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-920; SER-972; SER-1291;
RP SER-1295; SER-1335 AND SER-1363, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, 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).
CC -!- FUNCTION: Cell membrane-cytoskeleton-associated protein that plays a
CC role in the regulation of actin polymerization at the barbed end of
CC actin filaments. Prevents F-actin heterodimeric capping protein (CP)
CC activity at the leading edges of migrating cells, and hence generates
CC uncapped barbed ends and enhances actin polymerization, however, seems
CC unable to nucleate filaments (PubMed:16054028). Plays a role in
CC lamellipodial protrusion formations and cell migration
CC (PubMed:16054028). {ECO:0000269|PubMed:16054028}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts (via C-terminus) with
CC heterodimeric capping protein (CP); this interaction uncaps barbed ends
CC capped by CP, enhances barbed-end actin polymerization and promotes
CC lamellipodial formation and cell migration (PubMed:16054028). Interacts
CC with MYO1E (By similarity). Interacts with TRIO (By similarity).
CC {ECO:0000250|UniProtKB:Q5VZK9, ECO:0000269|PubMed:16054028}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16054028}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16054028}. Cell membrane
CC {ECO:0000250|UniProtKB:Q5VZK9}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:16054028}. Note=Found on macropinosomes (By
CC similarity). Colocalized with heterodimeric capping protein (CP) and F-
CC actin in lamellipodia but not with F-actin in stress fibers
CC (PubMed:16054028). {ECO:0000250|UniProtKB:Q5VZK9,
CC ECO:0000269|PubMed:16054028}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6EDY6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6EDY6-2; Sequence=VSP_032421, VSP_032422;
CC Name=3;
CC IsoId=Q6EDY6-3; Sequence=VSP_032423, VSP_032424;
CC -!- DOMAIN: The C-terminus is necessary for localization to the cell
CC membrane. {ECO:0000250|UniProtKB:Q5VZK9}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CARMIL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH12229.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC31591.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY437876; AAR96060.1; -; mRNA.
DR EMBL; AK051570; BAC34678.1; -; mRNA.
DR EMBL; AK043591; BAC31591.1; ALT_INIT; mRNA.
DR EMBL; AL590864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL606464; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL683873; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012229; AAH12229.1; ALT_INIT; mRNA.
DR CCDS; CCDS36621.1; -. [Q6EDY6-1]
DR RefSeq; NP_081101.3; NM_026825.3. [Q6EDY6-1]
DR RefSeq; XP_011242640.1; XM_011244338.2. [Q6EDY6-3]
DR PDB; 2KZ7; NMR; -; C=965-1039.
DR PDB; 3AA0; X-ray; 1.70 A; C=985-1005.
DR PDB; 3AAE; X-ray; 3.30 A; V/W/X/Y/Z=971-1002.
DR PDB; 4K17; X-ray; 2.90 A; A/B/C/D=1-668.
DR PDBsum; 2KZ7; -.
DR PDBsum; 3AA0; -.
DR PDBsum; 3AAE; -.
DR PDBsum; 4K17; -.
DR AlphaFoldDB; Q6EDY6; -.
DR BMRB; Q6EDY6; -.
DR SMR; Q6EDY6; -.
DR BioGRID; 213021; 2.
DR DIP; DIP-58942N; -.
DR IntAct; Q6EDY6; 1.
DR STRING; 10090.ENSMUSP00000072662; -.
DR iPTMnet; Q6EDY6; -.
DR PhosphoSitePlus; Q6EDY6; -.
DR SwissPalm; Q6EDY6; -.
DR jPOST; Q6EDY6; -.
DR MaxQB; Q6EDY6; -.
DR PaxDb; Q6EDY6; -.
DR PeptideAtlas; Q6EDY6; -.
DR PRIDE; Q6EDY6; -.
DR ProteomicsDB; 265543; -. [Q6EDY6-1]
DR ProteomicsDB; 265544; -. [Q6EDY6-2]
DR ProteomicsDB; 265545; -. [Q6EDY6-3]
DR Antibodypedia; 25380; 88 antibodies from 17 providers.
DR DNASU; 68732; -.
DR Ensembl; ENSMUST00000072889; ENSMUSP00000072662; ENSMUSG00000021338. [Q6EDY6-1]
DR GeneID; 68732; -.
DR KEGG; mmu:68732; -.
DR UCSC; uc007pvn.1; mouse. [Q6EDY6-1]
DR UCSC; uc007pvp.1; mouse. [Q6EDY6-2]
DR CTD; 55604; -.
DR MGI; MGI:1915982; Carmil1.
DR VEuPathDB; HostDB:ENSMUSG00000021338; -.
DR eggNOG; KOG4242; Eukaryota.
DR GeneTree; ENSGT00940000155112; -.
DR InParanoid; Q6EDY6; -.
DR OMA; DKQENRV; -.
DR OrthoDB; 208951at2759; -.
DR PhylomeDB; Q6EDY6; -.
DR TreeFam; TF316381; -.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 68732; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Lrrc16a; mouse.
DR EvolutionaryTrace; Q6EDY6; -.
DR PRO; PR:Q6EDY6; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q6EDY6; protein.
DR Bgee; ENSMUSG00000021338; Expressed in animal zygote and 240 other tissues.
DR ExpressionAtlas; Q6EDY6; baseline and differential.
DR Genevisible; Q6EDY6; MM.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0044354; C:macropinosome; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IMP:UniProtKB.
DR GO; GO:0051639; P:actin filament network formation; ISS:UniProtKB.
DR GO; GO:0051638; P:barbed-end actin filament uncapping; IMP:UniProtKB.
DR GO; GO:0016477; P:cell migration; ISS:BHF-UCL.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; ISS:UniProtKB.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:BHF-UCL.
DR GO; GO:0044351; P:macropinocytosis; ISS:UniProtKB.
DR GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; IMP:UniProtKB.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB.
DR GO; GO:1902745; P:positive regulation of lamellipodium organization; IMP:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0034315; P:regulation of Arp2/3 complex-mediated actin nucleation; IBA:GO_Central.
DR GO; GO:0031529; P:ruffle organization; ISS:BHF-UCL.
DR GO; GO:0046415; P:urate metabolic process; ISS:BHF-UCL.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR029764; CARMIL1.
DR InterPro; IPR031943; CARMIL_C.
DR InterPro; IPR041245; CARMIL_PH.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR PANTHER; PTHR24112:SF39; PTHR24112:SF39; 1.
DR Pfam; PF17888; Carm_PH; 1.
DR Pfam; PF16000; CARMIL_C; 1.
DR Pfam; PF13516; LRR_6; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton; Leucine-rich repeat;
KW Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1374
FT /note="F-actin-uncapping protein LRRC16A"
FT /id="PRO_0000325816"
FT REPEAT 245..269
FT /note="LRR 1"
FT REPEAT 275..298
FT /note="LRR 2"
FT REPEAT 304..327
FT /note="LRR 3"
FT REPEAT 336..363
FT /note="LRR 4"
FT REPEAT 391..418
FT /note="LRR 5"
FT REPEAT 423..447
FT /note="LRR 6"
FT REPEAT 485..510
FT /note="LRR 7"
FT REPEAT 547..570
FT /note="LRR 8"
FT REPEAT 574..597
FT /note="LRR 9"
FT REPEAT 658..682
FT /note="LRR 10"
FT REPEAT 962..985
FT /note="LRR 11"
FT REGION 961..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..1084
FT /note="Inhibits capping activity of CP"
FT /evidence="ECO:0000269|PubMed:16054028"
FT REGION 1040..1374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1058..1092
FT /note="Necessary for localization at the cell membrane"
FT /evidence="ECO:0000250|UniProtKB:Q5VZK9"
FT COILED 714..738
FT /evidence="ECO:0000255"
FT COMPBIAS 1040..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1190..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1258..1272
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1346..1374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZK9"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZK9"
FT MOD_RES 920
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 972
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1096
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZK9"
FT MOD_RES 1229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZK9"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZK9"
FT MOD_RES 1289
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZK9"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZK9"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5VZK9"
FT MOD_RES 1335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 260
FT /note="I -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032421"
FT VAR_SEQ 261..1374
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032422"
FT VAR_SEQ 918
FT /note="M -> MTLCCTS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032423"
FT VAR_SEQ 1332..1374
FT /note="SRRSWGPAQEYQEQKQRSSGKDGHQGSKCSDSGEEAEKEFIFV -> CPTNF
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032424"
FT MUTAGEN 991
FT /note="K->A: Decreased ability to bind heterodimeric
FT capping protein (CP) and to inhibit the actin-capping
FT activity of CP."
FT /evidence="ECO:0000269|PubMed:16054028"
FT MUTAGEN 993
FT /note="R->A: Loss of ability to bind heterodimeric capping
FT protein (CP) and to inhibit the actin-capping activity of
FT CP."
FT /evidence="ECO:0000269|PubMed:16054028"
FT MUTAGEN 993
FT /note="R->E: Loss of ability to bind heterodimeric capping
FT protein (CP) and to inhibit the actin-capping activity of
FT CP."
FT /evidence="ECO:0000269|PubMed:16054028"
FT CONFLICT 8
FT /note="V -> A (in Ref. 1; AAR96060)"
FT /evidence="ECO:0000305"
FT CONFLICT 782
FT /note="L -> W (in Ref. 1; AAR96060 and 4; AAH12229)"
FT /evidence="ECO:0000305"
FT CONFLICT 796
FT /note="N -> S (in Ref. 4; AAH12229)"
FT /evidence="ECO:0000305"
FT CONFLICT 1309
FT /note="S -> P (in Ref. 1; AAR96060 and 4; AAH12229)"
FT /evidence="ECO:0000305"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:4K17"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 50..61
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:4K17"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 73..77
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 83..90
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 100..116
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 135..147
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 196..199
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:4K17"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 232..244
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 260..272
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 291..301
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 319..331
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 355..362
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 379..389
FT /evidence="ECO:0007829|PDB:4K17"
FT TURN 391..393
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 414..422
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 438..449
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 466..472
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 486..492
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 502..510
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 529..544
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 561..564
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 588..601
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 606..609
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 617..628
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 640..649
FT /evidence="ECO:0007829|PDB:4K17"
FT HELIX 651..667
FT /evidence="ECO:0007829|PDB:4K17"
FT STRAND 968..971
FT /evidence="ECO:0007829|PDB:2KZ7"
FT HELIX 989..992
FT /evidence="ECO:0007829|PDB:3AA0"
FT STRAND 1031..1034
FT /evidence="ECO:0007829|PDB:2KZ7"
SQ SEQUENCE 1374 AA; 151860 MW; A7BE0350B3770101 CRC64;
MTDESSDVPR ELMESIKDVI GRKIKISVKK KVKLEVKGDR VENKVLVLTS CRAFLLSARI
PSKLELTFSY LEIHGVICHK PAQMVVETEK CNMSMKMVSP EDVSEVLAHI GTCLRRIFPG
LSPLRIMKKV SMEPSERLAS LQALWDSQTL AEPGPCGGFS QMYACVCDWL GFSYKEEVQW
DVDTIYLTQD TRELNLQDFS HLEHRDLIPI IAALEYNQWF TKLSSKDLKL STDVCEQILR
VVSRSNRLEE LVLENAGLRI DFAQKLAGAL AHNPNSGLHT INLAGNSLED RGVSSLSIQF
AKLPKGLKHL NLSKTSLSPK GVNSLCQSLS ANPLTASTLT HLDLSGNALR GDDLSHMYNF
LAQPNTIVHL DLSNTECSLE MVCSALLRGC LQCLAVLNLS RSVFSHRKGK EVPPSFKQFF
SSSLALIQIN LSGTKLSPEP LKALLLGLAC NHSLKGVSLD LSNCELGHCL RSGGAQVLEG
CIAEIHNITS LDISDNGLES DLSTLIVWLS KNRSIQHLAL GKNFNNMKSK NLTPVLDNLV
QMIQDEDSPL QSLSLADSKL KAEVTIIINA LGSNTSLTKV DISGNGMGDM GAKMLAKALQ
INTKLRTVIW DKNNITAQGF QDIAVAMEKN YTLRFMPIPM YDAAQALKTN PEKTEEALQK
IENYLLRNHE TRKYLQEQAY RLQQGIVTST TQQMIDRICV KVQDHLNSLR ACGGDAIQED
LKAAERLMRD AKNSKTLLPN LYHVGGASWA GASGLSSSPI QETLESMAGE VTRVVDEQLK
DLLESMVDAA ETLCPNVMRK AHIRQDLIHA STEKISIPRT FVKNVLLEQS GIDILNKISE
VKLTVASFLS DRIVDEILDS LSSSHRKLAN HFSRLNKSLP QREDLEVELV EEKPVKRAIL
TVEDLTEVER LEDLDTCMMT PKSKRKSIHS RMLRPVSRAF EMEFDLDKAL EEVPIHIEDP
PFPSVRQEKR SSGLISELPS EEGRRLEHFT KLRPKRNKKQ QPTQAAVCTI SILPQDGEQN
GLMGRVDEGV DEFFTKKVTK MDCKRSSSRS SDAHELGEGD EKKKRDSRRS GFLNLIKSRS
RSERPPTVLM TEELSSPKGA MRSPPVDTTR KEIKAAEHNG APDRTEEIKT PEPLEEGPAE
EAGRAERSDS RGSPQGGRRY VQVMGSGLLA EMKAKQERRA ACAQKKLGND VISQDPSSPV
SCNTERLEGG ATVPKLQPGL PEARFGSGTP EKNAKAEPRV DGGCRSRSSS SMPTSPKPLL
QSPKPSPSAR PSIPQKPRTA SRPEDTPDSP SGPSSPKVAL LPPILKKVSS DKERDGQNSS
QSSPRSFSQE ASRRSWGPAQ EYQEQKQRSS GKDGHQGSKC SDSGEEAEKE FIFV
