CARL1_HUMAN
ID CARL1_HUMAN Reviewed; 1371 AA.
AC Q5VZK9; B8X1J0; Q6ZUH5; Q6ZW07; Q9NXU7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=F-actin-uncapping protein LRRC16A {ECO:0000305};
DE AltName: Full=CARMIL homolog {ECO:0000250|UniProtKB:Q95VZ3};
DE AltName: Full=Capping protein regulator and myosin 1 linker protein 1 {ECO:0000312|HGNC:HGNC:21581};
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 AltName: Full=Leucine-rich repeat-containing protein 16A {ECO:0000312|HGNC:HGNC:21581};
GN Name=CARMIL1 {ECO:0000303|PubMed:16054028, ECO:0000312|HGNC:HGNC:21581};
GN Synonyms=CARMIL {ECO:0000250|UniProtKB:Q95VZ3}, LRRC16, LRRC16A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 766-1371 (ISOFORM 2).
RC TISSUE=Colon, Esophageal carcinoma, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP SUBUNIT, AND INTERACTION WITH F-ACTIN-CAPPING PROTEIN; MYO1E AND TRIO.
RX PubMed=19846667; DOI=10.1091/mbc.e08-10-1071;
RA Liang Y., Niederstrasser H., Edwards M., Jackson C.E., Cooper J.A.;
RT "Distinct roles for CARMIL isoforms in cell migration.";
RL Mol. Biol. Cell 20:5290-5305(2009).
RN [4]
RP FUNCTION, AND TISSUE SPECIFICITY.
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-916; SER-968; SER-1288;
RP SER-1291 AND SER-1331, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1067; SER-1288 AND SER-1331,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-968; SER-1288; SER-1315;
RP SER-1331 AND SER-1360, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122; SER-968; SER-1067;
RP SER-1094; THR-1228; SER-1280; SER-1288; SER-1291; SER-1324; SER-1331 AND
RP SER-1360, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-916, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=26578515; DOI=10.1074/jbc.m115.676882;
RA Lanier M.H., McConnell P., Cooper J.A.;
RT "Cell migration and invadopodia formation require a membrane-binding domain
RT of CARMIL2.";
RL J. Biol. Chem. 291:1076-1091(2016).
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:19846667). {ECO:0000269|PubMed:16054028,
CC ECO:0000269|PubMed:19846667}.
CC -!- SUBUNIT: Homodimer (PubMed:19846667). Interacts (via C-terminus) with
CC heterodimer 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 (By similarity). Interacts
CC with heterodimer capping protein (CP) (PubMed:19846667). Interacts with
CC MYO1E (PubMed:19846667). Interacts with TRIO (PubMed:19846667).
CC {ECO:0000250|UniProtKB:Q6EDY6, ECO:0000269|PubMed:19846667}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19846667}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6EDY6}. Cell membrane
CC {ECO:0000269|PubMed:26578515}. Cell projection, lamellipodium
CC {ECO:0000269|PubMed:19846667}. Note=Found on macropinosomes
CC (PubMed:19846667). Colocalized with heterodimeric capping protein (CP)
CC and F-actin in lamellipodia but not with F-actin in stress fibers
CC (PubMed:19846667). {ECO:0000269|PubMed:19846667}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=CARMIL1a {ECO:0000303|PubMed:19846667};
CC IsoId=Q5VZK9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5VZK9-2; Sequence=VSP_032420;
CC Name=3;
CC IsoId=Q5VZK9-3; Sequence=VSP_032418, VSP_032419;
CC Name=4;
CC IsoId=Q5VZK9-4; Sequence=VSP_032415, VSP_032416, VSP_032417;
CC -!- TISSUE SPECIFICITY: Expressed in lung, placenta, small intestine,
CC liver, thymus, colon, skeletal muscle, heart and brain. Higher
CC expression in kidney. {ECO:0000269|PubMed:16054028}.
CC -!- DOMAIN: The C-terminus is necessary for localization to the cell
CC membrane (PubMed:26578515). {ECO:0000269|PubMed:26578515}.
CC -!- SIMILARITY: Belongs to the CARMIL family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA90912.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; FJ009082; ACI49709.1; -; mRNA.
DR EMBL; AK123817; BAC85701.1; -; mRNA.
DR EMBL; AK125696; BAC86250.1; -; mRNA.
DR EMBL; AK000055; BAA90912.1; ALT_INIT; mRNA.
DR EMBL; AL022170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL024509; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160037; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS54973.1; -. [Q5VZK9-1]
DR RefSeq; NP_060110.4; NM_017640.5. [Q5VZK9-1]
DR PDB; 3LK2; X-ray; 2.20 A; T=961-1012.
DR PDB; 3LK3; X-ray; 2.68 A; T=964-1078.
DR PDBsum; 3LK2; -.
DR PDBsum; 3LK3; -.
DR AlphaFoldDB; Q5VZK9; -.
DR SMR; Q5VZK9; -.
DR BioGRID; 120745; 52.
DR DIP; DIP-56920N; -.
DR IntAct; Q5VZK9; 14.
DR MINT; Q5VZK9; -.
DR STRING; 9606.ENSP00000331983; -.
DR GlyGen; Q5VZK9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5VZK9; -.
DR PhosphoSitePlus; Q5VZK9; -.
DR BioMuta; CARMIL1; -.
DR DMDM; 74762279; -.
DR EPD; Q5VZK9; -.
DR jPOST; Q5VZK9; -.
DR MassIVE; Q5VZK9; -.
DR MaxQB; Q5VZK9; -.
DR PaxDb; Q5VZK9; -.
DR PeptideAtlas; Q5VZK9; -.
DR PRIDE; Q5VZK9; -.
DR ProteomicsDB; 65702; -. [Q5VZK9-1]
DR ProteomicsDB; 65703; -. [Q5VZK9-2]
DR ProteomicsDB; 65704; -. [Q5VZK9-3]
DR ProteomicsDB; 65705; -. [Q5VZK9-4]
DR Antibodypedia; 25380; 88 antibodies from 17 providers.
DR DNASU; 55604; -.
DR Ensembl; ENST00000329474.7; ENSP00000331983.6; ENSG00000079691.18. [Q5VZK9-1]
DR GeneID; 55604; -.
DR KEGG; hsa:55604; -.
DR MANE-Select; ENST00000329474.7; ENSP00000331983.6; NM_017640.6; NP_060110.4.
DR UCSC; uc011djw.2; human. [Q5VZK9-1]
DR CTD; 55604; -.
DR DisGeNET; 55604; -.
DR GeneCards; CARMIL1; -.
DR HGNC; HGNC:21581; CARMIL1.
DR HPA; ENSG00000079691; Low tissue specificity.
DR MIM; 609593; gene.
DR neXtProt; NX_Q5VZK9; -.
DR OpenTargets; ENSG00000079691; -.
DR PharmGKB; PA162394368; -.
DR VEuPathDB; HostDB:ENSG00000079691; -.
DR eggNOG; KOG4242; Eukaryota.
DR GeneTree; ENSGT00940000155112; -.
DR HOGENOM; CLU_003119_3_0_1; -.
DR InParanoid; Q5VZK9; -.
DR OMA; DKQENRV; -.
DR OrthoDB; 208951at2759; -.
DR PhylomeDB; Q5VZK9; -.
DR TreeFam; TF316381; -.
DR PathwayCommons; Q5VZK9; -.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; Q5VZK9; -.
DR BioGRID-ORCS; 55604; 10 hits in 1076 CRISPR screens.
DR ChiTaRS; CARMIL1; human.
DR EvolutionaryTrace; Q5VZK9; -.
DR GeneWiki; LRRC16A; -.
DR GenomeRNAi; 55604; -.
DR Pharos; Q5VZK9; Tbio.
DR PRO; PR:Q5VZK9; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5VZK9; protein.
DR Bgee; ENSG00000079691; Expressed in oocyte and 149 other tissues.
DR ExpressionAtlas; Q5VZK9; baseline and differential.
DR Genevisible; Q5VZK9; HS.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031941; C:filamentous actin; ISS:CAFA.
DR GO; GO:0030027; C:lamellipodium; IDA:BHF-UCL.
DR GO; GO:0044354; C:macropinosome; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0051639; P:actin filament network formation; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; NAS:BHF-UCL.
DR GO; GO:0051638; P:barbed-end actin filament uncapping; ISS:CAFA.
DR GO; GO:0016477; P:cell migration; IMP:BHF-UCL.
DR GO; GO:0030032; P:lamellipodium assembly; IMP:BHF-UCL.
DR GO; GO:0044351; P:macropinocytosis; IDA:UniProtKB.
DR GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; ISS:CAFA.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; ISS:CAFA.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:1902745; P:positive regulation of lamellipodium organization; IDA: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; IMP:BHF-UCL.
DR GO; GO:0046415; P:urate metabolic process; IMP:UniProtKB.
DR DisProt; DP01701; -.
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..1371
FT /note="F-actin-uncapping protein LRRC16A"
FT /id="PRO_0000325815"
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 481..506
FT /note="LRR 7"
FT REPEAT 543..566
FT /note="LRR 8"
FT REPEAT 570..593
FT /note="LRR 9"
FT REPEAT 654..678
FT /note="LRR 10"
FT REPEAT 958..981
FT /note="LRR 11"
FT REGION 957..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..1082
FT /note="Inhibits capping activity of CAPZA2"
FT /evidence="ECO:0000250|UniProtKB:Q6EDY6"
FT REGION 1036..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1089
FT /note="Necessary for localization at the cell membrane"
FT /evidence="ECO:0000269|PubMed:26578515"
FT REGION 1172..1371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 710..734
FT /evidence="ECO:0000255"
FT COMPBIAS 1036..1068
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1103..1151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1188..1202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1242..1256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 122
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 916
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 968
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1094
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1228
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1315
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..161
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032415"
FT VAR_SEQ 292..337
FT /note="GVSSLSIQFAKLPKGLKHLNLSKTSLSPKGVNSLSQSLSANPLTAS -> ET
FT TTKIKRQNVPTVLQTYLVVCPSDYQPCPLPLGKDNYYSDFSHDG (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032416"
FT VAR_SEQ 338..1371
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032417"
FT VAR_SEQ 486..499
FT /note="SLDISDNGLESDLS -> QLGTRYRNAVLRVY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032418"
FT VAR_SEQ 500..1371
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032419"
FT VAR_SEQ 1177..1221
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_032420"
FT VARIANT 77
FT /note="V -> I (in dbSNP:rs9358856)"
FT /id="VAR_039923"
FT VARIANT 545
FT /note="P -> L (in dbSNP:rs12207840)"
FT /id="VAR_039924"
FT VARIANT 639
FT /note="A -> G (in dbSNP:rs7454756)"
FT /id="VAR_039925"
FT VARIANT 1117
FT /note="N -> S (in dbSNP:rs9885914)"
FT /id="VAR_039926"
FT CONFLICT 255
FT /note="N -> D (in Ref. 1; BAC85701)"
FT /evidence="ECO:0000305"
FT CONFLICT 889
FT /note="K -> R (in Ref. 1; BAA90912)"
FT /evidence="ECO:0000305"
FT CONFLICT 1202
FT /note="G -> S (in Ref. 1; ACI49709)"
FT /evidence="ECO:0000305"
FT STRAND 978..980
FT /evidence="ECO:0007829|PDB:3LK3"
FT HELIX 985..988
FT /evidence="ECO:0007829|PDB:3LK2"
FT STRAND 999..1002
FT /evidence="ECO:0007829|PDB:3LK3"
FT HELIX 1026..1029
FT /evidence="ECO:0007829|PDB:3LK3"
SQ SEQUENCE 1371 AA; 151557 MW; 6DECD6387FD73DCE CRC64;
MTEESSDVPR ELIESIKDVI GRKIKISVKK KVKLEVKGDK VENKVLVLTS CRAFLVTARI
PTKLELTFSY LEIHGVVCSK SAQMIVETEK CSISMKMASP EDVSEVLAHI GTCLRKIFPG
LSPVRIMKKV SMEPSERLAS LQALWDSQTV AEQGPCGGFS QMYACVCDWL GFSYREEVQW
DVDTIYLTQD TRELNLQDFS HLDHRDLIPI IAALEYNQWF TKLSSKDLKL STDVCEQILR
VVSRSNRLEE LVLENAGLRT DFAQKLASAL AHNPNSGLHT INLAGNPLED RGVSSLSIQF
AKLPKGLKHL NLSKTSLSPK GVNSLSQSLS ANPLTASTLV HLDLSGNVLR GDDLSHMYNF
LAQPNAIVHL DLSNTECSLD MVCGALLRGC LQYLAVLNLS RTVFSHRKGK EVPPSFKQFF
SSSLALMHIN LSGTKLSPEP LKALLLGLAC NHNLKGVSLD LSNCELRSGG AQVLEGCIAE
IHNITSLDIS DNGLESDLST LIVWLSKNRS IQHLALGKNF NNMKSKNLTP VLDNLVQMIQ
DEESPLQSLS LADSKLKTEV TIIINALGSN TSLTKVDISG NGMGDMGAKM LAKALQINTK
LRTVIWDKNN ITAQGFQDIA VAMEKNYTLR FMPIPMYDAS QALKTNPEKT EDALQKIENY
LLRNHETRKY LQEQAYRLQQ GIVTSTTQQM IDRICVKVQD HLNSLRNCGG DAIQEDLKSA
ERLMRDAKNS KTLLPNLYHV GGASWAGASG LLSSPIQETL ESMAGEVTRV VDEQLKALLE
SMVDAAENLC PNVMKKAHIR QDLIHASTEK ISIPRTFVKN VLLEQSGIDI LNKISEVKLT
VASFLSDRIV DEILDALSHC HHKLADHFSR RGKTLPQQES LEIELAEEKP VKRSIITVEE
LTEIERLEDL DTCMMTPKSK RKSIHSRMLR PVSRAFEMEF DLDKALEEVP IHIEDPPFPS
LRQEKRSSGF ISELPSEEGK KLEHFTKLRP KRNKKQQPTQ AAVCAANIVS QDGEQNGLMG
RVDEGVDEFF TKKVTKMDSK KWSTRGSESH ELNEGGDEKK KRDSRKSSGF LNLIKSRSKS
ERPPTILMTE EPSSPKGAVR SPPVDCPRKD TKAAEHNGNS ERIEEIKTPD SFEESQGEEI
GKVERSDSKS SPQAGRRYGV QVMGSGLLAE MKAKQEKRAA CAQKKLGNDA VSQDSSSPAL
SGVERSDGGG AVPKLHPGLP ENRFGLGTPE KNTKAEPKAE AGSRSRSSSS TPTSPKPLLQ
SPKPSLAARP VIPQKPRTAS RPDDIPDSPS SPKVALLPPV LKKVPSDKER DGQSSPQPSP
RTFSQEVSRR SWGQQAQEYQ EQKQRSSSKD GHQGSKSNDS GEEAEKEFIF V
