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 24-JAN-2024, entry version 164. 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, GN 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 72. DR DIP; DIP-56920N; -. DR IntAct; Q5VZK9; 18. 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; 9606-ENSP00000331983; -. DR PeptideAtlas; Q5VZK9; -. DR ProteomicsDB; 65702; -. [Q5VZK9-1] DR ProteomicsDB; 65703; -. [Q5VZK9-2] DR ProteomicsDB; 65704; -. [Q5VZK9-3] DR ProteomicsDB; 65705; -. [Q5VZK9-4] DR Pumba; Q5VZK9; -. DR Antibodypedia; 25380; 100 antibodies from 18 providers. DR DNASU; 55604; -. DR Ensembl; ENST00000329474.7; ENSP00000331983.6; ENSG00000079691.19. [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 AGR; HGNC:21581; -. 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; 5476233at2759; -. 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; 11 hits in 1155 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 151 other cell types or tissues. DR ExpressionAtlas; Q5VZK9; baseline and differential. 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: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; 6.10.140.1850; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1. 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; F-ACTIN-UNCAPPING PROTEIN LRRC16A; 1. DR PANTHER; PTHR24112; LEUCINE-RICH REPEAT, ISOFORM F-RELATED; 1. DR Pfam; PF17888; Carm_PH; 1. DR Pfam; PF16000; CARMIL_C; 1. DR Pfam; PF13516; LRR_6; 2. DR SMART; SM00368; LRR_RI; 6. DR SUPFAM; SSF52047; RNI-like; 2. DR Genevisible; Q5VZK9; HS. 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 //