CARML_DICDI
ID CARML_DICDI Reviewed; 1050 AA.
AC Q95VZ3; Q54D40;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Protein CARMIL;
DE Short=dDcarmil;
DE AltName: Full=Capping protein, arp2/3 and myosin I linker;
DE AltName: Full=Leucine-rich repeat-containing protein p116;
DE Short=p116;
GN Name=carmil; ORFNames=DDB_G0292386;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 843-861 AND 980-986,
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=11425877; DOI=10.1083/jcb.153.7.1479;
RA Jung G., Remmert K., Wu X., Volosky J.M., Hammer J.A. III;
RT "The Dictyostelium CARMIL protein links capping protein and the Arp2/3
RT complex to type I myosins through their SH3 domains.";
RL J. Cell Biol. 153:1479-1497(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP INDUCTION [LARGE SCALE ANALYSIS].
RX PubMed=18590548; DOI=10.1186/1471-2180-8-109;
RA Carilla-Latorre S., Calvo-Garrido J., Bloomfield G., Skelton J., Kay R.R.,
RA Ivens A., Martinez J.L., Escalante R.;
RT "Dictyostelium transcriptional responses to Pseudomonas aeruginosa: common
RT and specific effects from PAO1 and PA14 strains.";
RL BMC Microbiol. 8:109-109(2008).
RN [4]
RP IDENTIFICATION.
RX PubMed=18559084; DOI=10.1186/1471-2164-9-291;
RA Sillo A., Bloomfield G., Balest A., Balbo A., Pergolizzi B., Peracino B.,
RA Skelton J., Ivens A., Bozzaro S.;
RT "Genome-wide transcriptional changes induced by phagocytosis or growth on
RT bacteria in Dictyostelium.";
RL BMC Genomics 9:291-291(2008).
CC -!- FUNCTION: Serves as the scaffold for the assembly of a complex that
CC links key players in the nucleation and termination of actin filament
CC assembly with a ubiquitous barbed end-directed motor. This complex is
CC composed of at least capping proteins (acpA and acpB), the Arp2/3
CC complex, type I myosins (myoB and myoC) and carmil. It has at least a
CC modest ability to activate Arp2/3-dependent actin nucleation. CARMIL
CC localizes along with the Arp2/3 complex, myoB, and myoC in the leading
CC edge of cells and it plays a significant role in the structure and
CC function of these actin-rich cellular extensions.
CC {ECO:0000269|PubMed:11425877}.
CC -!- SUBUNIT: Interacts (via PXXP domains) with myoB and myoC (via SH3
CC domain). Interacts (via N-terminus) with the capping proteins acpA and
CC acpB. Interacts (via the region between the LRR domain and COOH-
CC terminal proline-rich domain) with the seven member Arp2/3 complex
CC (arpB/Arp2, arpC/Arp3, arcA/p41-arc, arcB/p34-arc, arcC/p21-arc,
CC arcD/p20-arc and arcE/p16-arc). {ECO:0000269|PubMed:11425877}.
CC -!- SUBCELLULAR LOCATION: Cell projection, pseudopodium
CC {ECO:0000269|PubMed:11425877}. Note=Found in dynamic actin-rich
CC cellular extensions, including the leading edge of cells undergoing
CC chemotactic migration, and dorsal, cup-like, macropinocytic extensions.
CC -!- INDUCTION: Down-regulated by Pseudomonas aeruginosa, PAO1 strain and
CC PA14 strain infection. {ECO:0000269|PubMed:18590548}.
CC -!- DISRUPTION PHENOTYPE: Cells exhibit a striking defect in the formation
CC of dorsal, cup-like, macropinocytic structures, a concomitant reduction
CC in the rate of fluid phase pinocytosis, a significant decrease in the
CC efficiency of chemotactic aggregation, and a decrease in cellular F-
CC actin content. {ECO:0000269|PubMed:11425877}.
CC -!- SIMILARITY: Belongs to the CARMIL family. {ECO:0000305}.
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DR EMBL; AF388524; AAK72255.1; -; Genomic_DNA.
DR EMBL; AAFI02000190; EAL61172.1; -; Genomic_DNA.
DR RefSeq; XP_629656.1; XM_629654.1.
DR AlphaFoldDB; Q95VZ3; -.
DR SMR; Q95VZ3; -.
DR STRING; 44689.DDB0185176; -.
DR PaxDb; Q95VZ3; -.
DR EnsemblProtists; EAL61172; EAL61172; DDB_G0292386.
DR GeneID; 8628720; -.
DR KEGG; ddi:DDB_G0292386; -.
DR dictyBase; DDB_G0292386; carmil.
DR eggNOG; KOG4242; Eukaryota.
DR HOGENOM; CLU_003119_3_0_1; -.
DR InParanoid; Q95VZ3; -.
DR OMA; ASDYTYE; -.
DR PhylomeDB; Q95VZ3; -.
DR Reactome; R-DDI-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:Q95VZ3; -.
DR Proteomes; UP000002195; Chromosome 6.
DR GO; GO:0015629; C:actin cytoskeleton; TAS:dictyBase.
DR GO; GO:0031252; C:cell leading edge; IDA:dictyBase.
DR GO; GO:0030027; C:lamellipodium; IBA:GO_Central.
DR GO; GO:0061851; C:leading edge of lamellipodium; IDA:dictyBase.
DR GO; GO:0070685; C:macropinocytic cup; IDA:dictyBase.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:dictyBase.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0017024; F:myosin I binding; IDA:dictyBase.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
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; IDA:dictyBase.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
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 Pfam; PF17888; Carm_PH; 1.
DR Pfam; PF13516; LRR_6; 3.
PE 1: Evidence at protein level;
KW Cell projection; Direct protein sequencing; Leucine-rich repeat;
KW Reference proteome; Repeat.
FT CHAIN 1..1050
FT /note="Protein CARMIL"
FT /id="PRO_0000390402"
FT REPEAT 243..266
FT /note="LRR 1"
FT REPEAT 268..291
FT /note="LRR 2"
FT REPEAT 329..352
FT /note="LRR 3"
FT REPEAT 383..409
FT /note="LRR 4"
FT REPEAT 411..436
FT /note="LRR 5"
FT REPEAT 442..464
FT /note="LRR 6"
FT REPEAT 470..493
FT /note="LRR 7"
FT REPEAT 563..590
FT /note="LRR 8"
FT REGION 1..179
FT /note="Required for interaction with capping protein"
FT REGION 851..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1050
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 959..963
FT /note="PXXP motif; important for binding to SH3 domain-
FT containing proteins"
FT MOTIF 968..971
FT /note="PXXP motif; important for binding to SH3 domain-
FT containing proteins"
FT COMPBIAS 864..889
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..923
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..971
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1011..1025
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 852
FT /note="Q -> G (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1050 AA; 113887 MW; D6F18849AA9C692B CRC64;
MSEEISPNDR KFITNLLTQK NQESLLLSIG DKISKKKNKK PSKRIILITK NRIFFLKPSQ
NKVKKDIHLL DIQEIKSSTS NEFTIVAKVD NKQFSYGLIT NKTDEIINQI RVTFNHQFFG
CPEESTFKCT DIKDSRLVEI EQKDLPCGGF VETYQSICDH LGVPPRDDIC WDMTNIISSK
NIRSFNIGEI ELPTSAGDTI RCLLGALKYN NYFKSFNFNN YTFNKEQFGY LAEVLKCNST
VEDLSLNNVG LKHDTMPIIA TALSSNKNLA LTAIDISNNQ IEDKGMTAFS SYVASSLRGI
ASLDVSNTNC NKAGISVLTN ALKKNIKMSS TLSYLNLSGN KMEADGSAGL SSFLASPNTL
KTLNISNTTP SMETIVGALV IGCAELKTID ISDNKLTKKE VPHLVRFIGA SSTLKHFNLS
GTKVPVENLK ELVVAITSNI YLQDVVLDLK NNDLGIAGAR MLASLATDKL SNVIYLDVSE
NDFGDEGVSV ICDGFVGNST IKKLILNGNF KQSKTKSRPS AIESVISLLE SECPLETLHM
TVGNSKSPLK ADILSLIYSL ATNSSLLELD ISGHQMGPKG AIGLGKALQT NKTLHTLIWD
DNLTTAIGFA GFQVGLERNL TLKNMPTPLN DIIQCHREPK FQQIWKEIDS CINRNQSPTR
AFEGNGGNSI GATNLSFLAS GQQQGVEKLL NKIKSIGRKV TDPNNILIVK DAESTEKVIG
GIHLIKESIH ASLEMELNQK LKDFVQVVND VINAKKNEMT QQILESMQNT FQSMDGPTIK
RLATTIQYGS KDVDEQQIHS TLVKGAGAEL SSRAHECFIS ALDIASDYTY EKITIGLDSV
FKDLILEESQ AQNEASGATP IPDSPVPTRS PQPTSPPITP QPTPTTNVPP VTAPRTGAAA
PLKPANPPPV STTTTPPVST TPKPTQPVSK FGAKLSANSA VAEAIARNMG GGAPPIRKPV
APEPEPEPVT PTKDVTPLKS KPVVAPRSTP TTSTPTKTPV KKPSGPSVPG SLSDAPESDS
AELTHVTASR PHIASKRKPP TRRPRPPTEN
