CARMIL2
entrez
146206
canonical
uniprot
Q6F5E8
canonical
ensembl
ENSG00000159753
resolver
ensp
ENSP00000334958
resolver
ensp
ENSP00000441481
resolver
ensp
ENSP00000512465
resolver
ensp
ENSP00000512466
resolver
enst
ENST00000696175
resolver
enst
ENST00000696176
resolver
genesymbol
CARMIL2
resolver
genesymbol_syn
LRRC16C
resolver
genesymbol_syn
RLTPR
resolver
hgnc
HGNC:27089
resolver
uniprot
A0A8Q3SIB7
resolver
uniprot
A0A8Q3SII9
resolver
uniprot
B8X2Z3
resolver
uniprot_entry
A0A8Q3SIB7_HUMAN
resolver
uniprot_entry
A0A8Q3SII9_HUMAN
resolver
uniprot_entry
CARL2_HUMAN
resolver
uniprot_sec
B8X2Z3
resolver
amino_acid_sequence
MAQTPDGISCELRGEITRFLWPKEVELLLKTWLPGEGAVQNHVLALLRWRAYLLHTTCLPLRVDCTFSYLEVQAMALQETPPQVTFELESLRELVLEFPGVAALEQLAQHVAAAIKKVFPRSTLGKLFRRPTPASMLARLERSSPSESTDPCSPCGGFLETYEALCDYNGFPFREEIQWDVDTIYHRQGCRHFSLGDFSHLGSRDLALSVAALSYNLWFRCLSCVDMKLSLEVSEQILHMMSQSSHLEELVLETCSLRGDFVRRLAQALAGHSSSGLRELSLAGNLLDDRGMTALSRHLERCPGALRRLSLAQTGLTPRGMRALGRALATNAAFDSTLTHLDLSGNPGALGASEDSGGLYSFLSRPNVLSFLNLAGTDTALDTVRGCSVGGWMTGRADWRAGRGGLGPPAGVANSLPPQLFAAVSRGCCTSLTHLDASRNVFSRTKSRAAPAALQLFLSRARTLRHLGLAGCKLPPDALRALLDGLALNTHLRDLHLDLSACELRSAGAQVIQDLVCDAGAVSSLDLADNGFGSDMVTLVLAIGRSRSLRHVALGRNFNVRCKETLDDVLHRIVQLMQDDDCPLQSLSVAESRLKLGASVLLRALATNPNLTALDISGNAMGDAGAKLLAKALRVNSRLRSVVWDRNHTSALGLLDVAQALEQNHSLKAMPLPLNDVAQAQRSRPELTARAVHQIQACLLRNNRADPASSDHTTRLQPLGLVSDPSEQEVNELCQSVQEHVELLGCGAGPQGEAAVRQAEDAIQNANFSLSILPILYEAGSSPSHHWQLGQKLEGLLRQVGEVCRQDIQDFTQATLDTARSLCPQMLQGSSWREQLEGVLAGSRGLPELLPEQLLQDAFTRLRDMRLSITGTLAESIVAQALAGLSAARDQLVESLAQQATVTMPPALPAPDGGEPSLLEPGELEGLFFPEEKEEEKEKDDSPPQKWPELSHGLHLVPFIHSAAEEAEPEPELAAPGEDAEPQAGPSARGSPSPAAPGPPAGPLPRMDLPLAGQPLRHPTRARPRPRRQHHHRPPPGGPQVPPALPQEGNGLSARVDEGVEEFFSKRLIQQDRLWAPEEDPATEGGATPVPRTLRKKLGTLFAFKKPRSTRGPRTDLETSPGAAPRTRKTTFGDLLRPPTRPSRGEELGGAEGDTSSPDPAGRSRPRYTRDSKAYSMILLPAEEEATLGARPDKRRPLERGETELAPSFEQRVQVMLQRIGVSRGSGGAEGKRKQSKDGEIKKAGSDGDIMDSSTEAPPISIKSRTHSVSADPSCRPGPGSQGPESATWKTLGQQLNAELRSRGWGQQDGPGPPSPGQSPSPCRTSPSPDSLGLPEDPCLGPRNEDGQLRPRPLSAGRRAVSVHEDQLQAPAERPLRLQRSPVLKRRPKLEAPPSPSLGSGLGTEPLPPQPTEPSSPERSPPSPATDQRGGGPNP
uniprot
proteins
disease_involvement
DISEASE: Immunodeficiency 58 (IMD58) [MIM:618131]: An autosomal recessive primary immunodeficiency characterized by a variety of infectious diseases, including mycobacterial diseases, mucocutaneous candidiasis, silent but detectable EBV viremia, and staphylococcal diseases. Patients suffer from dermatitis, esophagitis, recurrent skin abscesses and chest infections. Immunologic analysis shows defective T-cell function and deficient CD3/CD28 stimulation responses in both CD4+ and CD8+ T cells. B-cell function may also be impaired. {ECO:0000269|PubMed:27647349, ECO:0000269|PubMed:27896283, ECO:0000269|PubMed:28112205, ECO:0000269|PubMed:29479355}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Cell membrane-cytoskeleton-associated protein that plays a role in the regulation of actin polymerization at the barbed end of actin filaments. Prevents F-actin heterodimeric capping protein (CP) activity at the leading edges of migrating cells, and hence generates uncapped barbed ends and enhances actin polymerization (PubMed:26466680). Plays a role in cell protrusion formations; involved in cell polarity, lamellipodial assembly, membrane ruffling and macropinosome formations (PubMed:19846667, PubMed:26466680, PubMed:26578515). Involved as well in cell migration and invadopodia formation during wound healing (PubMed:19846667, PubMed:26466680, PubMed:26578515). Required for CD28-mediated stimulation of NF-kappa-B signaling, involved in naive T cells activation, maturation into T memory cells, and differentiation into T helper and T regulatory cells (PubMed:27647348, PubMed:27647349, PubMed:28112205). {ECO:0000269|PubMed:19846667, ECO:0000269|PubMed:26466680, ECO:0000269|PubMed:26578515, ECO:0000269|PubMed:27647348, ECO:0000269|PubMed:27647349, ECO:0000269|PubMed:28112205}.
uniprot
proteins
mass_dalton
154689
uniprot
proteins
mutagenesis
MUTAGEN 1021; /note="R->A: Loss of ability to bind heterodimeric capping protein (CP), unable to inhibit the actin-capping activity of CP and to rescue the loss of lamellipodial ruffling, macropinocytosis, cell polarity, and invadopodia-mediated matrix degradation; when associated with A-1023."; /evidence="ECO:0000269|PubMed:26466680"; MUTAGEN 1023; /note="R->A: Loss of ability to bind heterodimeric capping protein (CP), unable to inhibit the actin-capping activity of CP and to rescue the loss of lamellipodial ruffling, macropinocytosis, cell polarity, and invadopodia-mediated matrix degradation; when associated with A-1021."; /evidence="ECO:0000269|PubMed:26466680"; MUTAGEN 1096..1106; /note="KKLGTLFAFKK->EEEEEEEEEEE: Loss of accumulation at the cell membrane. Does not alter colocalization at vimentin filaments. Alters monopolar cell polarity, increasing the number of leading edges lacking lamellipodia and ruffles. Inhibits cell migration during wound healing."; /evidence="ECO:0000269|PubMed:26578515"; MUTAGEN 1096..1106; /note="KKLGTLFAFKK->GGGGGGGGGGG: Loss of accumulation at the cell membrane. Does not alter colocalization at vimentin filaments. Alters monopolar cell polarity, increasing the number of leading edges lacking lamellipodia and ruffles. Inhibits cell migration during wound healing."; /evidence="ECO:0000269|PubMed:26578515"; MUTAGEN 1096..1106; /note="Missing: Loss of accumulation at the cell membrane. Does not alter colocalization at vimentin filaments. Alters monopolar cell polarity, increasing the number of leading edges lacking lamellipodia and ruffles. Inhibits cell migration during wound healing."; /evidence="ECO:0000269|PubMed:26578515
uniprot
proteins
protein_family
CARMIL family
uniprot
proteins
pubmed
15588584
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19846667
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26466680
uniprot
proteins
pubmed
26578515
uniprot
proteins
pubmed
27647348
uniprot
proteins
pubmed
27647349
uniprot
proteins
pubmed
27896283
uniprot
proteins
pubmed
28112205
uniprot
proteins
pubmed
29479355
uniprot
proteins
sequence_length
1435
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19846667, ECO:0000269|PubMed:26466680}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19846667, ECO:0000269|PubMed:26466680, ECO:0000269|PubMed:26578515}. Cell membrane {ECO:0000269|PubMed:26466680, ECO:0000269|PubMed:26578515}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, lamellipodium {ECO:0000269|PubMed:26578515}. Cell projection, ruffle {ECO:0000269|PubMed:26466680, ECO:0000269|PubMed:26578515}. Note=Colocalizes to dynamic vimentin filaments both in the central cytoplasm and at leading edges of migrating cells (PubMed:19846667, PubMed:26466680, PubMed:26578515). Colocalizes with F-actin, Arp2/3 complex and cortactin to leading edge lamellipodia, ruffles and macropinosomes of migrating cells (PubMed:26578515). {ECO:0000269|PubMed:19846667, ECO:0000269|PubMed:26466680, ECO:0000269|PubMed:26578515}.
uniprot
proteins