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Protein

Capping protein, Arp2/3 and myosin-I linker protein 2

Gene

CARMIL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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:26578515, PubMed:26466680). Involved as well in cell migration and invadopodia formation during wound healing (PubMed:19846667, PubMed:26578515, PubMed:26466680).3 Publications

GO - Molecular functioni

  • phospholipid binding Source: UniProtKB
  • protein complex binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Capping protein, Arp2/3 and myosin-I linker protein 21 Publication
Alternative name(s):
Capping protein regulator and myosin 1 linker 2Imported
F-actin-uncapping protein RLTPRCurated
Leucine-rich repeat-containing protein 16C
RGD, leucine-rich repeat, tropomodulin and proline-rich-containing protein1 Publication
Gene namesi
Name:CARMIL2Imported
Synonyms:LRRC16C, RLTPR1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:27089. RLTPR.

Subcellular locationi

Isoform 2 :

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cell-cell junction Source: Ensembl
  • cell leading edge Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • F-actin capping protein complex Source: Ensembl
  • immunological synapse Source: Ensembl
  • intermediate filament cytoskeleton Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • macropinosome Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • ruffle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1021 – 10211R → 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. 1 Publication
Mutagenesisi1023 – 10231R → 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. 1 Publication
Mutagenesisi1096 – 110611KKLGTLFAFKK → 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 migation during wound healing. 1 PublicationAdd
BLAST
Mutagenesisi1096 – 110611KKLGTLFAFKK → 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 migation during wound healing. 1 PublicationAdd
BLAST
Mutagenesisi1096 – 110611Missing : 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 migation during wound healing. 1 PublicationAdd
BLAST

Organism-specific databases

PharmGKBiPA162401371.

Polymorphism and mutation databases

BioMutaiRLTPR.
DMDMi172045901.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14351435Capping protein, Arp2/3 and myosin-I linker protein 2PRO_0000325817Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei991 – 9911PhosphoserineCombined sources
Modified residuei993 – 9931PhosphoserineCombined sources
Modified residuei1120 – 11201PhosphoserineBy similarity
Modified residuei1246 – 12461PhosphoserineCombined sources
Modified residuei1315 – 13151PhosphoserineBy similarity
Modified residuei1420 – 14201PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ6F5E8.
MaxQBiQ6F5E8.
PaxDbiQ6F5E8.
PeptideAtlasiQ6F5E8.
PRIDEiQ6F5E8.

PTM databases

iPTMnetiQ6F5E8.
PhosphoSiteiQ6F5E8.

Expressioni

Tissue specificityi

Expressed in all tissues tested, including thymus, spleen, colon, leukocytes, peripheral blood, skin, skin keratinocytes and skin fibroblasts.1 Publication

Developmental stagei

Expressed in fetal skin.1 Publication

Gene expression databases

BgeeiENSG00000159753.
CleanExiHS_RLTPR.
ExpressionAtlasiQ6F5E8. baseline and differential.
GenevisibleiQ6F5E8. HS.

Organism-specific databases

HPAiHPA041402.

Interactioni

Subunit structurei

Isoform 2: Interacts (via C-terminus) with heterodimeric capping protein (CP); the interaction inhibits CP activity and hence promotes actin polymerization at the barbed end of actin filaments (PubMed:26466680).1 Publication

GO - Molecular functioni

  • protein complex binding Source: UniProtKB

Protein-protein interaction databases

BioGridi126970. 4 interactions.
IntActiQ6F5E8. 2 interactions.
STRINGi9606.ENSP00000334958.

Structurei

3D structure databases

ProteinModelPortaliQ6F5E8.
SMRiQ6F5E8. Positions 39-758.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati64 – 8825LRR 1Add
BLAST
Repeati89 – 11123LRR 2Add
BLAST
Repeati249 – 27224LRR 3Add
BLAST
Repeati274 – 29724LRR 4Add
BLAST
Repeati303 – 32624LRR 5Add
BLAST
Repeati335 – 36228LRR 6Add
BLAST
Repeati393 – 42331LRR 7Add
BLAST
Repeati429 – 45224LRR 8Add
BLAST
Repeati461 – 48121LRR 9Add
BLAST
Repeati492 – 51423LRR 10Add
BLAST
Repeati519 – 54325LRR 11Add
BLAST
Repeati546 – 57227LRR 12Add
BLAST
Repeati581 – 60424LRR 13Add
BLAST
Repeati608 – 63124LRR 14Add
BLAST
Repeati636 – 66025LRR 15Add
BLAST
Repeati664 – 68724LRR 16Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni573 – 66795Tropomodulin-likeAdd
BLAST
Regioni1087 – 111428Necessary for localization at the cell membrane1 PublicationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi905 – 1046142Pro-richAdd
BLAST
Compositional biasi1311 – 1435125Pro-richAdd
BLAST

Domaini

The N-terminal leucine-rich repeat (LRR) domain is necessary for localization to vimentin filaments (PubMed:26466680). The C-terminus is necessary for localization to the cell membrane (PubMed:26578515).2 Publications

Sequence similaritiesi

Belongs to the CARMIL family.Curated
Contains 16 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG4242. Eukaryota.
ENOG410YEE1. LUCA.
GeneTreeiENSGT00390000014487.
HOGENOMiHOG000230565.
HOVERGENiHBG108095.
InParanoidiQ6F5E8.
OMAiKKVFPRS.
OrthoDBiEOG091G01FI.
PhylomeDBiQ6F5E8.
TreeFamiTF316381.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR029763. CARMIL2.
IPR031943. CARMIL_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
PANTHERiPTHR24112:SF32. PTHR24112:SF32. 3 hits.
PfamiPF16000. CARMIL_C. 1 hit.
PF13516. LRR_6. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6F5E8-1) [UniParc]FASTAAdd to basket
Also known as: CARMIL2a1 Publication

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAQTPDGISC ELRGEITRFL WPKEVELLLK TWLPGEGAVQ NHVLALLRWR
60 70 80 90 100
AYLLHTTCLP LRVDCTFSYL EVQAMALQET PPQVTFELES LRELVLEFPG
110 120 130 140 150
VAALEQLAQH VAAAIKKVFP RSTLGKLFRR PTPASMLARL ERSSPSESTD
160 170 180 190 200
PCSPCGGFLE TYEALCDYNG FPFREEIQWD VDTIYHRQGC RHFSLGDFSH
210 220 230 240 250
LGSRDLALSV AALSYNLWFR CLSCVDMKLS LEVSEQILHM MSQSSHLEEL
260 270 280 290 300
VLETCSLRGD FVRRLAQALA GHSSSGLREL SLAGNLLDDR GMTALSRHLE
310 320 330 340 350
RCPGALRRLS LAQTGLTPRG MRALGRALAT NAAFDSTLTH LDLSGNPGAL
360 370 380 390 400
GASEDSGGLY SFLSRPNVLS FLNLAGTDTA LDTVRGCSVG GWMTGRADWR
410 420 430 440 450
AGRGGLGPPA GVANSLPPQL FAAVSRGCCT SLTHLDASRN VFSRTKSRAA
460 470 480 490 500
PAALQLFLSR ARTLRHLGLA GCKLPPDALR ALLDGLALNT HLRDLHLDLS
510 520 530 540 550
ACELRSAGAQ VIQDLVCDAG AVSSLDLADN GFGSDMVTLV LAIGRSRSLR
560 570 580 590 600
HVALGRNFNV RCKETLDDVL HRIVQLMQDD DCPLQSLSVA ESRLKLGASV
610 620 630 640 650
LLRALATNPN LTALDISGNA MGDAGAKLLA KALRVNSRLR SVVWDRNHTS
660 670 680 690 700
ALGLLDVAQA LEQNHSLKAM PLPLNDVAQA QRSRPELTAR AVHQIQACLL
710 720 730 740 750
RNNRADPASS DHTTRLQPLG LVSDPSEQEV NELCQSVQEH VELLGCGAGP
760 770 780 790 800
QGEAAVRQAE DAIQNANFSL SILPILYEAG SSPSHHWQLG QKLEGLLRQV
810 820 830 840 850
GEVCRQDIQD FTQATLDTAR SLCPQMLQGS SWREQLEGVL AGSRGLPELL
860 870 880 890 900
PEQLLQDAFT RLRDMRLSIT GTLAESIVAQ ALAGLSAARD QLVESLAQQA
910 920 930 940 950
TVTMPPALPA PDGGEPSLLE PGELEGLFFP EEKEEEKEKD DSPPQKWPEL
960 970 980 990 1000
SHGLHLVPFI HSAAEEAEPE PELAAPGEDA EPQAGPSARG SPSPAAPGPP
1010 1020 1030 1040 1050
AGPLPRMDLP LAGQPLRHPT RARPRPRRQH HHRPPPGGPQ VPPALPQEGN
1060 1070 1080 1090 1100
GLSARVDEGV EEFFSKRLIQ QDRLWAPEED PATEGGATPV PRTLRKKLGT
1110 1120 1130 1140 1150
LFAFKKPRST RGPRTDLETS PGAAPRTRKT TFGDLLRPPT RPSRGEELGG
1160 1170 1180 1190 1200
AEGDTSSPDP AGRSRPRYTR DSKAYSMILL PAEEEATLGA RPDKRRPLER
1210 1220 1230 1240 1250
GETELAPSFE QRVQVMLQRI GVSRGSGGAE GKRKQSKDGE IKKAGSDGDI
1260 1270 1280 1290 1300
MDSSTEAPPI SIKSRTHSVS ADPSCRPGPG SQGPESATWK TLGQQLNAEL
1310 1320 1330 1340 1350
RSRGWGQQDG PGPPSPGQSP SPCRTSPSPD SLGLPEDPCL GPRNEDGQLR
1360 1370 1380 1390 1400
PRPLSAGRRA VSVHEDQLQA PAERPLRLQR SPVLKRRPKL EAPPSPSLGS
1410 1420 1430
GLGTEPLPPQ PTEPSSPERS PPSPATDQRG GGPNP
Length:1,435
Mass (Da):154,689
Last modified:March 18, 2008 - v2
Checksum:iB0D452CE375436A5
GO
Isoform 2 (identifier: Q6F5E8-2) [UniParc]FASTAAdd to basket
Also known as: CARMIL2b1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     384-419: Missing.
     1346-1372: Missing.

Show »
Length:1,372
Mass (Da):148,208
Checksum:i00F54C84A1D25869
GO

Sequence cautioni

The sequence BAD26751 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei384 – 41936Missing in isoform 2. 1 PublicationVSP_047857Add
BLAST
Alternative sequencei1346 – 137227Missing in isoform 2. 1 PublicationVSP_047858Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB113647 mRNA. Translation: BAD26751.1. Different initiation.
FJ026014 mRNA. Translation: ACI49710.1.
AC009095 Genomic DNA. No translation available.
AC010530 Genomic DNA. No translation available.
CCDSiCCDS45513.1. [Q6F5E8-1]
RefSeqiNP_001013860.1. NM_001013838.1. [Q6F5E8-1]
NP_001303955.1. NM_001317026.1. [Q6F5E8-2]
UniGeneiHs.611432.

Genome annotation databases

EnsembliENST00000334583; ENSP00000334958; ENSG00000159753. [Q6F5E8-1]
ENST00000545661; ENSP00000441481; ENSG00000159753. [Q6F5E8-2]
GeneIDi146206.
KEGGihsa:146206.
UCSCiuc002etn.4. human. [Q6F5E8-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB113647 mRNA. Translation: BAD26751.1. Different initiation.
FJ026014 mRNA. Translation: ACI49710.1.
AC009095 Genomic DNA. No translation available.
AC010530 Genomic DNA. No translation available.
CCDSiCCDS45513.1. [Q6F5E8-1]
RefSeqiNP_001013860.1. NM_001013838.1. [Q6F5E8-1]
NP_001303955.1. NM_001317026.1. [Q6F5E8-2]
UniGeneiHs.611432.

3D structure databases

ProteinModelPortaliQ6F5E8.
SMRiQ6F5E8. Positions 39-758.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126970. 4 interactions.
IntActiQ6F5E8. 2 interactions.
STRINGi9606.ENSP00000334958.

PTM databases

iPTMnetiQ6F5E8.
PhosphoSiteiQ6F5E8.

Polymorphism and mutation databases

BioMutaiRLTPR.
DMDMi172045901.

Proteomic databases

EPDiQ6F5E8.
MaxQBiQ6F5E8.
PaxDbiQ6F5E8.
PeptideAtlasiQ6F5E8.
PRIDEiQ6F5E8.

Protocols and materials databases

DNASUi146206.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000334583; ENSP00000334958; ENSG00000159753. [Q6F5E8-1]
ENST00000545661; ENSP00000441481; ENSG00000159753. [Q6F5E8-2]
GeneIDi146206.
KEGGihsa:146206.
UCSCiuc002etn.4. human. [Q6F5E8-1]

Organism-specific databases

CTDi146206.
GeneCardsiRLTPR.
HGNCiHGNC:27089. RLTPR.
HPAiHPA041402.
MIMi610859. gene.
neXtProtiNX_Q6F5E8.
PharmGKBiPA162401371.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4242. Eukaryota.
ENOG410YEE1. LUCA.
GeneTreeiENSGT00390000014487.
HOGENOMiHOG000230565.
HOVERGENiHBG108095.
InParanoidiQ6F5E8.
OMAiKKVFPRS.
OrthoDBiEOG091G01FI.
PhylomeDBiQ6F5E8.
TreeFamiTF316381.

Miscellaneous databases

GenomeRNAii146206.
PROiQ6F5E8.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000159753.
CleanExiHS_RLTPR.
ExpressionAtlasiQ6F5E8. baseline and differential.
GenevisibleiQ6F5E8. HS.

Family and domain databases

Gene3Di3.80.10.10. 2 hits.
InterProiIPR029763. CARMIL2.
IPR031943. CARMIL_C.
IPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
[Graphical view]
PANTHERiPTHR24112:SF32. PTHR24112:SF32. 3 hits.
PfamiPF16000. CARMIL_C. 1 hit.
PF13516. LRR_6. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCARL2_HUMAN
AccessioniPrimary (citable) accession number: Q6F5E8
Secondary accession number(s): B8X2Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 18, 2008
Last modified: September 7, 2016
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.