ID A0A2K6FWS8_PROCO Unreviewed; 1332 AA.
AC A0A2K6FWS8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Capping protein regulator and myosin 1 linker 1 {ECO:0000313|Ensembl:ENSPCOP00000018425.1};
GN Name=CARMIL1 {ECO:0000313|Ensembl:ENSPCOP00000018425.1};
OS Propithecus coquereli (Coquerel's sifaka) (Propithecus verreauxi
OS coquereli).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC Indriidae; Propithecus.
OX NCBI_TaxID=379532 {ECO:0000313|Ensembl:ENSPCOP00000018425.1, ECO:0000313|Proteomes:UP000233160};
RN [1] {ECO:0000313|Ensembl:ENSPCOP00000018425.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the CARMIL family.
CC {ECO:0000256|ARBA:ARBA00007298}.
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DR STRING; 379532.ENSPCOP00000018425; -.
DR Ensembl; ENSPCOT00000029067.1; ENSPCOP00000018425.1; ENSPCOG00000021104.1.
DR GeneTree; ENSGT00940000155112; -.
DR OMA; DKQENRV; -.
DR Proteomes; UP000233160; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0031941; C:filamentous actin; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0044354; C:macropinosome; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0051639; P:actin filament network formation; IEA:Ensembl.
DR GO; GO:0051638; P:barbed-end actin filament uncapping; IEA:Ensembl.
DR GO; GO:0016477; P:cell migration; IEA:Ensembl.
DR GO; GO:0030032; P:lamellipodium assembly; IEA:Ensembl.
DR GO; GO:0044351; P:macropinocytosis; IEA:Ensembl.
DR GO; GO:2000813; P:negative regulation of barbed-end actin filament capping; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:1902745; P:positive regulation of lamellipodium organization; IEA:Ensembl.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IEA:Ensembl.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IEA:Ensembl.
DR GO; GO:0031529; P:ruffle organization; IEA:Ensembl.
DR GO; GO:0046415; P:urate metabolic process; IEA:Ensembl.
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; 5.
DR SUPFAM; SSF52047; RNI-like; 2.
PE 3: Inferred from homology;
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Reference proteome {ECO:0000313|Proteomes:UP000233160}.
FT DOMAIN 26..119
FT /note="CARMIL pleckstrin homology"
FT /evidence="ECO:0000259|Pfam:PF17888"
FT DOMAIN 743..1036
FT /note="CARMIL C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16000"
FT REGION 994..1119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1023
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1060..1109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1146..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1304..1332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1332 AA; 147205 MW; 6264334C35FBC4FB CRC64;
MTEESADVPR ELIESIKDVI GRKIKIAVKK KVKLEVKGDK VENKVLVLTS CRAFLVTARI
PTKLELTFSY LEIHGVICCK PAQMVVETEK CSISMKMASP EDVIDVLAHI GTCLRKIFPG
LSPVRIMKRV SVEPSERLAS LQALWDSQTV AEQGPCGGFS QMYACACDWL GFSYREEVQW
DVDTIYLTQD TRELNLQDFS HLDHRDLIPI IAALEYNQWF TKLSSKDLKL STDVCEQILR
VVSRSNRLEE LVLENAGLRT DFAQKLASAL AHNPNSGLHT INLAGNPLED RGVSSLSVQF
AKLPKGLKYL NLSKTSLSPK GVNSLSQSLS ANPLTASTLI HLDLSGNVLR GDDLSHMYNF
LAQPNAIAHL DLSNTECSLE MVCGALLRGC LQYLAVLNLS RTVFSHRKGK EVPPSFKQFF
SSSLALMQIN LSGTKLSPEP LKALLLGLAC NHSLKGVSLD LSNCELRSGG AQVLEGCIAE
IHNITSLDIS DNGLESDLST LIVWLGKNRS IQHLALGRNF NNMKSKNLTP VLDNLVQMIQ
DEESPLQSLS LADSKLKTEV TIIINALGSN TSLTKVDISG NGMGDMGAKM LAKALQINTK
LRTVIWDKNN ITAQGFQDIA VAMEKNYTLR FMPIPMYDAS QALKTNPEKT EEALQKIENY
LLRNHETRKY LQEQAYRLQQ GIVTSTTQQL LPNLYHVGGA SWAGATGLLS SPIQETLESM
AGEVTRVVDE QLKALLESMV DAAENLCPSV MKKAHIRQDL IRASTEKISI PRTFVKNVLL
EQSGIDILNK ISEVKLTVAS FLSDRIVDEI LDALSHCHHK LADHFSRRGK TLPQQESSEI
ELAEEKPVKR SIITVEELTE IERLEDLDTC MMTPKSKRKS IHSRMLRPVS RAFEMEFDLD
KALEEVPIHI EDPPFPSIRQ EKWSSGFISE LPSEEGKRLE HFTKLRPKRN KKQQPTQAAV
CAANIVSQDG EQNGLMGRVD EGVDEFFTKK VTKMDSKKWS TRGSESQELS EGGDEKKKRD
SWKSGGFLNL IKSRSKSERP PTVLMTEEPS SPKGSVRSQA VDTPRKDTKA AEHIGSSEQR
IEEIKTPDSF EDNQGEETGK VDRSDSKSSP QGGRRYGVQV MGSGLLAEMK AKQEKRAACA
QKKLVNDAIS QDSSSPALSN MERLDGGGAV PKLHPGLPES RFGLGTPEKN AKAEPKVEGG
SRSCSSSSTP PSPKPLLQSP KPSLVTRPII PQKPRTTSRP EDILDSPSGS SSHKVALLPP
VLKKVPSDKE RDGQSSPQPS PRTFSQEISR RSWGQQAQEY QEQKQRSSSK DGHQGSKSSD
SGEEAEKEFI FV
//
