ID Q7JP75_CAEEL Unreviewed; 1437 AA.
AC Q7JP75;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 2.
DT 27-MAR-2024, entry version 153.
DE SubName: Full=WAPL domain-containing protein {ECO:0000313|EMBL:CCD63399.2};
GN Name=cyk-1 {ECO:0000313|EMBL:CCD63399.2,
GN ECO:0000313|WormBase:F11H8.4b};
GN ORFNames=CELE_F11H8.4 {ECO:0000313|EMBL:CCD63399.2}, F11H8.4
GN {ECO:0000313|WormBase:F11H8.4b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CCD63399.2, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CCD63399.2, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CCD63399.2,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- INTERACTION:
CC Q7JP75; G5EC32: sorb-1; NbExp=6; IntAct=EBI-2003118, EBI-325337;
CC -!- SIMILARITY: Belongs to the formin homology family. Diaphanous
CC subfamily. {ECO:0000256|ARBA:ARBA00008214}.
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DR EMBL; BX284603; CCD63399.2; -; Genomic_DNA.
DR RefSeq; NP_741211.3; NM_171880.4.
DR AlphaFoldDB; Q7JP75; -.
DR SMR; Q7JP75; -.
DR IntAct; Q7JP75; 3.
DR STRING; 6239.F11H8.4b.1; -.
DR EPD; Q7JP75; -.
DR PaxDb; 6239-F11H8-4b; -.
DR EnsemblMetazoa; F11H8.4b.1; F11H8.4b.1; WBGene00000872.
DR GeneID; 175983; -.
DR UCSC; F11H8.4b; c. elegans.
DR AGR; WB:WBGene00000872; -.
DR WormBase; F11H8.4b; CE48031; WBGene00000872; cyk-1.
DR eggNOG; KOG1924; Eukaryota.
DR GeneTree; ENSGT00960000189248; -.
DR InParanoid; Q7JP75; -.
DR OMA; FHHCIES; -.
DR OrthoDB; 1118745at2759; -.
DR PhylomeDB; Q7JP75; -.
DR Reactome; R-CEL-5663220; RHO GTPases Activate Formins.
DR Reactome; R-CEL-6785631; ERBB2 Regulates Cell Motility.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8980692; RHOA GTPase cycle.
DR Reactome; R-CEL-9013149; RAC1 GTPase cycle.
DR Reactome; R-CEL-9013405; RHOD GTPase cycle.
DR Reactome; R-CEL-9013406; RHOQ GTPase cycle.
DR Reactome; R-CEL-9013423; RAC3 GTPase cycle.
DR Reactome; R-CEL-9035034; RHOF GTPase cycle.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000872; Expressed in germ line (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; Q7JP75; baseline and differential.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005826; C:actomyosin contractile ring; IDA:WormBase.
DR GO; GO:0032154; C:cleavage furrow; IDA:WormBase.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:WormBase.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR GO; GO:0035046; P:pronuclear migration; IGI:WormBase.
DR Gene3D; 1.20.58.630; -; 1.
DR Gene3D; 6.10.30.30; -; 1.
DR Gene3D; 1.20.58.2220; Formin, FH2 domain; 1.
DR Gene3D; 1.10.238.150; Formin, FH3 diaphanous domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR InterPro; IPR010472; FH3_dom.
DR InterPro; IPR014768; GBD/FH3_dom.
DR InterPro; IPR010473; GTPase-bd.
DR PANTHER; PTHR45691; PROTEIN DIAPHANOUS; 1.
DR PANTHER; PTHR45691:SF6; PROTEIN DIAPHANOUS; 1.
DR Pfam; PF06367; Drf_FH3; 1.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM01139; Drf_FH3; 1.
DR SMART; SM01140; Drf_GBD; 1.
DR SMART; SM00498; FH2; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF101447; Formin homology 2 domain (FH2 domain); 1.
DR PROSITE; PS51444; FH2; 1.
DR PROSITE; PS51232; GBD_FH3; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Proteomics identification {ECO:0007829|EPD:Q7JP75,
KW ECO:0007829|PeptideAtlas:Q7JP75};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940}.
FT DOMAIN 196..614
FT /note="GBD/FH3"
FT /evidence="ECO:0000259|PROSITE:PS51232"
FT DOMAIN 806..1208
FT /note="FH2"
FT /evidence="ECO:0000259|PROSITE:PS51444"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1197..1228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1373..1437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1090..1117
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 37..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..793
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1437 AA; 159929 MW; F0A43CDFA7475EB8 CRC64;
MSSDDYESID TPRVASLADM NRLPTQSRHS SYSTDDDEDV TPTPSASNSA PKNTILDPLQ
AQFLHPNSEN SDIDEPRVQL REKKKATRAQ DATVSHFLED QVPNQKFKRR SAERHSMLAG
AADFASRRSP FHLSGANGSG RWTDLFSSSR FKRKQRQKLN NVPSSSYSNN DYGTYAGTQS
IGGFSIASNS SGESFALSGT EDEIREEFRK IMLDKGLPEA DKIISNTPLD QMKMMIENSR
KQDNQAKGRS PEWVVRVLGE ILKTKNIPEC KQDIVTVRVQ LVGQGVSFLN KFAVEVHDES
GRTGADLICC LYSLVLKRLR SSEVGSKYEL DLIDFLQEIV RCVRTLINTH VGLVLVLRRN
SPVYSLLIQT LCVLNRREQN DHEAAEIRAI RVDVVRTCYT LIFVQHDTLS TPIEMTGQQK
MFMELSLIAK AESKRLNEPV SRFRPLISCI DFLESRDPKQ GMYVLLMINM MINGVDRNIS
DDQMWTEETM WQARMRLRSE AAKDKLHKYI EKFTTSETVN SQIRDVAQNM LTEHNADLET
LMGKLENVKG EYDTLDGCFE LLAANSEATG TETVLLSILQ LMTLTNEDMS TKRSYMKLIE
TAISDILLHR TPIDPQADYK FVFEVPVAEI IDKMQDEEMA KKVRQATSAK QEAVAMQGEY
WKTLCDFQKE AEELRKHIND PKIPLPPPTK MNLSAPSTSA GGSSALPPIT GGPPPPPGLP
PITGGPPPPP PPGGLPPITG GPPPPPPPGG LPPISGGPPP PPPPPGGCPP PPPPPPPGGF
KGGPPPPPPP GMFAPMAPVI PDYLPPKKVP KVDGPMRKFP WGAHTINPRD IPRESFWVGT
NEEQLTSDRM FDRLRTKFAT KPAANSGTLG GVLNSKKKVK TAQVIHDDKL LQKLGILQGS
IKMSHSELKL AILEVNEKVL TVGFLEQLRS AMPVEKELID KLRAVNKAQF EEMPEGEQFV
TRLLQIQGLP LRLDLVLFKM RFSEVLNELK PAMSSVMEAC EEVRASEGFR TFLKLVLATG
NFMGGATKNY SSAYAFDMRM LTRLVDTKDV DNRHTLLHHL IEEMKRIDPR RARFALTDFH
HCIESSRVNA DEIRKTVQLT ENNIKKLENC LKVYKIQGER DLFDEKMRPF HEKAVKEFST
VSSMCGKMKN DWESLVKYYA FNDKKYPMEE FFADIRTFSE QYSNAWKELD AEAEAKRKEA
EFETQKRKQL QQSQQERKPL QERQAINRVP RTPAAMIRVS TAADKAGVLD ELERATGNAD
FLQTLMSATN SRTPRSGLPA RTRGGGRLGG GLDRQRSRHQ NALGQLQDLT GCASEPVLSG
QFARSRNVPQ NDLQRQNMEL PSSVKPTTAL DRAKAFGVGL PIGQNELKVR VRRKGQPAVP
VTNINGTSQI SPTHKENDPT GSSSTSSGPA SSNTATSSSS GTVVPSTDDL LARLNDF
//
