EXC6_CAEEL
ID EXC6_CAEEL Reviewed; 843 AA.
AC Q9TYU9;
DT 16-SEP-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Excretory canal abnormal protein 6 {ECO:0000312|WormBase:F58B6.2};
GN Name=exc-6 {ECO:0000312|WormBase:F58B6.2};
GN Synonyms=inft-1 {ECO:0000312|WormBase:F58B6.2};
GN ORFNames=F58B6.2 {ECO:0000312|WormBase:F58B6.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ILE-213; LYS-360 AND GLY-361.
RX PubMed=25771894; DOI=10.1016/j.devcel.2015.01.009;
RA Shaye D.D., Greenwald I.;
RT "The disease-associated formin INF2/EXC-6 organizes lumen and cell
RT outgrowth during tubulogenesis by regulating F-actin and microtubule
RT cytoskeletons.";
RL Dev. Cell 32:743-755(2015).
CC -!- FUNCTION: Constitutively active protein required for microtubule and F-
CC actin growth, structural maintenance and organization during excretory
CC cell tubulogenesis. {ECO:0000269|PubMed:25771894}.
CC -!- INTERACTION:
CC Q9TYU9; G5EC32: sorb-1; NbExp=4; IntAct=EBI-2317613, EBI-325337;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:25771894}. Note=Localizes to leading edge F-actin
CC and microtubules. {ECO:0000269|PubMed:25771894}.
CC -!- TISSUE SPECIFICITY: Expressed in the excretory cell and mostly
CC accumulates at the tip of the excretory cell canals.
CC {ECO:0000269|PubMed:25771894}.
CC -!- DISRUPTION PHENOTYPE: Defective cytoskeleton organization characterized
CC by disrupted F-actin and microtubule dynamics leading to abnormal
CC excretory cell tubulogenesis. Specifically, F-actin structure and
CC organization in excretory cell canals throughout life is disrupted and
CC microtubule organizing centers accumulate at the tips of excretory cell
CC canals, with a strong reduction along the canals, and the direction of
CC microtubule growth is altered. {ECO:0000269|PubMed:25771894}.
CC -!- SIMILARITY: Belongs to the formin homology family. {ECO:0000305}.
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DR EMBL; BX284603; CCD72047.2; -; Genomic_DNA.
DR RefSeq; NP_497334.2; NM_064933.3.
DR AlphaFoldDB; Q9TYU9; -.
DR SMR; Q9TYU9; -.
DR IntAct; Q9TYU9; 2.
DR STRING; 6239.F58B6.2; -.
DR EPD; Q9TYU9; -.
DR PaxDb; Q9TYU9; -.
DR PeptideAtlas; Q9TYU9; -.
DR EnsemblMetazoa; F58B6.2.1; F58B6.2.1; WBGene00019030.
DR GeneID; 175277; -.
DR KEGG; cel:CELE_F58B6.2; -.
DR UCSC; F58B6.2; c. elegans.
DR CTD; 175277; -.
DR WormBase; F58B6.2; CE46968; WBGene00019030; exc-6.
DR eggNOG; KOG1922; Eukaryota.
DR GeneTree; ENSGT00940000171596; -.
DR HOGENOM; CLU_016554_0_0_1; -.
DR InParanoid; Q9TYU9; -.
DR OMA; CNDLESY; -.
DR OrthoDB; 566415at2759; -.
DR PRO; PR:Q9TYU9; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00019030; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0031941; C:filamentous actin; IDA:UniProtKB.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0030041; P:actin filament polymerization; IBA:GO_Central.
DR GO; GO:0002064; P:epithelial cell development; IMP:WormBase.
DR GO; GO:0060562; P:epithelial tube morphogenesis; IMP:UniProtKB.
DR GO; GO:1904531; P:positive regulation of actin filament binding; IMP:UniProtKB.
DR GO; GO:0031113; P:regulation of microtubule polymerization; IMP:UniProtKB.
DR GO; GO:0035150; P:regulation of tube size; IMP:WormBase.
DR Gene3D; 1.20.58.2220; -; 1.
DR InterPro; IPR015425; FH2_Formin.
DR InterPro; IPR042201; FH2_Formin_sf.
DR Pfam; PF02181; FH2; 1.
DR SMART; SM00498; FH2; 1.
DR PROSITE; PS51444; FH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Cytoplasm; Cytoskeleton; Microtubule; Reference proteome.
FT CHAIN 1..843
FT /note="Excretory canal abnormal protein 6"
FT /evidence="ECO:0000305"
FT /id="PRO_0000433781"
FT DOMAIN 127..512
FT /note="FH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00774"
FT REGION 54..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..767
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 773..843
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 213
FT /note="I->A: Loss of actin binding and organization."
FT /evidence="ECO:0000269|PubMed:25771894"
FT MUTAGEN 360
FT /note="K->A: Loss of actin binding and organization."
FT /evidence="ECO:0000269|PubMed:25771894"
FT MUTAGEN 361
FT /note="G->E: In rh103; excretory canal tubulogenesis
FT defects including shortened canals with multiple lumens and
FT increased canal width."
FT /evidence="ECO:0000269|PubMed:25771894"
SQ SEQUENCE 843 AA; 94062 MW; 75D065713C12CA50 CRC64;
MTSDTIRQTL DELLLDKNGG SSNEARAFFL SQIIDQLKLI SSQTDAERQL QKLQLKDPND
NIVKATPPPP PPPPPLISIL QQAPPPPPPP PPPTLKAPPP PPILGLKTPS KSLKTPTPRP
KECPTSFLPK KEKKTKTRTV QWSKINASVV QDDSVWGKLA KASNVDIDFD LLDNFFGIES
LAVSGAAEVV KKSTRKDAHV ELLTAKRSQN VAIMLKQFKN IDELIDDVSQ NKPVAEIDAL
QNLFGMLPQS EEEEALRRYT GDISLLSPPS SFFYRLVQIQ FYRLRIETQI FLSDFSRLMR
ELAPNVEILI RTSQEILTSP TLPRLLLIFV NMGNYLNGNN SQGNAFGFTL NSLWKLIDLK
GNKQEFSLLH LLVTCEPDLV AHLQEELSTL KDASQISFDE IKISLKTLRD GRCKLEKQLE
TCSGASFTQF LELIKIDCKF ELDEFGANYD KLTELQYQLA DYFCENRNTF QLDECLKIFN
FLMNRLQQTL KEHVTRETRK LKKEEKKETQ TTRECEKTMK KPEKIDLFDA LTASNGGPES
PRKRAAGILD MRQKLGNVRI RKLRDVTTLE SSFTPPPPPP LESPTDSTSS KENESVKPAK
TSTNYEMCND LESYITSLTR KRASHLPKAP PKEEPKLPEV LPEKSKIALK IEKIPEKIDK
PPLPQAAPII PKLPQKSIKA PSTVTTRSKV PPPTAAAAVR IVSVTTTTTP TKTAELRKPG
ARSPKTTVAT VPKVTVVPVS RVPVAPSTPL SRRMSAPVVR KPTMTAEKKR EITMKPSVST
SARPSLINTS SHPMVRSPLP KMSVLEKPKP LRITRPTVIP QSPTVTSSAR PSGLRQPAKP
KWV
