CNKR_CAEEL
ID CNKR_CAEEL Reviewed; 801 AA.
AC G5EEW9;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Connector enhancer of kinase suppressor of ras {ECO:0000250|UniProtKB:Q8WXI2};
DE Short=CNK-1 {ECO:0000312|EMBL:AAZ08414.1};
DE Short=Connector enhancer of KSR {ECO:0000250|UniProtKB:Q8WXI2};
GN Name=cnk-1 {ECO:0000312|EMBL:CAA83466.3, ECO:0000312|WormBase:R01H10.8};
GN ORFNames=R01H10.8;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAZ08414.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16085714; DOI=10.1073/pnas.0500937102;
RA Rocheleau C.E., Ronnlund A., Tuck S., Sundaram M.V.;
RT "Caenorhabditis elegans CNK-1 promotes Raf activation but is not essential
RT for Ras/Raf signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11757-11762(2005).
RN [2] {ECO:0000312|EMBL:CAA83466.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|EMBL:CAA83466.3};
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).
CC -!- FUNCTION: Non-essential component of the Ras signaling pathway.
CC {ECO:0000269|PubMed:16085714}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WXI2}.
CC Membrane {ECO:0000250|UniProtKB:Q8WXI2}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8WXI2}.
CC -!- DISRUPTION PHENOTYPE: No apparent phenotype. Double mutant cnk-1 and
CC lin-45 and double mutant cnk-1 and ksr-1 show high lethality in the
CC first larval stage, filling with fluid and with a rod-like appearance
CC due to loss of the excretory duct. Double mutant cnk-1 and lin-45 also
CC shows P12 to P11 cell fate transformations.
CC {ECO:0000269|PubMed:16085714}.
CC -!- SIMILARITY: Belongs to the CNKSR family. {ECO:0000255}.
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DR EMBL; DQ104391; AAZ08414.1; -; mRNA.
DR EMBL; Z31590; CAA83466.3; -; Genomic_DNA.
DR EMBL; Z36282; CAA83466.3; JOINED; Genomic_DNA.
DR PIR; S43566; S43566.
DR RefSeq; NP_499274.3; NM_066873.5.
DR AlphaFoldDB; G5EEW9; -.
DR SMR; G5EEW9; -.
DR IntAct; G5EEW9; 3.
DR STRING; 6239.R01H10.8; -.
DR EPD; G5EEW9; -.
DR PaxDb; G5EEW9; -.
DR PeptideAtlas; G5EEW9; -.
DR EnsemblMetazoa; R01H10.8.1; R01H10.8.1; WBGene00000564.
DR GeneID; 187518; -.
DR KEGG; cel:CELE_R01H10.8; -.
DR CTD; 187518; -.
DR WormBase; R01H10.8; CE38855; WBGene00000564; cnk-1.
DR eggNOG; KOG1738; Eukaryota.
DR GeneTree; ENSGT00940000169895; -.
DR HOGENOM; CLU_351339_0_0_1; -.
DR InParanoid; G5EEW9; -.
DR OMA; CTKIDAG; -.
DR OrthoDB; 323704at2759; -.
DR Reactome; R-CEL-5674135; MAP2K and MAPK activation.
DR SignaLink; G5EEW9; -.
DR PRO; PR:G5EEW9; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00000564; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR017874; CRIC_domain.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF10534; CRIC_ras_sig; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS51290; CRIC; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Membrane; Reference proteome.
FT CHAIN 1..801
FT /note="Connector enhancer of kinase suppressor of ras"
FT /id="PRO_0000424172"
FT DOMAIN 56..121
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 129..225
FT /note="CRIC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00621"
FT DOMAIN 262..344
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 632..736
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 351..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..790
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 801 AA; 90136 MW; A45797326186E614 CRC64;
MFSTTMGFPS TPLEAKQALG ISSGISSVSS GLRSGSPMLS ASYEPQLSFA RCVEQWKGKE
IARWIEGLGD QMNPYLGMIR DNIKSGKQLE ALDDDSLKKI GISALGARKT IFQAVSLLLY
FCHESEHENL QRLAQQVKTS CLYVERTMTS AMRMREKAIR RSEIVNILNS VSNAVLQLAE
HTKRFVFWLD RTPFDEEPEF INVRNSVSSF MWNLLRNVNV QPKALFETGS QIVRMSKELA
YECQKIVDCD DPLILYACFI ESALLRRRSD NINWGLNIQS SYRGVHVISE IKEGSPADAC
TKIDAGDEIL MINGRTVVGW DLTSVVQQVG ALDVLELSLI VKRRPREPQL PKQSKLAARA
LAPSSQTAKT YSTDDYDPFG QSEPLKRHRS CHVISEIIKE NERKIRISRR LIRRSSIASA
CPRKERKNID ERALDGDDED DWDVHEFIRN VDGEEEALVP RIAKRTRTMR HQPDGYVRSF
IDNKLVTDIE DDVVNDQLTF NVKCPNEFAQ IKEVDKEELK VLNLPEARVS DEDWKAPYQE
FAAPSFRAVG DSNISGFSLD SPRLLPVSSR MTSSVEESAF GVLPSPSTSS MNSVSSPAPF
GKFQMSTSQT EWSPNPDDLP GSPISAAYAG MEKLFEGWVR RRKTRAELNA NELTNKWPKI
WMCLRGHYLL LYTNQNTKRP EMVINLIKAT ISDSTDLKTS KKNIFRITAA PLDYHFSCFT
ALDWRNWTQK MKMAKEIFAN AGTQPRIMSQ SVSSYNNDLS DQNFFLGQQT GSGLSTLPRV
TTNGMTTSKS GGLGGGGFKQ K
