CNKR3_RAT
ID CNKR3_RAT Reviewed; 555 AA.
AC Q5SGD7; Q6VPP2;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Connector enhancer of kinase suppressor of ras 3;
DE Short=Connector enhancer of KSR 3;
DE AltName: Full=CNK homolog protein 3;
DE Short=CNK3;
DE AltName: Full=Maguin-like protein;
DE AltName: Full=Parturition-related protein 4;
GN Name=Cnksr3; Synonyms=Prp4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Brown Norway;
RA Tzolovsky G.I., McGurk L., Pathirana S., Slee R., Hillier S., Clinton M.,
RA Bownes M.;
RT "Cloning, expression and comparison of human, rat and mouse ML (maguin-
RT like) genes, and expression in mouse oogenesis.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 285-555.
RC TISSUE=Uterus;
RA Song J., Huang Z., Yue Z., Myatt L., Ma R.Z.;
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Involved in transepithelial sodium transport. Regulates
CC aldosterone-induced and epithelial sodium channel (ENaC)-mediated
CC sodium transport through regulation of ENaC cell surface expression.
CC Acts as a scaffold protein coordinating the assembly of an ENaC-
CC regulatory complex (ERC). {ECO:0000250|UniProtKB:Q6P9H4}.
CC -!- SUBUNIT: Interacts with epithelial sodium channel ENaC. Interacts
CC directly with SCNN1A (ENaC subunit alpha) and SCNN1B (ENaC subunit
CC beta) C-terminal tails. Interacts with ENaC regulatory proteins NEDD4L,
CC RAF1 and SGK1. {ECO:0000250|UniProtKB:Q6P9H4}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6P9H4}. Apical
CC cell membrane {ECO:0000250|UniProtKB:Q6P9H4}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:Q6P9H4}.
CC -!- DOMAIN: The PDZ domain is required for interaction with ENaC and SGK1,
CC but not for interaction with NEDDL4 and RAF1.
CC {ECO:0000250|UniProtKB:Q6P9H4}.
CC -!- SIMILARITY: Belongs to the CNKSR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR01114.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY328890; AAQ92305.1; -; mRNA.
DR EMBL; AY333962; AAR01114.1; ALT_INIT; mRNA.
DR RefSeq; NP_001012061.1; NM_001012061.1.
DR AlphaFoldDB; Q5SGD7; -.
DR SMR; Q5SGD7; -.
DR BioGRID; 258906; 1.
DR STRING; 10116.ENSRNOP00000024418; -.
DR iPTMnet; Q5SGD7; -.
DR PhosphoSitePlus; Q5SGD7; -.
DR PaxDb; Q5SGD7; -.
DR PRIDE; Q5SGD7; -.
DR Ensembl; ENSRNOT00000082931; ENSRNOP00000070619; ENSRNOG00000018052.
DR GeneID; 308113; -.
DR KEGG; rno:308113; -.
DR UCSC; RGD:1307544; rat.
DR CTD; 154043; -.
DR RGD; 1307544; Cnksr3.
DR eggNOG; KOG1738; Eukaryota.
DR GeneTree; ENSGT00940000154428; -.
DR InParanoid; Q5SGD7; -.
DR OMA; PNSFLDH; -.
DR OrthoDB; 1121556at2759; -.
DR PhylomeDB; Q5SGD7; -.
DR TreeFam; TF326495; -.
DR PRO; PR:Q5SGD7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018052; Expressed in cerebellum and 19 other tissues.
DR ExpressionAtlas; Q5SGD7; baseline and differential.
DR Genevisible; Q5SGD7; RN.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0120025; C:plasma membrane bounded cell projection; IEA:UniProt.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProt.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
DR GO; GO:2000651; P:positive regulation of sodium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0010765; P:positive regulation of sodium ion transport; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IEA:UniProt.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR010599; CNK2/3_dom.
DR InterPro; IPR017874; CRIC_domain.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR Pfam; PF10534; CRIC_ras_sig; 1.
DR Pfam; PF06663; DUF1170; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00228; PDZ; 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; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..555
FT /note="Connector enhancer of kinase suppressor of ras 3"
FT /id="PRO_0000311107"
FT DOMAIN 7..72
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 80..174
FT /note="CRIC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00621"
FT DOMAIN 211..293
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 325..546
FT /note="DUF1170"
FT REGION 308..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..391
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMA3"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CONFLICT 358
FT /note="D -> Y (in Ref. 2; AAR01114)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="K -> KG (in Ref. 2; AAR01114)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 61851 MW; 9427AEB3FF48626D CRC64;
MEPVTKWSPK QVVDWTRGLD DCLQPYVHKF EREKIDGEQL LKISHQDLEE LGVTRIGHQE
LVLEAVDLLC ALNYGLETDN MKNLVLKLRA SSHNLQNYIS SRRKSPAYDG NTSRKPPNEF
LTSVVELIGA AKALLAWLDR APFTGITDLS VTKNKIIQLC LDLTTAVQKD CLVAEMEDKV
LNVVKVLNGI CDKMMHSTTD PVMSQCACLE EVHLPNVRPG EGLGMYIKST YDGLHVITGT
TENSPADRSQ KIHAGDEVIQ VNRQTVVGWQ LKNLVKKLRE NPTGVVLLLK KRPTGSFSFT
PAPLKNLRWK PPLVQTSPPP TTTQSPESTM DASLKKEKPA ILDLYIPPPP AVPYSPRDEN
VSFSYRGHTK SKQPLPGRKG SESPNSFLDQ ESQRRRFTIT DSDQLPGYSV GTNILPIKMR
GKTPSYGKPR PLSMPADGNW MGIVDPFAKP RGHGRKGEDA LCRYFSNERI TPIIEESASP
VYRFSRPLTE RHLVRGADYI RGSRCYINSD LHSSATIPFQ EEGPKKKSAS SSAKASSGEP
SLLVSWLTRL KLLTH
