CNKR2_RAT
ID CNKR2_RAT Reviewed; 1032 AA.
AC Q9Z1T4; Q9R093;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Connector enhancer of kinase suppressor of ras 2;
DE Short=Connector enhancer of KSR 2;
DE AltName: Full=CNK homolog protein 2;
DE Short=CNK2;
DE AltName: Full=Membrane-associated guanylate kinase-interacting protein;
DE Short=Maguin;
GN Name=Cnksr2;
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] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP INTERACTION WITH DLG4 AND AIP1.
RX PubMed=10207009; DOI=10.1074/jbc.274.17.11889;
RA Yao I., Hata Y., Ide N., Hirao K., Deguchi M., Nishioka H., Mizoguchi A.,
RA Takai Y.;
RT "MAGUIN, a novel neuronal membrane-associated guanylate kinase-interacting
RT protein.";
RL J. Biol. Chem. 274:11889-11896(1999).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-685; SER-687;
RP SER-756; SER-767 AND SER-906, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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: May function as an adapter protein or regulator of Ras
CC signaling pathways, in synaptic junctions.
CC -!- SUBUNIT: Interacts with RAF1, RAB2L and RAL GTPase proteins (By
CC similarity). Interacts with DLG4 and AIP1. {ECO:0000250,
CC ECO:0000269|PubMed:10207009}.
CC -!- INTERACTION:
CC Q9Z1T4; Q9Z1T4: Cnksr2; NbExp=2; IntAct=EBI-8548356, EBI-8548356;
CC Q9Z1T4; P31016: Dlg4; NbExp=4; IntAct=EBI-8548356, EBI-375655;
CC Q9Z1T4; P70587: Lrrc7; NbExp=3; IntAct=EBI-8548356, EBI-7798464;
CC Q9Z1T4; Q96NW7: LRRC7; Xeno; NbExp=2; IntAct=EBI-8548356, EBI-524275;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Maguin-1;
CC IsoId=Q9Z1T4-1; Sequence=Displayed;
CC Name=2; Synonyms=Maguin-2;
CC IsoId=Q9Z1T4-2; Sequence=VSP_010891, VSP_010892;
CC -!- TISSUE SPECIFICITY: Expressed in neurons and localized in the cell body
CC and neurites. {ECO:0000269|PubMed:10207009}.
CC -!- PTM: Phosphorylated on tyrosine. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CNKSR family. {ECO:0000305}.
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DR EMBL; AF102853; AAD04567.1; -; mRNA.
DR EMBL; AF102854; AAD04568.1; -; mRNA.
DR PIR; T18293; T18293.
DR RefSeq; NP_001106837.1; NM_001113366.1. [Q9Z1T4-1]
DR RefSeq; NP_067718.1; NM_021686.3. [Q9Z1T4-2]
DR AlphaFoldDB; Q9Z1T4; -.
DR SMR; Q9Z1T4; -.
DR BioGRID; 248765; 3.
DR IntAct; Q9Z1T4; 4.
DR MINT; Q9Z1T4; -.
DR STRING; 10116.ENSRNOP00000009802; -.
DR iPTMnet; Q9Z1T4; -.
DR PhosphoSitePlus; Q9Z1T4; -.
DR PaxDb; Q9Z1T4; -.
DR PRIDE; Q9Z1T4; -.
DR Ensembl; ENSRNOT00000009802; ENSRNOP00000009802; ENSRNOG00000007014. [Q9Z1T4-1]
DR Ensembl; ENSRNOT00000080512; ENSRNOP00000071915; ENSRNOG00000007014. [Q9Z1T4-2]
DR GeneID; 59322; -.
DR KEGG; rno:59322; -.
DR CTD; 22866; -.
DR RGD; 708454; Cnksr2.
DR eggNOG; KOG1738; Eukaryota.
DR GeneTree; ENSGT00940000156709; -.
DR InParanoid; Q9Z1T4; -.
DR OMA; EDMEMPP; -.
DR OrthoDB; 1121556at2759; -.
DR PhylomeDB; Q9Z1T4; -.
DR TreeFam; TF326495; -.
DR Reactome; R-RNO-5674135; MAP2K and MAPK activation.
DR PRO; PR:Q9Z1T4; -.
DR Proteomes; UP000002494; Chromosome X.
DR Bgee; ENSRNOG00000007014; Expressed in frontal cortex and 9 other tissues.
DR Genevisible; Q9Z1T4; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0099147; C:extrinsic component of postsynaptic density membrane; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0014069; C:postsynaptic density; IDA:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0035556; P:intracellular signal transduction; ISO:RGD.
DR GO; GO:0099173; P:postsynapse organization; IDA:SynGO.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.30.29.30; -; 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; 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; PF06663; DUF1170; 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 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1032
FT /note="Connector enhancer of kinase suppressor of ras 2"
FT /id="PRO_0000089972"
FT DOMAIN 11..76
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT DOMAIN 84..178
FT /note="CRIC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00621"
FT DOMAIN 215..297
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 332..515
FT /note="DUF1170"
FT DOMAIN 570..669
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 324..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 874..917
FT /evidence="ECO:0000255"
FT COMPBIAS 324..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 682..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..712
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 726..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..890
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YA9"
FT MOD_RES 338
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80YA9"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 683
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q80YA9"
FT MOD_RES 685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 906
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 896
FT /note="N -> S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10207009"
FT /id="VSP_010891"
FT VAR_SEQ 897..1032
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10207009"
FT /id="VSP_010892"
SQ SEQUENCE 1032 AA; 117390 MW; 02BD762461F8D7EC CRC64;
MALIMEPVSK WSPSQVVDWM KGLDDCLQQY IKNFEREKIS GDQLLRITHQ ELEDLGVSRI
GHQELILEAV DLLCALNYGL ETENLKTLSH KLNASAKNLQ NFITGRRRSG HYDGRTSRKL
PNDFLTSVVD LIGAAKSLLA WLDRSPFAAV TDYSVTRNNV IQLCLELTTI VQQDCTVYET
ENKILHVCKT LSGVCDHIIS LSSDPLVSQS AHLEVIQLAN IKPSEGLGMY IKSTYDGLHV
ITGTTENSPA DRCKKIHAGD EVIQVNHQTV VGWQLKNLVN ALREDPSGVI LTLKKRPQSM
LTSAPALLKN MRWKPLALQP LIPRSPTSSV ATPSSTISTP TKRDSSALQD LYIPPPPAEP
YIPRDEKGNL PCEDLRGHMV GKPVHKGSES PNSFLDQEYR KRFNIVEEDT VLYCYEYEKG
RSSSQGRRES TPTYGKLRPI SMPVEYNWVG DYEDPNKMKR DSRRENSLLR YMSNEKIAQE
EYMFQRNSKK DTGKKSKKKG DKSTSPTHYS LLPSLQMDAL RQDIMGTPVP ETTLYHTFQQ
SSLQHKSKKK NKGAIAGKSK RRISCKDLGR GDCEGWLWKK KDAKSYFSQK WKKYWFVLKD
ASLYWYINEE DEKAEGFISL PEFKIDRASE CRKKYAFKAC HPKIKSFYFA AEHLDDMNRW
LNRINMLTAG YAERERIKQE QDYWSESDKE EADTPSTPKQ DSPPPPYDTY PRPPSMSCAS
PYVEAKHSRL SSTETSQSQS SHEEFRQEVT GSSAVSPIRK TASQRRSWQD LIETPLTSSG
LHYLQTLPLE DSVFSDSAAI SPEHRRQSTL PTQKCHLQDH YGPYPLAESE RMQVLNGNGG
KPRSFTLPRD SGFNHCCLNA PVSACDPQDD IQPPEVEEEE EEEEEEAAGE NIGEKNENRE
EKLGDSLQDL YRALEEASLS PLGEHRISTK IEYKLSFIKR CNDPVMNEKL HRLRILKSTL
KAREGEVAII DKVLDNPDLT SKEFQQWKQM YLDLFLDICQ NTTSNDPLSI SSEVDVITSS
LTHTHSYIET HV
