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Database: UniProt
Entry: I3J913_ORENI
LinkDB: I3J913_ORENI
Original site: I3J913_ORENI 
ID   I3J913_ORENI            Unreviewed;       950 AA.
AC   I3J913;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 2.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Connector enhancer of kinase suppressor of ras 2 {ECO:0000313|Ensembl:ENSONIP00000005353.2};
GN   Name=CNKSR2 {ECO:0000313|Ensembl:ENSONIP00000005353.2};
OS   Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX   NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000005353.2, ECO:0000313|Proteomes:UP000005207};
RN   [1] {ECO:0000313|Proteomes:UP000005207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Broad Institute Genome Assembly Team;
RG   Broad Institute Sequencing Platform;
RA   Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSONIP00000005353.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the CNKSR family.
CC       {ECO:0000256|ARBA:ARBA00009498}.
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DR   AlphaFoldDB; I3J913; -.
DR   STRING; 8128.ENSONIP00000065634; -.
DR   Ensembl; ENSONIT00000005357.2; ENSONIP00000005353.2; ENSONIG00000004252.2.
DR   eggNOG; KOG1738; Eukaryota.
DR   GeneTree; ENSGT00940000156709; -.
DR   HOGENOM; CLU_013414_0_0_1; -.
DR   TreeFam; TF326495; -.
DR   Proteomes; UP000005207; Linkage group LG10.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd01260; PH_CNK_mammalian-like; 1.
DR   CDD; cd09511; SAM_CNK1_2_3-suppressor; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR049628; CNK1-3_SAM.
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   PANTHER; PTHR12844; CONNECTOR ENCHANCER OF KINASE SUPPRESSOR OF RAS; 1.
DR   PANTHER; PTHR12844:SF21; CONNECTOR ENHANCER OF KINASE SUPPRESSOR OF RAS 2; 1.
DR   Pfam; PF06663; CNK2_3_dom; 1.
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; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS51290; CRIC; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005207}.
FT   DOMAIN          11..76
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          84..178
FT                   /note="CRIC"
FT                   /evidence="ECO:0000259|PROSITE:PS51290"
FT   DOMAIN          215..297
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          561..660
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          324..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        324..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..380
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        667..688
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        739..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   950 AA;  107915 MW;  3145133B5907EE5E CRC64;
     MALVMEPVSK WSSSQVVDWM KGLDDCLQQY IKTFEKEKVG GEQLLRITHQ ELEDLGVSRI
     GHQELILEAV DLLCALNYGL ETENLKTLSH KLNASAKNLQ NFITGRRRSG HYDGRATRKL
     PNDFLTSVVD LIAAAKSLLA WLDRSPFAAV ADYSVTRNNV IQLCLELTTI VQQDCSVYET
     ENKILNVCKT LSEVCDQIIS LSSDPMVSQS AHLEVVQLAN IKSTEGLGMY IKSTYDGLHV
     ITGTTEGSLA DRCKKIHAGD EVIQVNHQTV VGWQLKNLVN LLRGDPAGVT LTLKKRPQST
     LTSTPALLKN MRWKPLALQP IFPQSPSSSV ATPTSTLSTP SRRSSCALQD LYIPPPPAEP
     YTPRDDKGSL PDDDPQSDVH VAEGSESPNS YLDQECRRRF PLVEEDTILY CYEYDQNQEG
     ASVRRGSTPT YGRLRPISMP VEYNWVGDNE DLAKLKRESR RENSLMHFES EDKTSREDFL
     LGRSLSQNRR KTERGASPTH YTLVPALQME VSRSTSSSDS ASLYHVFERS SLLSRSKKKG
     KAGSPLTSIS KRRISCRDLG QGDCQGWLWK KKDAKTYFSQ KWKKYWFILK DTCLYWYMNE
     EDEKAEGFVS LPEFKIDRAT ECRRKFAFKA CHPKIKTFYF AAENVDDMSR WLSRLSMAVA
     GYSEQQEKMR QDQDYWSESD HEDMEMPSMS KQDSPPPPYD TYPRASSVSP YLEPKRGHLS
     SSDTFQSRSS HEEFRPESQE GSSNNGISPG PKTSSHRNSW HDQMESNTRM HYLQTFPMEE
     SLLSEDRDQL AMEYRRQATL PAQRSLLQEQ YRALPLPLRA SIDSEAGGKP RSFTLPRDSG
     LHAILAATAA SDQGEPHAVH ECWQQGAVHE NRRQMGMQTD SLVDLYRALE QTNLSDHRPA
     NRLEYKRSFV RRVNDPLLND KLHRLRILHS SLNSLTHPHT LMHTSSTVYF
//
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