ID A0A3P8PQD2_ASTCA Unreviewed; 946 AA.
AC A0A3P8PQD2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Connector enhancer of kinase suppressor of ras 2-like {ECO:0000313|Ensembl:ENSACLP00000019275.1};
GN Name=CNKSR2 {ECO:0000313|Ensembl:ENSACLP00000019275.1};
OS Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000019275.1, ECO:0000313|Proteomes:UP000265100};
RN [1] {ECO:0000313|Ensembl:ENSACLP00000019275.1, ECO:0000313|Proteomes:UP000265100}
RP NUCLEOTIDE SEQUENCE.
RA Datahose.;
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSACLP00000019275.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the CNKSR family.
CC {ECO:0000256|ARBA:ARBA00009498}.
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DR AlphaFoldDB; A0A3P8PQD2; -.
DR STRING; 8154.ENSACLP00000019275; -.
DR Ensembl; ENSACLT00000019720.1; ENSACLP00000019275.1; ENSACLG00000013090.1.
DR GeneTree; ENSGT00940000156709; -.
DR OMA; DQRETQN; -.
DR Proteomes; UP000265100; Chromosome 10.
DR Bgee; ENSACLG00000013090; Expressed in brain and 1 other cell type or tissue.
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;
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 REGION 851..871
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 946 AA; 107359 MW; D1E9FCD9D0A25357 CRC64;
MALVMEPVSK WSSSQVVDWM KGLDDCLQQY IKTFEKEKVG GEQLLRITHQ ELEDLGVSRI
GHQELILEAV DLLCALNYGL ETENLKTLSH KLNASAKNLQ NFITGRRRSG HYDGRATRKL
PNDFLTSVVD LIAAAKSLLA WLDRSPFAAV ADYSVTRNNV IQLCLELTTI VQQDCSVYET
ENKILNVCKT LSEVCDQIIS LSSDPMVSQS AHLEVVQLPN 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 EDKTSHEDFL
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 HEEFRSEPQE GSSNNGISPG PKTSSHRNSW HDQMESNTRM HYLQTFPMEE
SLLSQDRDQL AMEYRRQATL PAQRSLLQEQ YRALPLPLRA SIDSEAGGKP RSFTLPRDSG
LHAILAATAA SDQGEPQHYP LDRSRDAGHG RDCRMQTDSL VDLYRALEQT NLSDHRPANR
LEYKRSFVRR VNDPLLNDKL HRLRILHSSL NNVPLQDTNR SLGFLG
//
