ID G3SZY2_LOXAF Unreviewed; 1034 AA.
AC G3SZY2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Connector enhancer of kinase suppressor of Ras 2 {ECO:0000313|Ensembl:ENSLAFP00000006229.3};
GN Name=CNKSR2 {ECO:0000313|Ensembl:ENSLAFP00000006229.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000006229.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000006229.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000006229.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000006229.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000006229.3};
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 RefSeq; XP_003416001.1; XM_003415953.2.
DR AlphaFoldDB; G3SZY2; -.
DR STRING; 9785.ENSLAFP00000006229; -.
DR Ensembl; ENSLAFT00000007403.3; ENSLAFP00000006229.3; ENSLAFG00000007401.3.
DR GeneID; 100656707; -.
DR KEGG; lav:100656707; -.
DR CTD; 22866; -.
DR eggNOG; KOG1738; Eukaryota.
DR GeneTree; ENSGT00940000156709; -.
DR HOGENOM; CLU_013414_0_0_1; -.
DR InParanoid; G3SZY2; -.
DR OMA; DQRETQN; -.
DR OrthoDB; 5406576at2759; -.
DR TreeFam; TF326495; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:Ensembl.
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:UP000007646}.
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 570..669
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
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 539..559
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 861..905
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 543..559
FT /note="Basic 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 COMPBIAS 891..905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1034 AA; 117494 MW; 4775136031F6ADA5 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 SKGPIAGKSK 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 SGFNHCCPNA PVSACDPQDD VQPTEVEEEE EEEEEEGEAA GENVGEKSES
REEKLGDSLQ DLYRALEQAS LSPLGEHRIS TKLEYKLSFI KRCNDPVMNE KLHRLRILKS
TLKAREGEVA IIDKVLDNPD LTSKEFQQWK QMYLDLFLDI CQTTTSNDPL NISSEVDVIT
SSLTHTHSYI ETHV
//
