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Database: UniProt
Entry: A0A9J8BX57_CYPCA
LinkDB: A0A9J8BX57_CYPCA
Original site: A0A9J8BX57_CYPCA 
ID   A0A9J8BX57_CYPCA        Unreviewed;       547 AA.
AC   A0A9J8BX57;
DT   28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2023, sequence version 1.
DT   18-JUN-2025, entry version 9.
DE   RecName: Full=Connector enhancer of kinase suppressor of ras 3-like {ECO:0008006|Google:ProtNLM};
OS   Cyprinus carpio carpio.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=630221 {ECO:0000313|Ensembl:ENSCCRP00000162479.1, ECO:0000313|Proteomes:UP001108240};
RN   [1] {ECO:0000313|Ensembl:ENSCCRP00000162479.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (MAR-2025) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the CNKSR family.
CC       {ECO:0000256|ARBA:ARBA00009498}.
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DR   Ensembl; ENSCCRT00000185087.1; ENSCCRP00000162479.1; ENSCCRG00000015664.2.
DR   GeneTree; ENSGT00940000163429; -.
DR   Proteomes; UP001108240; Unplaced.
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; cd06748; PDZ_CNK1_2_3-like; 1.
DR   FunFam; 2.30.42.10:FF:000060; Connector enhancer of kinase suppressor of Ras 2; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR010599; CNK2/3_dom.
DR   InterPro; IPR051566; CNKSR.
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   PANTHER; PTHR12844; CONNECTOR ENCHANCER OF KINASE SUPPRESSOR OF RAS; 1.
DR   PANTHER; PTHR12844:SF17; CONNECTOR ENHANCER OF KINASE SUPPRESSOR OF RAS 3; 1.
DR   Pfam; PF06663; CNK2_3_dom; 1.
DR   Pfam; PF10534; CRIC_ras_sig; 1.
DR   Pfam; PF00595; PDZ; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   PROSITE; PS51290; CRIC; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP001108240}.
FT   DOMAIN          21..75
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          83..177
FT                   /note="CRIC"
FT                   /evidence="ECO:0000259|PROSITE:PS51290"
FT   DOMAIN          214..296
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   REGION          301..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        316..332
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        412..424
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   547 AA;  61097 MW;  60D530B7D51F8CF2 CRC64;
     MMDPRTEAQH RRRAAGLDER WLDDSLQQYV PHFERKKISG EQLLKISHQD LEELTMTRVG
     HQELILEAVD LLCALNCGVE TDNLKTLVGQ MRAASNNLHN CASERRKNPT YDGGSPNKPP
     NVFLTAVVEL IGAAKGMLAW LDRSPLTGIS DFTSIKNKII QLCLELTTTV QKDCTVFEME
     EKILEVSSVL TGICDSTMRM TSDPLKSQMT CLEEVTITDI KAAEGMGIYI KSTYDGLHVI
     TGTTENSPAD RTQRIHAGDE VIQVNRQTVV GWQLKNLVEK LREDPQNVTL MVKKRPSGTC
     SFTPAPLKNM RWRPPVTQSP SYEPAAQSSR NPVQIKRPEK PAILDLYIPP PPSMPYSPRD
     AETREYAAVK MRPKGSESPN SSLDLASRRR SNISDYNSKP SVNPAEVAAP KARLRQRTPS
     RGKPRPMSMP VDTCLSVSDS PSRPWALGRK GDEILHRYLS NEQIPTISEE SPCYPLPYRP
     TGERQLVRGV DHIRGSQCFI NADLHSSATI PYQEAVARKP AAKSSKRRPS EASVFSSWIA
     RLKLLTH
//
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