ID A0A452F0W4_CAPHI Unreviewed; 850 AA.
AC A0A452F0W4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Connector enhancer of kinase suppressor of Ras 2 {ECO:0000313|Ensembl:ENSCHIP00000017947.1};
GN Name=CNKSR2 {ECO:0000313|Ensembl:ENSCHIP00000017947.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000017947.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000017947.1}
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; A0A452F0W4; -.
DR Ensembl; ENSCHIT00000025761.1; ENSCHIP00000017947.1; ENSCHIG00000017548.1.
DR GeneTree; ENSGT00940000156709; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR Bgee; ENSCHIG00000017548; Expressed in cerebellum and 12 other cell types or tissues.
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; PF00169; PH; 1.
DR Pfam; PF00536; SAM_1; 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:UP000291000}.
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..270
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 521..620
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 273..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 813..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..509
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..647
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..663
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..842
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 850 AA; 96456 MW; 7A7B9E02CB63A545 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 PLIPRSPTSS VATPSSTIST PTKRDSSALQ
DLYIPPPPAE PYIPRDEKGN LPCEDLRGHM VGKPVHKGSE SPNSFLDQEY RKRFNIVEED
TVLYCYEYEK GRSSSQGRRE STPTYGKLRP ISMPVEYNWV GDYEDPNKMK RDSRRENSLL
RYMSNEKIAQ EEYMFQRNSK KDTGKKSKKK GDKSSSPTHY SLLPSLQMDA LRQDIMGTPV
PEATLYHTFQ QSSLQHKSKK KNKGPIAGKS KRRISCKDLG RGDCEGWLWK KKDAKSYFSQ
KWKKYWFVLK DASLYWYINE EDEKAEGFIS LPEFKIDRAS ECRKKYAFKA CHPKIKSFYF
AAEHLDDMNR WLNRINMLTA GYAERERIKQ EQDYWSESDK EEADTPSTPK QDSPPPPYDT
YPRPPSMSCA SPYVEAKHSR LSSTETSQSQ SSHEEFRQEV TGSSVVSPIR KTASQRRSWQ
DLIETPLTSS GLHYLQTLPL EDSVFSDSAA ISPEHRRQST LPTQKCHLQD HYGPYPLAES
ERMQVLNGNG GKPRSFTLPR DSGFNHCCLN APVSACDPQD DVQPTEVEEE EEEEEEEEGE
AAGENIGDKS
//
