ID A0A3Q0CX71_MESAU Unreviewed; 953 AA.
AC A0A3Q0CX71;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 18-JUN-2025, entry version 27.
DE RecName: Full=Connector enhancer of kinase suppressor of ras 2 {ECO:0000256|ARBA:ARBA00074798};
DE AltName: Full=CNK homolog protein 2 {ECO:0000256|ARBA:ARBA00082233};
GN Name=Cnksr2 {ECO:0000313|RefSeq:XP_021085268.1};
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_021085268.1};
RN [1] {ECO:0000313|RefSeq:XP_021085268.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- SIMILARITY: Belongs to the CNKSR family.
CC {ECO:0000256|ARBA:ARBA00009498}.
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DR RefSeq; XP_021085268.1; XM_021229609.1.
DR AlphaFoldDB; A0A3Q0CX71; -.
DR GeneID; 101832800; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR CDD; cd06748; PDZ_CNK1_2_3-like; 1.
DR CDD; cd01260; PH_CNK_mammalian-like; 1.
DR CDD; cd09511; SAM_CNK1_2_3-suppressor; 1.
DR FunFam; 1.10.150.50:FF:000019; Connector enhancer of kinase suppressor of Ras 2; 1.
DR FunFam; 2.30.29.30:FF:000092; Connector enhancer of kinase suppressor of Ras 2; 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; 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; IPR051566; CNKSR.
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 Kinase {ECO:0000313|RefSeq:XP_021085268.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW Transferase {ECO:0000313|RefSeq:XP_021085268.1}.
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 491..590
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 402..431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..291
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..614
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..635
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..661
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..808
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..824
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 108241 MW; 0BD5CBA5DC2D9185 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 STPTYENSLL RYMSNEKIAQ EEYMFQRNSK KDTGKKSKKK
GDKSNSPTHY SLLPSLQMDA LRQDIMGTPV PETTLYHTFQ QSSLQHKSKK KNKGAIAGKS
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 DIQPPEVEEE EEEEEGEAAG ENLGEKSENQ EEKLGDSLQD LYRALEEASL
SPIGEHRIST KMEYKLSFMK RCNDPVMNEK LHRLRILRST LKAREGEVAI IDKVLDNPDL
TSKEFQQWKQ MYLDLFLDIC QNTTSNDPLS ISSEVDVITS SLTHTHSYIE THV
//
