ID A0A7J8J6B4_MOLMO Unreviewed; 868 AA.
AC A0A7J8J6B4;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 02-APR-2025, entry version 11.
DE SubName: Full=Connector enhancer of kinase suppressor of Ras 2 {ECO:0000313|EMBL:KAF6491905.1};
GN ORFNames=HJG59_003071 {ECO:0000313|EMBL:KAF6491905.1};
OS Molossus molossus (Pallas' mastiff bat) (Vespertilio molossus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Molossidae;
OC Molossus.
OX NCBI_TaxID=27622 {ECO:0000313|EMBL:KAF6491905.1, ECO:0000313|Proteomes:UP000550707};
RN [1] {ECO:0000313|EMBL:KAF6491905.1, ECO:0000313|Proteomes:UP000550707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMolMol1 {ECO:0000313|EMBL:KAF6491905.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6491905.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
CC -!- SIMILARITY: Belongs to the CNKSR family.
CC {ECO:0000256|ARBA:ARBA00009498}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6491905.1}.
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DR EMBL; JACASF010000002; KAF6491905.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8J6B4; -.
DR Proteomes; UP000550707; Unassembled WGS sequence.
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; 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 Kinase {ECO:0000313|EMBL:KAF6491905.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000550707};
KW Transferase {ECO:0000313|EMBL:KAF6491905.1}.
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..297
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 540..639
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 454..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 831..868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..340
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..530
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..663
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..684
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..710
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 845..859
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 868 AA; 98325 MW; 9D9CE5A7BD63F8E6 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 TPTYENSLLR YMSSEKIAQE EYMFQRNSKK DTGKKSKKKG DKSNSPTHYS
LLPSLQMDTL RQDIMGTPVP ETTLYHTFQQ SSLQHKSKKK NKGPLAGKSK RRISCKDLGR
GDCEGWLWKK KDAKSYFSQK WKKYWFVLKD ASLYWYINEE DEKAEGFISL PEFKIDRASE
CRKKYAFKAC HPKIKSFYFA AEHLDDMNRW LNRINMLTAG YAERERIKQE QDYWSESDKE
EADTPSTPKQ DSPPPPYDTY PRPPSMSCAS PYVESKHSRL SSTETSQSQS SHEEFRQEVT
ESSAVSPIRK TASQRRSWQD LIETPLTSSG LHYLQTLPLE DSVFSDSAAM SPEHRRQSTL
PTQKCHLQDH YGPYPLAESE RMQVLNGNGG KPRSFTLPRD SGFNHCCLNA PVSACDPQDD
AQPTEVEEEE EEEEEEGEAA GENIGDKS
//
