ID A0A9J7N1I5_BRAFL Unreviewed; 1615 AA.
AC A0A9J7N1I5;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 18-JUN-2025, entry version 12.
DE SubName: Full=Uncharacterized protein LOC118423066 isoform X3 {ECO:0000313|RefSeq:XP_035686870.1};
GN Name=LOC118423066 {ECO:0000313|RefSeq:XP_035686870.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739 {ECO:0000313|Proteomes:UP000001554, ECO:0000313|RefSeq:XP_035686870.1};
RN [1] {ECO:0000313|Proteomes:UP000001554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|Proteomes:UP000001554};
RX PubMed=32313176;
RA Simakov O., Marletaz F., Yue J.X., O'Connell B., Jenkins J., Brandt A.,
RA Calef R., Tung C.H., Huang T.K., Schmutz J., Satoh N., Yu J.K.,
RA Putnam N.H., Green R.E., Rokhsar D.S.;
RT "Deeply conserved synteny resolves early events in vertebrate evolution.";
RL Nat. Ecol. Evol. 0:0-0(2020).
RN [2] {ECO:0000313|RefSeq:XP_035686870.1}
RP IDENTIFICATION.
RC STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035686870.1};
RC TISSUE=Testes {ECO:0000313|RefSeq:XP_035686870.1};
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_035686870.1; XM_035830977.1.
DR GeneID; 118423066; -.
DR Proteomes; UP000001554; Chromosome 9.
DR CDD; cd06748; PDZ_CNK1_2_3-like; 1.
DR CDD; cd09511; SAM_CNK1_2_3-suppressor; 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; 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:SF42; CONNECTOR ENHANCER OF KSR PROTEIN CNK; 1.
DR Pfam; PF10534; CRIC_ras_sig; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF07647; SAM_2; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000001554}.
FT DOMAIN 11..76
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 93..182
FT /note="CRIC"
FT /evidence="ECO:0000259|PROSITE:PS51290"
FT DOMAIN 220..302
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1148..1249
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT REGION 297..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..755
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 853..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1510..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1474..1501
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 305..331
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..450
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..501
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..603
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..681
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..730
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 994..1017
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1048
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1332
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1369..1379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1398..1407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1413..1430
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1511..1533
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1540..1551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1615 AA; 181224 MW; 4B07A3BBC53054EC CRC64;
MANSMESVGS WTPKQVGLWL KGLDDAVQPY IQSFILAGVT GEQLLNLSHR DMDRLNITKL
GHQELILEAV DLLCALNFGL ENETLQSLTV ALGLNVENLD MAMTVRNQQS ILVGLAGPRD
NYKLPPDILR AICDVLSAAK AVVSWLDRTP FVQMMNYIAI RNRIVRICLG FTSSIHKDPN
KRDAEETVVP LCKELAMLSQ SLQLSVKDDP QVCSAARVEV ITLTNVDHKL GLGMFIQSSF
NGTHYVTGTK EGSPAYTCKR IHPGDEILQV NYQTVVGWKL KKLVDALKED PHGVVITFKK
RPKTSRSSGT PSRPSSGSSS RLSQNSRHSS GNHIRGRSLD SASPANSVGR VPPSPLVELY
LPPPPPEPYK PRQNFFDRVR TPTSNITQSQ VQVHQPLWED EDMSPPPPQP LSDRSQSVHI
PTHRQDQQAT WDDDERSPPS SRPLSGRSQS VHFPSHGQRT YWDGDEERFS PTDAPPFSSR
AQSFNQPRGQ QWELTQRDFS QPQPPVTMAE QSMYSSPPQN QWIPFPENVS HDVETPAQAS
RYESIDVQHW ESEGEVPPEE PVPAYMPRGG HRRSKREDSE EEGASIDSVS TVVTRSPVSP
ASPQWEEGEG LSPTRPLPLG ARSPNYLLDR QSKYRRSATF SEGTENHDPS FRLAQETRET
LREAMLRARQ NRKDRPRERP KSLPPDTGMQ GFRAGGEREE RREVSNQRLS DHVRMEVETI
SEASTSAESS PQRSVPPRPL SQPDSAPRPL SADREVIVID KQNAIKDFVP SNLRKLTGDM
SSMPAFRVER ETRPRGKNAS RGPPPPYERS RMDGRHSFKS VPEVSKLPMD EVARRTRPLT
EQFSAKLAIF EGGSESNVMK RPQRKHFAER VSELQEAVKS PAKDESKEEE EESNFQRGVV
GKAETDDSTI RTTRYVHRIS LRFKKDKDKS ESAGANPEGA SPQAADSEPA NVLPVSVQPS
KQSFRKESPE VANLDDIQSR FAPSPIVPPP NQERLVREKT KQFTRRMDPV ESARIVEQEP
SYSGSPNKEV KYDTPPFPDQ RDSVREARTN PTVQKQEVLP KSPTSAPGSY SVKIVGGVPV
RIGSTSHVQQ NMNTAKNPFC SCLSPSYSRV SFQMPPPDQS SVRLRSKNKV TGTQKYSRRR
MSCKDLGNGD CEGWLWKKKD QRKIFGQKWK KLWFVLKKFS LYYYAGQDAL KAEGIINLPE
YSVVYATDTE CGRKFGIKAS HMEIKTFFFA TDSKEDRDRW LNKLQLASIQ YDRQSIHDPE
LNILELAKQC PAIVEGFGYY SESDEESEPP SPNPVSPTRQ SPSPPRKRKE SSPERPVFDD
TPVVSPVATA PVGNSMKRSR EKPRKPSYLA AFDMNGTKKS PPSERKSPSN PPRPPYDPPR
PPHDPPRPPS NPPVEQWGQL STTSSDSECT HVTPISSTSS SSSTASSPML LLPPPPQFGS
TDELKNLYRQ SWNVLQEEKM MKMLELGQGN LSEKQEKKLK LQKLTRVLKD KEGNLEAIDR
LLKSPQLTSR EVQDWKDQNQ HILEDVEKHK DGADPPQRPP STSSRHNSQS GPVPKPRTSI
HRNSQGPIEE MTQRLSITKR PLSTDLDRIE SDAGIKPPLP EIDDDEDDSY SSTSL
//
