ID S7N3P4_MYOBR Unreviewed; 1406 AA.
AC S7N3P4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE SubName: Full=Triple functional domain protein {ECO:0000313|EMBL:EPQ10655.1};
GN ORFNames=D623_10029799 {ECO:0000313|EMBL:EPQ10655.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ10655.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR EMBL; KE163046; EPQ10655.1; -; Genomic_DNA.
DR Proteomes; UP000052978; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11853; SH3_Kalirin_2; 1.
DR CDD; cd14113; STKc_Trio_C; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR047053; Kalirin_TRIO_SH3_2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF104; TRIPLE FUNCTIONAL DOMAIN PROTEIN; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF16609; SH3-RhoG_link; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000052978};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 272..448
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 460..574
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 858..923
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 992..1082
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1103..1357
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 728..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1406 AA; 154344 MW; D42AF8FF3D19A85F CRC64;
MPNGIKPVDP LDSLSPVGSA YRSSAQPGTC KYWILDLDSL SVSSNDASPP ASVASLQPHM
MGAQSSPGPK RPGNTLRKWL TSPVRRLSSG KADGHVKKLA HKHKKSREVR KSTDAGSQKD
SDDSAATPQD ETVEERGRNE GLSSGTLSKS SSSGMQSCGE EEGEEGADAV PLPPPMAIQQ
HSLLQPDSQD DKASSRLLVR PTSSETPSAA ELVSAIEELV KSKMALEDRP SSLLVDQGDS
SSPSFNPSDN SLLSSSSPID EMEERKSSSL KRRHYVLQEL VETERDYVRD LGYVVEGYMA
LMKEDGVPDD MKGKDKIVFG NIHQIYDWHR DFFLGELEKC LEDPEKLGSL FVKHERRLHM
YIVYCQNKPK SEHIVSEYID TFFEDLKQRL GHRLQLTDLL IKPVQRIMKY QLLLKDFLKY
SKKASLDTSE LERAVEVMCI VPKRCNDMMN VGRLQGFDGK IVAQGKLLLQ DTFLVTDQDA
GLLPRCRERR VFLFEQIVIF SEPLDKKKGF STPGFLFKNS IKVSCLCLEE SVENDPCKFA
LTSRTGDVVE TFVLHSSSPS VRQTWIHEIN QILENQRNFL NGTNKIPVAG RQDSFLAQKG
VRGARFHPLS LMSDLQHRGV HSRLLLVTKG LRSPQPVRHH SPVLVSSAAS SQAEADKMSG
MSTPGPSLPP PSSSLSLEAG PSQPGRLPPS GPSEGPEREA EQIPKMKVIE SPRKSAGSAA
GASQDGNAKE AKEARAHPED GRSRSSLGSL PLGKPRPGAI SPLNSPLATV FPSPLGKEPF
PPSSPLQKGG SFWSSIPASP ASRPGSFTFP GDSDSLQRQA HRHSAPGKDT DRMSTCSSAS
EQSVQSTQSN GSESSSSSNI STMLVTHDYT AVKEDEINVY QGEVVQILAS NQQNMFLVFR
AATDQCPAAE GWIPGFVLGH TSAVIMESPD GTLKKSTSWH TALRLRKKSE KKDKDGKREG
KLENGYRKSR EGLGNKVSVK LLSPNYIYDV PPEFVIPLSE VTCEAGETVV LRCRVCGRPK
ASITWKGPEH NTLNNDGHYS ISYSDLGEAS LKIVGVTTDD DGIYTCIAVN DMGSASCSAS
LRVLGPGSDG ILVTWKDNFD SFYSEVAELG RGRFSVVKKC DQKGTKQTVA TKFVNKKLMK
RDQVTHELGV LRNVQHPLLV GLLDTFETPT SYVLVLEMAD QGRLLDCVVR WGNLTEGKIR
AYLGEVLEAV RYLHNCRIAH LDLKPENILV GQSSATPTIK LADFGDAVQL NTTYYIHQLL
GNPEFAAPEI ILGNPVSLTS DTWSVGVLTY VLLSGVSPFL DDSVEETCLN ICRLDFSFPD
DYFKGVSQKA KDFVCFLLQE DPARRPSAAL ALQEQWLQAG HGHGKGTGVL DTSRLTSFIE
RRKHQNDVRP IRSVKNFLQS RLLPRV
//
