ID A0A671ERP1_RHIFE Unreviewed; 2976 AA.
AC A0A671ERP1;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=KALRN {ECO:0000313|Ensembl:ENSRFEP00010015921.1};
OS Rhinolophus ferrumequinum (Greater horseshoe bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Rhinolophidae;
OC Rhinolophinae; Rhinolophus.
OX NCBI_TaxID=59479 {ECO:0000313|Ensembl:ENSRFEP00010015921.1, ECO:0000313|Proteomes:UP000472240};
RN [1] {ECO:0000313|Ensembl:ENSRFEP00010015921.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=25689317; DOI=10.1146/annurev-animal-090414-014900;
RA Koepfli K.P., Paten B., O'Brien S.J., Koepfli K.P., Paten B., Antunes A.,
RA Belov K., Bustamante C., Castoe T.A., Clawson H., Crawford A.J.,
RA Diekhans M., Distel D., Durbin R., Earl D., Fujita M.K., Gamble T.,
RA Georges A., Gemmell N., Gilbert M.T., Graves J.M., Green R.E., Hickey G.,
RA Jarvis E.D., Johnson W., Komissarov A., Korf I., Kuhn R., Larkin D.M.,
RA Lewin H., Lopez J.V., Ma J., Marques-Bonet T., Miller W., Murphy R.,
RA Pevzner P., Shapiro B., Steiner C., Tamazian G., Venkatesh B., Wang J.,
RA Wayne R., Wiley E., Yang H., Zhang G., Haussler D., Ryder O., O'Brien S.J.;
RT "The Genome 10K Project: a way forward.";
RL Annu Rev Anim Biosci 3:57-111(2015).
RN [2] {ECO:0000313|Ensembl:ENSRFEP00010015921.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=29166127; DOI=10.1146/annurev-animal-022516-022811;
RA Teeling E.C., Vernes S.C., Davalos L.M., Ray D.A., Gilbert M.T.P.,
RA Myers E.;
RT "Bat Biology, Genomes, and the Bat1K Project: To Generate Chromosome-Level
RT Genomes for All Living Bat Species.";
RL Annu Rev Anim Biosci 6:23-46(2018).
RN [3] {ECO:0000313|Ensembl:ENSRFEP00010015921.1, ECO:0000313|Proteomes:UP000472240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Teeling E., Myers G., Vernes S., Pippel M., Winkler S., Fedrigo O.,
RA Rhie A., Koren S., Phillippy A., Lewin H., Damas J., Howe K.,
RA Mountcastle J., Jarvis E.D.;
RT "G10K-VGP greater horseshoe bat female genome, primary haplotype.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|Ensembl:ENSRFEP00010015921.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR Ensembl; ENSRFET00010017383.1; ENSRFEP00010015921.1; ENSRFEG00010010836.1.
DR GeneTree; ENSGT00940000155248; -.
DR InParanoid; A0A671ERP1; -.
DR OMA; AKXFIMA; -.
DR Proteomes; UP000472240; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd11852; SH3_Kalirin_1; 1.
DR CDD; cd11853; SH3_Kalirin_2; 1.
DR CDD; cd00176; SPEC; 4.
DR CDD; cd14115; STKc_Kalirin_C; 1.
DR Gene3D; 1.20.58.60; -; 5.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR028570; Kalirin_TRIO_SH3_1.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF49; KALIRIN; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF00435; Spectrin; 4.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00326; SH3; 2.
DR SMART; SM00150; SPEC; 7.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 2.
DR SUPFAM; SSF46966; Spectrin repeat; 6.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS50002; SH3; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472240};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 37..182
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1270..1445
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1457..1569
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1635..1700
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1918..2093
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2105..2215
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2309..2374
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2461..2554
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2561..2655
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2674..2928
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1583..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1739..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2232..2296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2402..2441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 908..935
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1606..1631
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1793
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1802..1826
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2275..2289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2402..2424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2703
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2976 AA; 338261 MW; BF8486933095FBA7 CRC64;
MNPPEGAAEE GGAADSDVDA FFRTGSFRND GLKASDVLPI LKEKVAFVSG GRDKRGGPIL
TFPARSNHDR IRQEDLRKLV TYLASVPSED VCKRGFTVII DMRGSKWDLI KPLLKTLQEA
FPAEIHVALI IKPDNFWQKQ KTNFGSSKFI FETSMVSVEG LTKLVDPSQL TEEFDGSLDY
NHEEWIELRL SLEEFFNSAV HLLSRLEDLQ EMLARKEFPV DVEGSRRLIE EHTQLKKKVL
KAPVEELDRE GQRLLQCIRC SDGFSGRNCI PGSADFQSLV PKITSLLDKL HSTRQHLHQM
WHVRKLKLDQ CFQLRLFEQD AEKMFDWISH NKELFLQSHT EIGVSYQHAL DLQTQHNHFA
MNSMNAYVNI NRIMSVASRL SEAGHYASQQ IKQISTQLDQ EWKSFAAALD ERSTILAMSA
VFHQKAEQFL SGVDAWCKMC SEGGLPSEMQ DLELAIHHHQ SLYEQVTQAY TEVSQDGKAL
LDVLQRPLSP GNSESLTATA NYSKAVHQVL DVVHEVLHHQ RRLESIWQHR KVRLHQRLQL
CVFQQDVQQV LDWIENHGEA FLSKHTGVGK SLHRARALQK RHDDFEEVAQ NTYTNADKLL
EAAEQLAQTG ECDPEEIYKA ARHLEVRIQD FVRRVEQRKL LLDMSVSFHT HTKELWTWME
DLQKEMLEDV CADSVDAVQE LIKQFQQQQT ATLDATLNVI KEGEDLIQQL RDSAVSNNKP
PHSSSISHIE SVLQQLDDAQ VQMEELFHER KIKLDIFLQL RIFEQYTIEV TAELDAWNED
LLRQMNDFNT EDLTLAEQRL QRHTERKLAM NNMTFEVIQQ GQDLHQYIME VQASGIELIC
EKDIDLAAQV QELLEFLHEK QHELELNAEQ THKRLEQCLQ LRHLQAEVKQ VLGWIRNGES
MLNASLVNAS SLSEAEQLQR EHEQFQLAIE SLFHATSLQK THQSALQVQQ KAEALLQAGH
YDADAIRECA EKVALHWQQL MLKMEDRLKL VNASVAFYKT SEQVCSVLES LEQEYRRDED
WCGGRDKLGP AAEIDHVIPL ISKHLEQKEA FLKACTLARR NAEVFLKYIH RNNVSMPSAA
SHTRGPEQQV KAILSELLQR ENRVLHFWTL KKRRLDQCQQ YVVFERSAKQ ALDWIQETGE
YYLSTHTSTG ETTEETQELL KEYGEFRVPA KQTKEKVKLL IQLADSFVEK GHIHATEIRK
WVTTVDKHYR DFSLRMGKYR YSLEKALGVN TEDNKDLELD IIPASLSDRE VKLRDANHEV
NEEKRKSARK KEFIMAELLQ TEKAYVRDLH ECLETYLWEM TSGVEEIPPG ILNKEHIIFG
NIQEIYDFHN NIFLKELEKY EQLPEDVGHC FVTWADKFQM YVTYCKNKPD SNQLILEHAG
TFFDEIQQRH GLANSISSYL IKPVQRITKY QLLLKELLTC CEEGKGELKD GLEVMLSVPK
KANDAMHVSM LEGFDENLDV QGELILQDAF QVWDPKSLIR KGRERHLFLF EISLVFSKEI
KDSSGHTKYV YKNKLLTSEL GVTEHVEGDP CKFALWSGRT PSSDNKTVLK ASNIETKQEW
IKNIREVIQE RIIHLKGALK EPIQLPKTPA KQRNNSKRDG VEDVDSQGDG SSQPDTISIA
SRTSQNTVDS DKLSGGCELT VVLQDFNAGH SSELTIQVGQ TVELLERPSE RPGWCLVRTT
ERSPPQEGLV PSSALCISHS RSSVEMDCFF PLVKDGYSHS SNENGGKSES VANLQAQPSL
NSIHSSPGPK RSTNTLKKWL TSPVRRLNSG KADGNIKKQK KVRDGRKSFD LGSPKPGDET
TPQGDSADEK SKKGWGEDEP DEESHTPLPP PMKIFDNDPA QDEMSSSLLA ARQASSEVPT
AADLVSAIEQ LVKSKLSLEG GSYRGSLKDP AGCLNEGMTP PTPTRNLEEE QKAKALRGRM
FVLNELVQTE KDYVKDLGIV VEGFMKRIEE KGVPEDMRGK DKIVFGNIHQ IYDWHKDFFL
AELEKCIQEQ ERLAQLFIKH ERKLHIYVWY CQNKPRSEYI VAEYDAYFEE VKQEINQRLT
LSDFLIKPIQ RITKYQLLLK DFLRYSEKAG LECSDIEKAV ELMCLVPKRC NDMMNLGRLQ
GFEGTLTAQG KLLQQDTFYV IELDAGMQSR TKERRVFLFE QIVIFSELLR KGSLTPGYMF
KRSIKMNYLV LEENVDNDPC KFALMNRETS ERVILQAANA DIQQAWVQDI NQVLETQRDF
LNALQSPIEY QRKERSTAVM RSQPARAPQA SPRPYSSVPM GSEKPPKGSS YNPPLPPLKI
STSNGSPGFD YHQPGDKFEA SKSDLGGCNG TSSMAVIKDY YALKENEICV SQGEVVQVLA
ANQQNMCLVY QPASDHSPAA EGWVPGSILA PLTKAMAAAA ENSDGSIKKS CSWHTLRMRK
RAEVENTGKN EATGPRKPKD ILGNKVSVKE TNSSEESECD DLDPNTSMEI LNPNFIQEVA
PEFLVPLVDV TCLLGDTVTL QCKVCGRPKP AITWKGPDQN ILDTDNSSAT YTVSSCDSGE
ITLKICNLMP QDSGIYTCIA TNDHGTTSTS ATVKVQGVPA APNRPIAQER SCTSVILRWL
PPSSTGNCTI SGYTVEYREE GSQAWQQSVA STLDTYLVIE DLSPGSPYQF RVSASNPWGI
SLPSEPSEFV RLPEYDAAAD GATISWKENF DSAYTELNEI GRGRFSIVKK CIHKATRKDV
AVKFVSKKMK KKEQAAHEAA LLQHLQHPQY VTLHDTYESP TSYILILELM DDGRLLDYLM
NHDELMEEKV AFYIRDIMEA LQYLHNCRVA HLDIKPENLL IDLRIPVPRV KLIDLEDAVQ
ISGHFHIHHL LGNPEFAAPE VIQGIPVSLG TDIWSIGVLT YVMLSGVSPF LDESKEETCI
NVCRVDFSFP HEYFCGVSNA ARDFINVILQ EDFRRRPTAA TCLQHPWLQP HNGSYSKIPL
DTSRLACFIE RRKHQNDVRP IPNVKSYIVN RVNQGT
//
