ID A0A1U8BRS5_MESAU Unreviewed; 2977 AA.
AC A0A1U8BRS5;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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|RefSeq:XP_012969937.1};
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_012969937.1};
RN [1] {ECO:0000313|RefSeq:XP_012969937.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-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: 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 RefSeq; XP_012969937.1; XM_013114483.2.
DR GeneID; 101828803; -.
DR CTD; 8997; -.
DR OrthoDB; 2906033at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; 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:UP000189706};
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 38..183
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1271..1446
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1458..1570
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1636..1701
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1919..2094
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2106..2216
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2311..2376
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2462..2555
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2562..2656
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2675..2929
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1585..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1720..1846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1888..1907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2235..2299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2403..2424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 909..936
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1607..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1772..1794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1803..1827
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2276..2290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2704
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2977 AA; 339386 MW; 7E9415EEB291716C CRC64;
MTDRFWDQWY LWYLRLLRLL DRGILRSFRN DGLKASDVLP ILKEKVAFVS GGRDKRGGPI
LTFPARSNHD RIRQEDLRKL VTYLASVPSE DVCKRGFTVI IDMRGSKWDL IKPLLKTLQE
AFPAEIHVAL IIKPDNFWQK QKTNFGSSKF IFETSMVSVE GLTKLVDPSQ LTEEFDGSLD
YNHEEWIELR LSLEEFFNSA VHLLSRLEDL QEMLARKEFP VDVEGSRRLI DEHTQLKKKV
LKAPVEELDR EGQRLLQCIR CSDGFSGRNC IPGSADFQSL VPKITSLLDK LHSTRQHLHQ
MWHVRKLKLD QCFQLRLFEQ DAEKMFDWIS HNKELFLQSH TEIGVSYQHA LDLQTQHNHF
AMNSMNAYVN INRIMSVASR LSEAGHYASQ QIKQISTQLD QEWKSFAAAL DERSTILAMS
AVFHQKAEQF LSGVDAWCKM CSEGGLPSEM QDLELAIHHH QSLYEQVTQA YTEVSQDGKA
LLDVLQRPLS PGNSESLTAT ANYSKAVHQV LDVVHEVLHH QRRLESIWQH RKVRLHQRLQ
LCVFQQDVQQ VLDWIENHGE AFLSKHTGVG KSLHRARALQ KRHDDFEEVA QNTYTNADKL
LEAAEQLAQT GECDPEEIYK AARHLEVRIQ DFVRRVEQRK LLLDMSVSFH THTKELWTWM
EDLQKEMLED VCADSVDAVQ ELIKQFQQQQ TATLDATLNV IKEGEDLIQQ LRDSAVSNNK
TPHTSSISHI ESVLQQLDDA QVQMEELFHE RKIKLDIFLQ LRIFEQYTIE VTAELDAWNE
DLLRQMNDFN TEDLTLAEQR LQRHTERKLA MNNMTFEVIQ QGQDLHQYIM EVQASGIELI
CEKDIDLAAQ VQELLEFLHE KQHELELNAE QTHKRLEQCL QLRHLQAEVK QVLGWIRNGE
SMLNASLVNA SSLSEAEQLQ REHEQFQLAI ESLFHATSLQ KTHQSALQVQ QKAEALLQAG
HYDADAIREC AEKVALHWQQ LMLKMEDRLK LVNASVAFYK TSEQVCSVLE SLEQEYRRDE
DWCGGRDKLG PAAEMDHVIP LLSKHLEQKE AFLKACTLAR RNAEVFLKYI HRNNVSMPSV
ASHTRGPEQQ VKAILSELLQ RENRVLHFWT LKKRRLDQCQ QYVVFERSAK QALDWIQETG
EYYLSTHTST GETTEETQEL LKEYGEFRVP AKQTKEKVKL LIQLADSFVE KGHIHATEIR
KWVTTVDKHY RDFSLRMGKY RYTLEKALGV NTEDNKDLEL DIIPASLSDR EVKLRDASHE
VNEEKRKSAR KKEFIMAELL QTEKAYVRDL HECLETYLWE MTSGVEEIPP GILNKEHIIF
GNIQEIYDFH NNIFLKELEK YEQLPEDVGH CFVTWADKFQ MYVTYCKNKP DSNQLILEHA
GTFFDEIQQR HGLANSISSY LIKPVQRVTK YQLLLKELLT CCEEGKGELK DGLEVMLSVP
KKANDAMHVS MLEGFDENLD VQGELILQDA FQVWDPKSLI RKGRERHLFL FEISLVFSKE
IKDSSGHTKY VYKNKLLTSE LGVTEHVEGD PCKFALWSGR TPSSDNKTVL KASNIETKQE
WIKNIREVIQ ERIIHLKGAL KEPIQLPKTP AKLRNNSKRE GVEDGDSQGD GSSQPDTISI
ASRTSQNTVD SDKLSGGCEL TVVLQDFNAG HSSELSIQVG QTVELLERPS ERPGWCLVRT
TERSPPQEGL VPSSTLCISH SRSSVEMDCF FPLVKDSYSH SSGENGGKSE SVANLQSQHS
LNSIHSSPGP KRSTNTLKKW LTSPVRRLNS GKADGNIKKQ KKVRDGRKSF DLGSPKPGDE
TTPQGDSADE KSKKGWGEDE PDEESHTPLP PPMKIFDNDP TQDEMSSSLL AARQASAEVP
TAADLVSAIE KLVKSKLTLE GGSYRGSLKD PTGCLNEGMT PPTPPRNLEE EQKAKALRGR
MFVLNELVQT EKDYVKDLGI VVEGFMKRIE EKGVPEDMRG KDKIVFGNIH QIYDWHKDFF
LAELEKCIQE QDRLAQLFIK HERKLHIYVW YCQNKPRSEY IVAEYDAYFE EVKQEINQRL
TLSDFLIKPI QRITKYQLLL KDFLRYSEKA GLECSDIEKA VELMCLVPKR CNDMMNLGRL
QGFEGTLTAQ GKLLQQDTFY VIELDAGMQS RTKERRVFLF EQIVIFSELL RKGSLTPGYM
FKRSIKMNYL VLEENVDNDP CKFALMNRET SERVILQAAN SDIQQAWVQD INQVLETQRD
FLNALQSPIE YQRKERNTAV VRSQPPRVPQ ASPRPYSSVP VGSEKPPKGS SYNPPLPPLK
ISTSNGSPGF DYHQPGDKFE ASKQNDLGGC NGTSSMAVIK DYYALKENEI CVSQGEVVQV
LAVNQQNMCL VYQPASDHSP AAEGWVPGSI LAPLTKATAA AESSDGSIKK SCSWHTLRMR
KRAEVENTGK NEATGPRKPK DILGNKVSVK ETNSSEESEC DDLDPNTSME ILNPNFIQEV
APEFLVPLVD VTCLLGDTVI LQCKVCGRPK PTITWKGPDQ NILDTDNSSA TYTISSCDSG
EITLKICNLM PQDSGIYTCI ATNDHGSAST SATVKVQGVP AAPNRPIAQE RSCTSVILRW
LPPASTGNCT ISGYTVEYRE EGSQVWQQSV ASTLDTYLVI EDLSPGCPYQ FRVSASNPWG
ISLPSEASEF VRLPEYDAAA DGATISWKEN FDSAYTELNE IGRGRFSIVK KCIHKATRKD
VAVKFVSKKM KKKEQAAHEA ALLQHLQHPQ YVTLHDTYES PTSYILILEL MDDGRLLDYL
MNHDELMEEK VAFYIRDITE ALQYLHNCRV AHLDIKPENL LIDLRIPVPR VKLIDLEDAV
QISGHFHIHH LLGNPEFAAP EVIQGIPVSL GTDIWSIGVL TYVMLSGVSP FLDESKEETC
INVCRVDFSF PHEYFCGVSN AARDFINVIL QEDFRRRPTA ATCLQHPWLQ PHNGSYSKIP
LDTSRLACFI ERRKHQNDVR PIPNVKSYIV NRVNQGT
//
