ID A0A6P6DD37_OCTDE Unreviewed; 2947 AA.
AC A0A6P6DD37;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 10-JUN-2026, entry version 24.
DE RecName: Full=Kalirin {ECO:0000256|ARBA:ARBA00074269};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE AltName: Full=Protein Duo {ECO:0000256|ARBA:ARBA00083244};
DE AltName: Full=Serine/threonine-protein kinase with Dbl- and pleckstrin homology domain {ECO:0000256|ARBA:ARBA00077077};
GN Name=Kalrn {ECO:0000313|RefSeq:XP_023558017.1};
OS Octodon degus (Degu) (Sciurus degus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Octodontidae;
OC Octodon.
OX NCBI_TaxID=10160 {ECO:0000313|Proteomes:UP000515203, ECO:0000313|RefSeq:XP_023558017.1};
RN [1] {ECO:0000313|RefSeq:XP_023558017.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2026) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC H(+); 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:ARBA00048679};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00047899};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Interacts with the C-terminal of peptidylglycine alpha-
CC amidating monooxygenase (PAM) and with the huntingtin-associated
CC protein 1 (HAP1). Interacts with FASLG.
CC {ECO:0000256|ARBA:ARBA00065052}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
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_023558017.1; XM_023702249.1.
DR GeneID; 101561596; -.
DR CTD; 8997; -.
DR Proteomes; UP000515203; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; IEA:TreeGrafter.
DR GO; GO:0014069; C:postsynaptic density; IEA:TreeGrafter.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter.
DR GO; GO:0050773; P:regulation of dendrite development; IEA:UniProtKB-ARBA.
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; 5.
DR CDD; cd14115; STKc_Kalirin_C; 1.
DR FunFam; 1.20.900.10:FF:000001; Guanine nucleotide exchange factor DBS; 1.
DR FunFam; 1.10.510.10:FF:000152; kalirin isoform X1; 1.
DR FunFam; 2.30.29.30:FF:000091; kalirin isoform X1; 1.
DR FunFam; 2.30.30.40:FF:000038; kalirin isoform X1; 1.
DR FunFam; 2.30.30.40:FF:000040; kalirin isoform X1; 1.
DR FunFam; 2.60.40.10:FF:000325; kalirin isoform X1; 1.
DR FunFam; 2.60.40.10:FF:000368; kalirin isoform X1; 1.
DR FunFam; 3.30.200.20:FF:000169; kalirin isoform X1; 1.
DR FunFam; 1.20.58.60:FF:000034; kalirin isoform X2; 1.
DR FunFam; 3.40.525.10:FF:000003; kalirin isoform X2; 1.
DR FunFam; 1.20.58.60:FF:000024; Kalirin RhoGEF kinase a; 1.
DR FunFam; 1.20.58.60:FF:000023; Kalirin RhoGEF kinase b; 1.
DR FunFam; 1.20.58.60:FF:000032; Kalirin RhoGEF kinase b; 1.
DR FunFam; 2.30.29.30:FF:000040; Kalirin RhoGEF kinase b; 1.
DR FunFam; 1.20.900.10:FF:000008; rho guanine nucleotide exchange factor 25; 1.
DR FunFam; 1.20.58.60:FF:000015; triple functional domain protein-like; 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; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
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_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
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; IPR058918; KALRN/TRIO-like_spectrin.
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; IPR051336; RhoGEF_Guanine_NuclExch_SF.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR055251; SOS1_NGEF_PH.
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; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 1.
DR Pfam; PF00018; SH3_1; 1.
DR Pfam; PF23587; SH3_KALRN; 1.
DR Pfam; PF22697; SOS1_NGEF_PH; 2.
DR Pfam; PF00435; Spectrin; 4.
DR Pfam; PF23323; Spectrin_6; 1.
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; 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 Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000515203};
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 1274..1449
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1461..1573
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1639..1704
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1890..2065
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2077..2187
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2281..2346
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2432..2525
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2532..2626
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2645..2899
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 712..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1587..1635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1743..1863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2204..2260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2373..2393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 921..948
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 727..737
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1612..1632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1743..1760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1811..1820
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2213..2226
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2674
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2947 AA; 335236 MW; 00129AC66018A232 CRC64;
MNPQEGAAEE GGAADSDVDP FFRTGSFRND GLKASDVLPI LKEKVAFVSG GRDKRGGPIL
TFPARSNHDR IRQEDLRKLV TYLASVPSED VCKRGFTVII DMRGSKWDLI KPLLKTLQEA
FPAEIHVALI IKPDNFWQKQ KTNFGSSKFI FETSMVSVEG LTKLVDPSQL TEEFDGSLDY
NHEEWIELRL SLEEFFNSAV HLLSRLEDLQ EMLARKEFPV DVEGSRRLID EHTQLKKKVL
KAPVEELDRE GQRLLQCIRC SDGFSGRNCI PGSADFQSLV PKITSLLDKL HSTRQHLHQM
WHVRKLKLDQ CFQLRLFEQD AEKMFDWISH NKELFLQSHT EIGVSYQHAL DLQTQHNHFA
MNSMNAYVNI NRIMSVASRL SEAGHYASQQ IKQISTQLDQ EWKSFAAALD ERSTILAMSA
VFHQKAEQFL SGVDAWCKMC SEGGLPSEMQ DLELAIHHHQ TLYEQVTQAY TEVSQDGKAL
LDVLQRPLSP GNSESLTATA NYSTAVHQVL DVVHEVLHHQ RRLESIWQHR KVRLHQRLQL
CVFQQDVQQV LDWIENHGEA FLSKHTGVGK SLHRARALQK RHDDFEEVAQ NTYTNADKLL
EAAEQLAQTG ECDPEEIYKA ARHLEVRIQD FVRRVEQRKL LLDMSVSFHT HTKELWTWME
DLQKEMLEDV CADSVDAVQE LIKQFQQQQT ATLDATLNVI KEGEDLIQQL RSAPPSLGEP
TEARDSAVSN NKTPHSSSIS HIESVLQQLD DAQVQMEELF HERKIKLDIF LQLRIFEQYT
IEVTAELDAW NEDLLRQMND FNTEDLTLAE QRLQRHTERK LAMNNMTFEV IQQGQDLHQY
IMEVQASGIE LICEKDIDLA AQVQELLEFL HEKQHELELN AEQTHKRLEQ CLQLRHLQAE
VKQVLGWIRN GESMLNASLV NASSLSEAEQ LQREHEQFQL AIEKTHQSAL QVQQKAEALL
QAGHYDADAI RECAEKVALH WQQLMLKMED RLKLVNASVA FYKTSEQVCS VLESLEQEYR
RDEDWCGGRD KLGPAAEIDH VIPLISKHLE QKEAFLKACT LARRNAEVFL KYIHRNNVSM
PSVASHTRGP EQQVKAILSE LLQRENRVLH FWTLKKRRLD QCQQFVVFER SAKQALDWIQ
ETGEYYLSTH TSTGETTEET QELLKEYGDF RVPAKQTKEK VKLLIQLADS FIEKGHIHAT
EIRKWVTTVD KHYRDFSLRM GKYRYSLEKA LGVNTEDNKD LELDIIPASL SDREVKLRDA
NHEVNEEKRK SARKKEFIMA ELLQTEKAYV RDLHECLETY LWEMTSGVEE IPPGILNKEH
IIFGNIQEIY DFHNNIFLKE LEKYEQLPED VGHCFVTWAD KFQMYVTYCK NKPDSNQLIL
EHAGTFFDEI QQRHGLANSI SSYLIKPVQR ITKYQLLLKE LLTCCEEGKG ELKDGLEVML
SVPKKANDAM HVSMLEGFDE NLDVQGELIL QDAFQVWDPK SLIRKGRERH LFLFEISLVF
SKEIKDSSGH TKYVYKNKLL TSELGVTEHV EGDPCKFALW SGRTPSSDNK TVLKASNIET
KQEWIKNIRE VIQERIIHLK GALKEPIQLP KTPAKQRNNS KRDGVEDIDS QGDGSSQPDT
ISIASRTSQN TVDSDKLSGG CELTVVLQDF NAGHSSELTV QVGQTVELLE RPSERPGWCL
VRTTERSPPQ EGLVPSSALC ISHSRSSVEM DCFFPLVKDA YSHSSGENGG KSESVANLQA
QPSLNSIHSS PGPKRSTNTL KKWLTSPVRR LNSGKADGNI KKQKKVRDGR KSFDLGSPKP
GDETTPQGDS ADEKSKKGWG EDEPDEESHT PLPPPMKIFD NDPTQDEMTL EGGSYRGSLK
DPTGCLNEGM TPPTPPRNLE EEQKAKALRG RMFVLNELVQ TEKDYVKDLG IVVEGFMKRI
EEKGVPEDMR GKDKIVFGNI HQIYDWHKDF FLGELEKCIQ EQDRLAQLFI KHERKLHIYV
WYCQNKPRSE YIVAEYDAYF EEVKQEINQR LTLSDFLIKP IQRITKYQLL LKDFLRYSEK
AGLECADIEK AVELMCLVPK RCNDMMNLGR LQGFEGTLTA QGKLLQQDTF YVIELDAGLQ
SRTKERRVFL FEQIVIFSEL LRKGSLTPGY MFKRSIKMNY LVLEENVEND PCKFALMNRE
TSERVILQAA NSDIQQAWVQ DINQVLETQR DFLNALQSPI EYQRKERSTA VMRSQPPRAP
QASPRPYSSV PVGSEKPPKG SSYNPPVPPL KISTSNGSPG FDCHQPGDKF ESSKNDLGGC
NGTSSMAVIK DYYALKENEI CVSQGEVVQV LAVNQQNMCL VYQPASDHSP AAEGWVPGSI
LAPLSKAAAA GESSDGSIKK SCSWHTLRMR KRAEVENTGK NEATGPRKSK DILGNKVSVK
ETNSSEESEC DDLDPNTSME ILNPNFIQEV APEFLVPLVD VTCLLGDTVI LQCKVCGRPK
PTITWKGPDQ NILDTDNNSA TYTVSSCDSG EITLKICNLM PQDSGIYTCI ATNDHGTTST
SATVKVQGVP AAPNRPIAQE RSCTSVILRW LPPASTGNCT ISGYTVEYRE EGSQVWQQSV
ASTLDTYLVI EDLSPGCPYQ FRVSASNPWG ISLPSEPSEF VRLPEYDAAA DGATISWKDN
FDSAYTELNE IGRGRFSIVK KCIHKATRKD VAVKFVSKKM KKKEQAAHEA ALLQHLQHPQ
YVTLHDTYES PTSYILILEL MDDGRLLDYL MNHDELMEEK VAFYIRDIME ALQYLHNCRV
AHLDIKPENL LIDLRIPVPR VKLIDLEDAV QISGHFHIHH LLGNPEFAAP EVIQGIPVSL
GTDIWSIGVL TYVMLSGVSP FLDESKEETC INVCRVDFSF PHEYFCGVSN AARDFINVIL
QEDFRRRPTA ATCLQHPWLQ PHNGSYSKIP LDTSRLACFI ERRKHQNDVR PIPNVKSYIV
NRVNQGT
//
