ID A0A2K5S3E8_CEBIM Unreviewed; 2945 AA.
AC A0A2K5S3E8;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 10-JUN-2026, entry version 42.
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|Ensembl:ENSCCAP00000034912.1};
OS Cebus imitator (Panamanian white-faced capuchin) (Cebus capucinus
OS imitator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC Cebinae; Cebus.
OX NCBI_TaxID=2715852 {ECO:0000313|Ensembl:ENSCCAP00000034912.1, ECO:0000313|Proteomes:UP000233040};
RN [1] {ECO:0000313|Ensembl:ENSCCAP00000034912.1}
RP IDENTIFICATION.
RG Ensembl;
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 STRING; 9516.ENSCCAP00000034912; -.
DR Ensembl; ENSCCAT00000052689.1; ENSCCAP00000034912.1; ENSCCAG00000034890.1.
DR GeneTree; ENSGT00940000155248; -.
DR OMA; AKXFIMA; -.
DR Proteomes; UP000233040; Unassembled WGS sequence.
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 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 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; 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; 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; 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; 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; 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 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 Membrane {ECO:0000256|SAM:Phobius};
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:UP000233040};
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};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 14..160
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1240..1415
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1427..1539
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1605..1670
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1888..2063
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2075..2185
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2280..2345
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2430..2523
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2530..2624
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2643..2897
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 690..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1553..1601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1709..1816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2203..2245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2371..2413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 899..926
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 705..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1709..1726
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1777..1786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2402..2412
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2672
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2945 AA; 335101 MW; FA7B14A3D6FF26F9 CRC64;
MGPCDSASCR FPLWLVFLNT LFFLLFAGGR DKRGGPILTF PARSNHDRIR QEDLRKLVTY
LASVPSEDVC KRGFTVIIDM RGSKWDLIKP LLKTLQEAFP AEIHVALIIK PDNFWQKQKT
NFGSSKFIFE TSMVSVEGLT KLVDPSQLTE EFDGSLDYNH EEWIELRLSL EEFFNSAVHL
LSRLEDLQEM LARKEFPVDV EGSRRLIDEH TQLKKKVLKA PVEELDREGQ RLLQCIRCSD
GFSGRNCIPG SADFQSLVPK ITSLLDKLHS TRQHLHQMWH VRKLKLDQCF QLRLFEQDAE
KMFDWISHNK ELFLQSHTEI GVSYQYALDL QTQHNHFAMN SMNAYVNINR IMSVASRLSE
AGHYASQQIK QISTQLDQEW KSFAAALDER STILAMSAVF HQKAEQFLSG VDAWCKMCSE
GGLPSEMQDL ELAIHHHQTL YEQVTQAYTE VSQDGKALLD VLQRPLSPGN SESLTATANY
SKAVHQVLDV VHEVLHHQRR LESIWQHRKV RLHQRLQLCV FQQDVQQVLD WIENHGEAFL
SKHTGVGKSL HRARALQKRH DDFEEVAQNT YTNADKLLEA AEQLAQTGEC DPEEIYKAAR
HLEVRIQDFV RRVEQRKLLL DMSVSFHTHT KELWTWMEDL QKEMLEDVCA DSVDAVQELI
KQFQQQQTAT LDATLNVIKE GEDLIQQLRS APPSLGEPSE ARDSAVSNNK TPHTSSISHI
ESVLQQLDDA QVQMEELFHE RKIKLDIFLQ LRIFEQYTIE VTAELDAWNE DLLRQMNDFN
TEDLTLAEQR LQRHTERKLA MNNMTFEVIQ QGQDLHQYIM EVQASGIELI CEKDIDLAAQ
VQELLEFLHE KQHELELNAE QTHKRLEQCL QLRHLQAEVK QVLGWIRNGE SMLNASLVNA
SSLSEAEQLQ REHEQFQLAI ESLFHATSLQ KTHQSALQVQ QKAEVLLQAG HYDADAIREC
AEKVALHWQQ LMLKMEDRLK LVNASVAFYK TSEQVCSVLE SLEQEYRRDE DWCGGRDKLG
PAAEIDHVIP LISKHLEQKE AFLKACTLAR RNAEVFLKYI HRNNVSMPSV ASHTRGPEQQ
VKAILSELLQ RENRVLHFWT LKKRRLDQCQ QYVVFERSAK QALDWIQETG EFYLSTHTST
GETTEETQEL LKEYGEFRVP AKQTKEKVKL LIQLADSFVE KGHIHATEIR KWVTTVDKHY
RDFSLRMGKY RYSLEKALGV NTEVGRGIAD GSKRTIPENL RQFIMAELLQ TEKAYVRDLH
ECLETYLWEM TSGVEEIPPG ILNKEHIIFG NIQEIYDFHN NIFLKELEKY EQLPEDVGHC
FVTWADKFQM YVTYCKNKPD SNQLILEHAG TFFDEIQQRH GLANSISSYL IKPVQRITKY
QLLLKELLTC CEEGKGELKD GLEVMLSVPK KANDAMHVSM LEGFDENLDV QGELILQDAF
QVWDPKSLIR KGRERHLFLF EISLVFSKEI KDSTGHTKYV YKNKLLTSEL GVTEHVEGDP
CKFALWSGRT PSSDNKTVLK ASNIETKQEW IKNIREVIQE RIIHLKGALK EPLQLPKTPA
KQRNNSKRDG VEDIDSQGDG SSQPDTISIA SRTSQNTVDS DKLSGGCELT VVLQDFSAGH
STELTIQVGQ TVELLERPSE RPGWCLVRTT ERSPPLEGLV PSSALCISHS RSSVEMDCFF
PLVKDAYSHS SSENGGKSES VANLQAQPSL NSIHSSPGPK RSTNTLKKWL TSPVRRLNSG
KADGNIKKQK KVRDGRKSFD LGSPKPGDET TPQGDSADEK SKKGWGEDEP DEESHTPLPP
PMKIFDNDPT QDEMSSSLLA ARQASTEVPT AADLVSAIEK LVKNKLSLEG GSYRGSLKDP
AGCLNEGMAQ PTPPRNLEEE QKAKALRGRM FVLNELLQTE KDYVKDLGIV VEGFMKRIEE
KGVPEDMRGK DKIVFGNIHQ IYDWHKDFFL AELEKCIQEQ DRLAQLFIKH ERKLHIYVWY
CQNKPRSEYI VAEYDGYFEE VKQEINQRLT LSDFLIKPIQ RITKYQLLLK DFLRYSEKAG
LECSDIEKAV ELMCLVPKRC NDMMNLGRLQ GFEGTLTAQG KLLQQDTFYV IDLDAGMQSR
TKERRVFLFE QIVIFSELLR KGSLTPGYMF KKSIKMNYLV LEENVDNDPC KFALMNRETS
EKVILQAANA DIQQAWVQDI NQVLETQRDF LNALQSPIEY QRKERSTAVM RSQPARLPQA
SPRPYSSAPV VSEKPPKGSS YNPPLPPLKI PTSNGSPGFE YHQPGDKFEA SKQNDLGGCN
GTSSMAVIKD YYALKENEIC VSQGEVVQVL AVNQQNMCLV YQPASDHSPA AEGWVPGSIL
APLTKATAAE SSDGSIKKSC SWHTLRMRKR AEVENTGKNE ATGPRKPKDI LGNKVSVKET
NSSEESECDD LDPNTSMEIL NPNFIQEVAP EFLVPLVDVT CLLGDTVILQ CKVCGRPKPT
ITWKGPDQNI LDTDNSSATY SVSSCDSGEI TLKICNLMPQ DSGIYTCIAT NDHGTTSTSA
TVKVQGVPAA PNRPIAQERS CTSVILRWLP PSSTGNCTIS GYTVEYREEG SQTWQQSVAS
TLDTYLVIED LSPGCPYQFR VSASNPWGIS LPSEPSEFVR LPEYDPAADG ATISWKENFD
SAYTELNEIG RGRFSIVKKC IHKATRKDVA VKFVSKKMKK KEQAAHEAAL LQHLQHPQYI
TLHDTYESPT SYILILELMD DGRLLDYLMN HDELMEEKVA FYIRDIMEAL QYLHNCRVAH
LDIKPENLLI DLRIPVPRVK LIDLEDAVQI SGHFHIHHLL GNPEFAAPEV IQGIPVSLGT
DIWSIGVLTY VMLSGVSPFL DESKEETCIN VCRVDFSFPH EYFCGVSNAA RDFINVILQE
DFRRRPTAAT CLQHPWLQPH NGSYSKIPLD TSRLACFIER RKHQNDVRPI PNVKSYIVNR
VNQGT
//
