ID A0A8C6H0N6_MUSSI Unreviewed; 1294 AA.
AC A0A8C6H0N6;
DT 19-JAN-2022, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2022, sequence version 1.
DT 10-JUN-2026, entry version 22.
DE RecName: Full=Non-specific serine/threonine protein kinase {ECO:0008006|Google:ProtNLM};
OS Mus spicilegus (Mound-building mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10103 {ECO:0000313|Ensembl:ENSMSIP00000013831.1, ECO:0000313|Proteomes:UP000694415};
RN [1] {ECO:0000313|Ensembl:ENSMSIP00000013831.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JAN-2026) to UniProtKB.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR Ensembl; ENSMSIT00000017546.1; ENSMSIP00000013831.1; ENSMSIG00000011801.1.
DR GeneTree; ENSGT00940000155248; -.
DR Proteomes; UP000694415; Unplaced.
DR GO; GO:0005737; C:cytoplasm; 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:0004672; F:protein kinase activity; IEA:InterPro.
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; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd11853; SH3_Kalirin_2; 1.
DR CDD; cd14115; STKc_Kalirin_C; 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; 2.60.40.10: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; 1.20.900.10:FF:000008; rho guanine nucleotide exchange factor 25; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
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); 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_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; 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; 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 PANTHER; PTHR22826:SF49; KALIRIN; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF16609; SH3-RhoG_link; 1.
DR Pfam; PF23587; SH3_KALRN; 1.
DR Pfam; PF22697; SOS1_NGEF_PH; 1.
DR PRINTS; PR00014; FNTYPEIII.
DR SMART; SM00060; FN3; 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; SSF49265; Fibronectin type III; 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; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
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; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000694415};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 231..406
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 418..528
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 622..687
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 773..866
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 873..967
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 986..1240
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 35..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1015
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1294 AA; 144870 MW; 747497063EE06574 CRC64;
MKGGDQAYTR GPSLGWLFAK CCCCFPCRDS YSHSSSENGG KSESVAHLQS QPSLNSIHSS
PGPKRSTNTL KKWLTSPVRR LNSGKADGNI KKQKKVRDGR KSFDLGSPKP GDETTPQGDS
ADEKSKKGWG EDEPDEESHT PLPPPMKIFD NDPTQDEMSS LLAARQAPPD VPTAADLVSA
IEKLVKNKLT LEGGSYRGSL KDPTGCLNEG MTPPTPPRNL EEEQKAKALR GRMFVLNELV
QTEKDYVKDL GIVVEGFMKR IEEKGVPEDM RGKEKIVFGN IHQIYDWHKD FFLAELEKCI
QEQDRLAQLF IKHERKLHIY VWYCQNKPRS EYIVAEYDAY FEEVKQEINQ RLTLSDFLIK
PIQRITKYQL LLKDFLRYSE KAGLECSDIE KAVELMCLVP KRCNDMMNLG RLQGFEGTLT
AQGKLLQQDT FYVIELDAGM QSRTKERRVF LFEQIVIFSE LLRKGSLTPG YMFKRSIKMN
YLVLEDNVDG DPCKFALMNR ETSERVILQA ANSDIQQAWV QDINQVLETQ RDFLNALQSP
IEYQRKERST AVIRSQPPRV PQASPRPYSS GPVGSEKPPK GSSYNPPLPP LKISTSNGSP
GFDYHQPGDK FDASKNDLGG CNGTSTMTVI KDYYALKENE ICVSQGEVVQ VLAVNQQNMC
LVYQPASDHS PAAEGWVPGS ILAPLAKATA AAENSDGSIK KSCSWHTLRM RKRADVENSG
KNEATGPRKT KDILGNKVSV KETNSSEESE CDDLDPNTSM EILNPNFIQE VAPEFLVPLV
DVTCLLGDTV LLQCKACGRP KPSITWKGPD QNILDTDNSS ATYTISSCDS GESTLKICNL
MPQDSGIYTC IAANDHGTAS TSATVKVQGV PAAPNRPIAQ ERSCTSVILR WLPPASTGNC
TISGYTVEYR EEGSQVWQQS VASTLDTYLV IEDLSPGCPY QFRVSASNPW GISLPSEPSE
FVRLPEYDAA TDGATISWKE NFDSAYTELN EIGRGRFSIV KKCIHKATRK DVAVKFVSKK
MKKKEQAAHE AALLQHLQHP QYVTLHDTYE SPTSYILILE LMDDGRLLDY LMNHDELMEE
KVAFYIRDIM EALQYLHNCR VAHLDIKPEN LLIDLRIPVP RVKLIDLEDA VQISGHFHIH
HLLGNPEFAA PEVIQGIPVS LGTDIWSIGV LTYVMLSGVS PFLDESKEET CINVCRVDFS
FPHEYFCGVS NAARDFINVI LQEDFRRRPT AATCLQHPWL QPHNGSYSKI PLDTSRLACF
IERRKHQNDV RPIPNVKSYI VNRVNQGTSL SHNP
//
