ID A0A2I3S849_PANTR Unreviewed; 2931 AA.
AC A0A2I3S849;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 31.
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:ENSPTRP00000073001.1,
GN ECO:0000313|VGNC:VGNC:57664};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000073001.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000073001.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000073001.1}
RP IDENTIFICATION.
RG Ensembl;
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 EMBL; AACZ04048124; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSPTRT00000105791.1; ENSPTRP00000073001.1; ENSPTRG00000015311.6.
DR VGNC; VGNC:57664; KALRN.
DR GeneTree; ENSGT00940000155248; -.
DR Proteomes; UP000002277; Chromosome 3.
DR Bgee; ENSPTRG00000015311; Expressed in temporal lobe and 21 other cell types or tissues.
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; 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; 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; 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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
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 1..125
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1226..1401
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1413..1525
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1591..1656
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1874..2049
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2061..2171
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2266..2331
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2416..2509
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2516..2610
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2629..2883
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 655..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1539..1587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1695..1802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2188..2260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2357..2399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 864..891
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 666..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1562..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1695..1718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1727..1749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1758..1782
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2188..2206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2231..2245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2357..2379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2658
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2931 AA; 333921 MW; BD04BDCF2910A3A3 CRC64;
RTQMGWDYCN HDRIRQEDLR KLVTYLASVP SEDVCKRGFT VIIDMRGSKW DLIKPLLKTL
QEAFPAEIHV ALIIKPDNFW QKQKTNFGSS KFIFETSMVS VEGLTKLVDP SQLTEEFDGS
LDYNHEEWIE LRLSLEEFFN SAVHLLSRLE DLQEMLARKE FPVDVEGSRR LIDEHTQLKK
KVLKAPVEEL DREGQRLLQC IRCSDGFSGR NCIPGSADFQ SLVPKITSLL DKLHSTRQHL
HQMWHVRKLK LDQCFQLRLF EQDAEKMFDW ISHNKELFLQ SHTEIGVSYQ YALDLQTQHN
HFAMNSMNAY VNINRIMSVA SRLSEAGHYA SQQIKQISTQ LDQEWKSFAA ALDERSTILA
MSAVFHQKAE QFLSGVDAWC KMCSEGGLPS EMQDLELAIH HHQTLYEQVT QAYTEVSQDG
KALLDVLQRP LSPGNSESLT ATANYSKAVH QVLDVVHEVL HHQRRLESIW QHRKVRLHQR
LQLCVFQQDV QQVLDWIENH GEAFLSKHTG VGKSLHRARA LQKRHDDFEE VAQNTYTNAD
KLLEAAEQLA QTGECDPEEI YKAARHLEVR IQDFVRRVEQ RKLLLDMSVS FHTHTKELWT
WMEDLQKEML EDVCADSVDA VQELIKQFQQ QQTATLDATL NVIKEGEDLI QQLRSAPPSL
GEPSEARDSA VSNNKTPHSS SISHIESVLQ QLDDAQVQME ELFHERKIKL DIFLQLRIFE
QYTIEVTAEL DAWNEDLLRQ MNDFNTEDLT LAEQRLQRHT ERKLAMNNMT FEVIQQGQDL
HQYIMEVQAS GIELICEKDI DLAAQVQELL EFLHEKQHEL ELNAEQTHKR LEQCLQLRHL
QAEVKQVLGW IRNGESMLNA SLVNASSLSE AEQLQREHEQ FQLAIESLFH ATSLQKTHQS
ALQVQQKAEV LLQAGHYDAD AIRECAEKVA LHWQQLMLKM EDRLKLVNAS VAFYKTSEQV
CSVLESLEQE YRRDEDWCGG RDKLGPAAEI DHVIPLISKH LEQKEAFLKA CTLARRNAEV
FLKYIHRNNV SMPSVASHTR GPEQQVKAIL SELLQRENRV LHFWTLKKRR LDQCQQYVVF
ERSAKQALDW IQETGEFYLS THTSTGETTE ETQELLKEYG EFRVPAKQTK EKVKLLIQLA
DSFVEKGHIH ATEIRKWVTT VDKHYRDFSL RMGKYRYSLE KALGVNTEDN KDLELDIIPA
SLSDREVKLR DANHEVNEEK RKSARKKEFI MAELLQTEKA YVRDLHECLE TYLWEMTSGV
EEIPPGILNK EHIIFGNIQE IYDFHNNIFL KELEKYEQLP EDVGHCFVTW ADKFQMYVTY
CKNKPDSNQL ILEHAGTFFD EIQQRHGLAN SISSYLIKPV QRITKYQLLL KELLTCCEEG
KGELKDGLEV MLSVPKKAND AMHVSMLEGF DENLDVQGEL ILQDAFQVWD PKSLIRKGRE
RHLFLFEISL VFSKEIKDSS GHTKYVYKNK LLTSELGVTE HVEGDPCKFA LWSGRTPSSD
NKTVLKASNI ETKQEWIKNI REVIQERIIH LKGALKEPLQ LPKTPAKQRN NSKRDGVEDI
DSQGDGSSQP DTISIASRTS QNTVDSDKLS GGCELTVVLQ DFSAGHSSEL TIQVGQTVEL
LERPSERPGW CLVRTTERSP PLEGLVPSSA LCISHSRSSV EMDCFFPLVK DAYSHSSSEN
GGKSESVANL QAQPSLNSIH SSPGPKRSTN TLKKWLTSPV RRLNSGKADG NIKKQKKVRD
GRKSFDLGSP KPGDETTPQG DSADEKSKKG WGEDEPDEES HTPLPPPMKI FDNDPTQDEM
SSSLLAARQA STEVPTAADL VNAIEKLVKN KLSLEGSSYR GSLKDPAGCL NEGMAPPTPP
KNPEEEQKAK ALRGRMFVLN ELVQTEKDYV KDLGIVVEGF MKRIEEKGVP EDMRGKDKIV
FGNIHQIYDW HKDFFLAELE KCIQEQDRLA QLFIKHERKL HIYVWYCQNK PRSEYIVAEY
DAYFEEVKQE INQRLTLSDF LIKPIQRITK YQLLLKDFLR YSEKAGLECS DIEKAVELMC
LVPKRCNDMM NLGRLQGFEG TLTAQGKLLQ QDTFYVIELD AGMQSRTKER RVFLFEQIVI
FSELLRKGSL TPGYMFKRSI KMNYLVLEEN VDNDPCKFAL MNRETSERVV LQAANADIQQ
AWVQDINQVL ETQRDFLNAL QSPIEYQRKE RSTAVTRSQP ARLPQASPRP YSSVPAGSEK
PPKGSSYNPP LPPLKISTSN GSPGFEYHQP GDKFEASKQN DLGGCNGTSS MAVIKDYYAL
KENEICVSQG EVVQVLAVNQ QNMCLVYQPA SDHSPAAEGW VPGSILAPLT KATAAESSDG
SIKKSCSWHT LRMRKRAEVE NTGKNEATGP RKPKDILGNK VSVKETNSSE ESECDDLDPN
TSMEILNPNF IQEVAPEFLV PLVDVTCLLG DTVILQCKVC GRPKPTITWK GPDQNILDTD
NSSATYTVSS CDSGEITLKI CNLMPQDSGI YTCIATNDHG TTSTSATVKV QGVPAAPNRP
IAQERSCTSV ILRWLPPSST GNCTISGYTV EYREEGSQIW QQSVASTLDT YLVIEDLSPG
CPYQFRVSAS NPWGISLPSE PSEFVRLPEY DAAADGATIS WKENFDSAYT ELNEIGRGRF
SIVKKCIHKA TRKDVAVKFV SKKMKKKEQA AHEAALLQHL QHPQYITLHD TYESPTSYIL
ILELMDDGRL LDYLMNHDEL MEEKVAFYIR DIMEALQYLH NCRVAHLDIK PENLLIDLRI
PVPRVKLIDL EDAVQISGHF HIHHLLGNPE FAAPEVIQGI PVSLGTDIWS IGVLTYVMLS
GVSPFLDESK EETCINVCRV DFSFPHEYFC GVSNAARDFI NVILQEDFRR RPTAATCLQH
PWLQPHNGSY SKIPLDTSRL ACFIERRKHQ NDVRPIPNVK SYIVNRVNQG T
//
