ID A0A8C3JVJ0_9CHAR Unreviewed; 2890 AA.
AC A0A8C3JVJ0;
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=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};
OS Calidris pygmaea (Spoon-billed sandpiper).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Neoaves; Charadriiformes; Scolopacidae;
OC Calidris.
OX NCBI_TaxID=425635 {ECO:0000313|Ensembl:ENSCPGP00000013818.1, ECO:0000313|Proteomes:UP000694419};
RN [1] {ECO:0000313|Ensembl:ENSCPGP00000013818.1}
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 Ensembl; ENSCPGT00000015150.1; ENSCPGP00000013818.1; ENSCPGG00000009171.1.
DR Proteomes; UP000694419; 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 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; 6.
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; 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; 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; -; 4.
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; 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; 6.
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; 5.
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:UP000694419};
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..138
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1188..1363
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1375..1487
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1553..1618
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1836..2011
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2023..2133
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2227..2292
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2375..2468
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2475..2569
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2588..2842
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1501..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1638..1774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2150..2223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2314..2356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 835..862
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1534..1546
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1638..1674
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1725..1734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1763..1774
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2198..2208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2211..2220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2617
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2890 AA; 329350 MW; E73F4986CB5BE7E1 CRC64;
MLCGRGGRDK RGGPVLTFPA RSNHDRIRQE DLRKLVTYLA SVPSEDVCKR GFTVIIDMRG
SKWDLIKPLL KTLQEAFPAE IHVALIIKPD NFWQKQKTNF GSSKFIFETS MVSVEGLAKL
VDPSQLTDEF EGSLDYNHDE WIELRVSLEE FFNSAIHLLS RLEDLQEMLA RKEFPVDVEG
SRRLIDEHTQ LKKKVIKAPV EELDREGQRL LQCIRCSDGF SGRNCIPGSA DFQSLVPKIT
SLLDKLHSTR QHLHQMWHVR KLKLDQCFQL RLFEQDAEKM FDWISHNKEL FLQSHTEIGV
SYQHALDLQT QHNHFAMNSM NAYVNINRIM SVASRLSEAG HYASQQIKQI SSQLDQEWKS
FAAALDERST ILAMSAVFHQ KAEQFLSGVD AWCKMCSEGG LPSEMQDLEL AIHHHQTLYE
QVTQAYTEVS QDGKALLDVL QRPLSPGNSE SLTATANYSK AVHQVLDVVH EVLHHQRRLE
SIWQHRKVRL HQRLQLCVFQ QDVQQVLDWI ENHGEAFLSK HTGVGKSLHR ARALQKRHDD
FEEVAQNTYT NADKLLEAAE QLAQTGECDP EEIYKAARHL EVRIQDFVRR VEQRKLLLDM
SVSFHTHTKE LWTWMEDLQK ELLEDVSSTW RTGVRNLMDS AVSNNKTPHN SSISHIESVL
QQLDEAQVQM EELFHERKIK LDIFLQLRIF EQYTIEVTAE LDAWNEDLLR QMNDFNTEDL
TLAEQRLQRH TERKLAMNNM TFEVIQQGQD LHQYIMEVQA SGIELICEKD IDLATQVQEL
LEFLHEKQHE LELNADQTHK RLEQCLQLRH LQAEVKQVLG WIRNGESMLN ASLVNASSLS
EAEQLQREHE QFQLAIEKTH QSALQVQQKA EVLLQAGHYD ADAIRECAEK VALHWQQLML
KMEDRLKLVN ASVAFYKTSE QVCSVLESLE QEYRRDEDWC GGRDKLGPAA EIDHVIPLIS
KHLEQKEAFL KACTLARRNA EVFLKYIHRN NVSMPGVASH TRGPEQQVKA ILSELLQREN
RVLHFWTLKK RRLDQCQQYV VFERSAKQAL DWIQETGEYY LSTHNSTGES AEETQELLKE
YGEFRVPAKQ TKEKVKLLIQ LADSFVEKGH IHATEIRKWV TTVDKRYRDF SLRMGKYRYS
LEKALGINTE DNKDLELDII PASLSDREVK LRDANHEVNE EKRKSARKKE FIMAELLQTE
KAYVRDLHEC LETYLWEMTS GVEEIPAGIL NKEHIIFGNI QEIYDFHNNI FLKELEKYEQ
LPEDVGHCFV TWADKFQMYV TYCKNKPDSS QLILEHAGTF FDEIQQRHGL ANSISSYLIK
PVQRITKYQL LLKELLTCCE EGKGELKDGL EVMLSVPKKA NDAMHVSMLE GFDENLDVQG
ELILQDSFQV WDPKSLIRKG RERHLFLFEI SLVFSKEIKD SSGHTKYVYK NKLLTSELGV
TEHVEGDPCK FALWSGRTPS SDNKTVLKAS SIETKQEWIK NIREVIQERI IHLKGALKEP
IQLPKTPAKQ RNNSRRDGVD DADSQGDGSS QPDTISIASR TSQNTVDSDK LSGGCELTVV
LQDFTAGHSS ELSIQVGQTV ELLERPSERP GWCLVRTTER SPPQEGLVPS SALCISHSRS
SVEMDCFFPS GKDAYSVSSN DNGGKSDSVA NLQPQPSLNS IQSSPGPKRS TNTLKKWLTS
PVRRLNSGKT ESNIKKQKKV RDGRKSFDLG SPKTGDETTP QGDSADEKSK KGWGEDEPDE
ESHTPLPPPM KIFDNDPTQD EMSSSLLAAR QSSSDVPTAA DLVSAIEKLV KSKLTLEGGS
YRGSLKDATG CLNEGMTPST PPRNLEEEQK AKAMRGRMFV LNELVQTEKD YVKDLGTVVE
GFMKRIEEKG VSEDMKGKDK IVFGNIHQIY DWHKDFFLAE LEKCLQEPDR LAQLFIKHER
RLHMYVVYCQ NKPRSEYIVA EYEAYFEEVQ QEISQRLTIS DFLIKPIQRI TKYQLLLKDF
LRYSEKAGLE CSEIEKAVEL MCLVPKRCND MMNLGRLQGF EGKLTAQGKL LQQDTFYVTE
QDSGVQSRPK ERRVFLFEQI VIFSELLRKG SLTPGYMFKK SIKMNYLIIE ENVDNDPCKF
ALMSRETSER VILQAANPEI QQAWVQDINQ VLDTQRDFLN ALQSPIEYQR KESSSAVLRP
QTGRVPQPNS RPYSSVPVGS EKPLKATSRN PSLPPLKIST SNGSTGYEHS QPGDKYEQSK
TDLGGCNGTS SMVVIKDYYA LKEDEICVNQ GEVVQILAIN QQNMFLVYQP ANDHSPAAEG
WIPGNILAPL TKSTTDNSDG SIKKSCSWHT LRMRKRAEKE SSGKNEANGP RKSKDILGNK
VSVKETNSSE ESECDDLDPN TSVMCVSPCF LPVAPEFLVP LVDITCLLGD TVMLQCKVCG
RPKPTITWKG PDQNILDNDN STATYTVSSC DSGELTLKIC NLMPQDSGIY TCVATNEHGT
ASTSATIKVQ GVPAAPNRPI AQERSCTSVI LRWLPPSSTG NCTISGYTVE YREEGSQVWQ
QSVASTLDTY LVIEDLSPGC QYQFRVSASN PWGISLPSDP SEFVRLPEYD SAADGATISW
KENFDLAYAE LHEIGRGRFS IVKKCVHKAT RKDVAVKFIS KKMKKKEQAA HEAALLQHLQ
HPQYITIHDT YESPTSYILV LELMDDGRLL DYLMNHDELM EEKVAFYIRD TMEALQYLHN
CRVAHLDIKP ENLLIDLRIP VPRVKIIDLE DAVQITGHYH VHHLLGNPEF TAPEVIQGLP
VSLSTDIWSI GVLTYVMLSG VSPFLDESKE ETCINVCRVD FSFPPEYFSD VSHAARDFIN
VILQEDFRRR PTAATCLQHP WLQPHNSSYS KIPLDTSRLA SFIERRRHQY DVHPVPSVKS
FLMSRLNPGT
//
