ID A0A671LZ12_9TELE Unreviewed; 2713 AA.
AC A0A671LZ12;
DT 17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 1.
DT 10-JUN-2026, entry version 29.
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=LOC107704091 {ECO:0000313|Ensembl:ENSSANP00000025771.1};
OS Sinocyclocheilus anshuiensis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Cyprinidae; Cyprininae; Sinocyclocheilus.
OX NCBI_TaxID=1608454 {ECO:0000313|Ensembl:ENSSANP00000025771.1, ECO:0000313|Proteomes:UP000472260};
RN [1] {ECO:0000313|Proteomes:UP000472260}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26728391;
RA Yang J., Chen X., Bai J., Fang D., Qiu Y., Jiang W., Yuan H., Bian C.,
RA Lu J., He S., Pan X., Zhang Y., Wang X., You X., Wang Y., Sun Y., Mao D.,
RA Liu Y., Fan G., Zhang H., Chen X., Zhang X., Zheng L., Wang J., Cheng L.,
RA Chen J., Ruan Z., Li J., Yu H., Peng C., Ma X., Xu J., He Y., Xu Z., Xu P.,
RA Wang J., Yang H., Wang J., Whitten T., Xu X., Shi Q.;
RT "The Sinocyclocheilus cavefish genome provides insights into cave
RT adaptation.";
RL BMC Biol. 14:1-1(2016).
RN [2] {ECO:0000313|Ensembl:ENSSANP00000025771.1}
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 -!- 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; ENSSANT00000027446.1; ENSSANP00000025771.1; ENSSANG00000011223.1.
DR Proteomes; UP000472260; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019898; C:extrinsic component of membrane; 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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IEA:TreeGrafter.
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 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; 2.30.30.40: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: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; 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; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
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; 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; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR PANTHER; PTHR22826:SF106; TRIO, ISOFORM A; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF16609; SH3-RhoG_link; 2.
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; 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; 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; PS50010; DH_2; 2.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000472260};
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 1210..1385
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1397..1509
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1573..1638
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 1817..1970
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1982..2097
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2156..2221
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 2268..2358
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2409..2664
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1526..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1658..1762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 676..703
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1546..1572
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1658..1678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1708..1719
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1720..1733
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1753..1762
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2713 AA; 310473 MW; EB70CAAD2638D14F CRC64;
MLSIIVLRKK IIIGRSHLQK NRKSESANKI TIGASEEVSR HGFTVIVDMR GSKWDSIKPL
LKILQESFPS CIHVALIIKP DNFWQKQRTN FGSSKFEFET IMVSLEGLTK VVDPSQLTPD
FEGGLDYDHE EWIEVRVAFE DFTSNAARIL SRLEELQDLV SQRELPSDLD GSRRAMEEHA
SLKKKVTKAP VEELDAEGQR LLQRIQCEEK GRGDIQGLAP KVQALLDKLH ATRQHLHQSW
HMRKVKLDQC FQLRLFQQDA EKMFDWIVHN KGLFLTTYTE IGPNHQHVLE LQTQHNHFAM
NCMNVYVNIS RIMSVGNRLL ESGHYATQQI QQISGQLEQE WKAFAAALDE RSTLLEMSAN
FHQKTDQYMS NMDSWCKACG EGELPSELQD LEDTIHHHQG LYEHITTAYS EVSQDGKALL
DKLQRPLTPG SADSLTSSAN YSKAVHHVLD IIHEVLHHQR QLENIWQHRK LRLHQRLQLC
VFQQDVQQVL DWIENHGEAF LSKHTGVGKS LHRARALQKR HEDFEEVAQN TYTNADKLLE
AAEQLAQTGE CDPEEIYQAA HQLEDRIQDF VRRVEKRKVL LDMSVAFHTH SKELWTWLEE
LQKELLDDVY AESVEAVQEL IKRFGQQQQT TLQVTVNVIK EGEDLIQQLR YCPMRKHRDS
AISSNKTPHN SSMAHIESVL QQLDEAQAQM EELFQERKIK LELFLQLRIF ERDAIDVISD
LESWNEELSQ QMNEFDTEDL TLAEQRLQHH ADKALTMNNL TFHVIHQGQE LLQYVTEVQD
SGVELLCDRD VDMATRVQDL LDFLHEKQQE LDAAAEQHRR HLEQCVQLRH LQAEVKQVLG
WIRNGESMLN AGLITASSLQ EAEQLQREHE QFQHAIEKTH QSALQVQQKA EALLQANHYD
MDMIRDCAEK VASHWQQLML KMEDRLKLVN ASVAFYKTSE QVCSVLESLE QEYKREEDWC
GGIDKLGPNS ESDHVMPMIS KHLEQKEAFL KACTLARRNA DVFLKYLHRN SVNMPGMLAH
VKAPEQQVKN ILNELLQREN RVLHFWTMRK RRLDQCQQYV VFERSAKQAL EWIHDTGEFY
LSTHTSTGST IHHTQELLKE HEEFQITAKQ TKERVKLLIQ LADGFCEKGH SHASEIQKWI
ASVDKRYRDF SLRMDKYRSC LEKALGLSTD SNKSKDLQLD IIPASAPGAE VKLRDANHEL
NEEKRKSARR KEFIMAELIQ TEKTYVRDLR ECMDTYLWEM SSGVEEIPPG IVNKEHIIFG
NMQDLLEFHH NIFLKELEKY EQLPEDVGHC FVTWADKFRM YVNYCKNKPD STQLILEHAG
TYFDEIQQRH RLANSLSSYL IKPVQRITKY QLLLKELLTC CEEGKGEIKD GLEVMLSVPK
KANDAMHLSM LEGFDENIES QGELILQESF QVWDPKTLIR KGRERHLFLF EMSLIFSKDV
KDSNGRSKYL YKSKLMTSQL GVTEHVEGDP CKFALWLGRT PTSDNKIVLK ASCIENKQDW
IKHVREVIQE RTILLRGALK EPIHIPKATA TKHKGKRDGE DLDSQGDASS QPDTISIASR
TSQNTLDSDK LSSGSELTVV IHDFMASNGS ELTVRRGQTV ELVERPQDKP DWCLVRTTDR
SPAQEGLVPS SMLCIAHSRS SMEMEGIFNH KDTLSVSSND GGLSGSATLQ PGHLQSSPGP
KRPGNTLRKW LTSPVRRLSS GKADGHVKKL AHKHKKSRDV RKNADAGSQK DSDDSAATPQ
DETIEEVGDQ KHLNTIHSSE TPSAAELVSA IEELVKSKMV GDHRVVGDHS LSIFFYMITC
FTCHCLHGNH TDVFWHLQGY MSRMREEGVP DDMKGKDKIV FGNIQQIYDW HKDFFLGELE
KCLEDPDRLA PLFIRQERRL HMYIVYCQNK PKSEHIVSEY IDTYFEDLKQ RLGHRLQITD
LLIKPVQRIM KYQLLLKDFL KFSKKAGLDT VESEKAVEVM CVVPKRCDDM MNVGRLQGFD
GKIVAQGRLL LQDTFMVSDQ DGGLLSRMKE RRVFLFEQIV IFSEPLDKKK GFSMPGYLFK
NSIKVSWLGL EESPDNDPCK FILTSRSSTG STEHYVLHSS NRAVCQAWIQ QISSILENQR
NFLNGNTILE FPKSPMNYEQ PPSNWLNPGF LNRRPAGHIR QVREKSLAHS ESSSSSSVST
MLVTQDYVAL KEDEISVYQG EVVQTLASNQ QNMFLVFRAA TEQGPAAEGW IPGYVLGSLK
TVLYLSIRKS SSWHTALRIR RKSEKREKEG RKESKPENVS DLFAAVPPEF VIPLSEVVCD
RGDSVTLRCK ICGQPKASVC WRGPDQSTLS NGGRYTLTHS ETGEVILRIS PAILDDSGTY
TCIASNDVGS VTSTAYLRVL GQLSLFEHCS KQKLVPLYIE CRVKSPTLFF FVGTSCDGLL
WKDNFESLYT EVMELGRGRF AVTKWCEQRG SRRSVAAKLV NKKLMCREQV VQELGVLQCL
QHPHLVGLLD TYETPASYVL ILEIADQGRL LDYIVSWGNL TEEKVSLYLQ DILEALHYLH
TCRIAHLDLK PENVLIEQTS TQPLVKLTDF GDAAHLSNTP YIHPLLGSPE FSAPELVLGE
PAALASDLWS LGVLAYVMLS GASPFLDESV EETCLNICRL DFSFPEDYFR SVSQAARDFV
CVLLQGEPCR RPSAQVCLRE EPWMQPNAAS GAARLDTSRL ISFIERRKHQ NDLRPPYVVN
ELDLPSFMLI CRV
//
