ID A0A212C8L9_CEREH Unreviewed; 756 AA.
AC A0A212C8L9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 10-JUN-2026, entry version 39.
DE SubName: Full=TRIO {ECO:0000313|EMBL:OWK02315.1};
GN ORFNames=Celaphus_00018108 {ECO:0000313|EMBL:OWK02315.1};
OS Cervus elaphus hippelaphus (Central European red deer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Cervidae;
OC Cervinae; Cervus.
OX NCBI_TaxID=46360 {ECO:0000313|EMBL:OWK02315.1, ECO:0000313|Proteomes:UP000242450};
RN [1] {ECO:0000313|EMBL:OWK02315.1, ECO:0000313|Proteomes:UP000242450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hungarian {ECO:0000313|EMBL:OWK02315.1};
RX PubMed=29294181;
RA Bana N.A., Nyiri A., Nagy J., Frank K., Nagy T., Steger V., Schiller M.,
RA Lakatos P., Sugar L., Horn P., Barta E., Orosz L.;
RT "The red deer Cervus elaphus genome CerEla1.0: sequencing, annotating,
RT genes, and chromosomes.";
RL Mol. Genet. Genomics 293:665-684(2018).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWK02315.1}.
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DR EMBL; MKHE01000025; OWK02315.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A212C8L9; -.
DR OrthoDB; 10256089at2759; -.
DR Proteomes; UP000242450; Chromosome 25.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:TreeGrafter.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:TreeGrafter.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IEA:TreeGrafter.
DR CDD; cd11853; SH3_Kalirin_2; 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; 2.60.40.10:FF:000368; kalirin isoform X1; 1.
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); 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR000719; Prot_kinase_dom.
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; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR PANTHER; PTHR24342:SF21; TRIO RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF23587; SH3_KALRN; 1.
DR Pfam; PF22697; SOS1_NGEF_PH; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00220; S_TKc; 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; PS50835; IG_LIKE; 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000242450};
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 156..221
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 290..380
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 401..707
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 79..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 756 AA; 83096 MW; 2AE39C2BDA3B766B CRC64;
MMNVGRLQGF DGKIVAQGKL LLQDTFLVTD QDTGLLPRCK ERRVFLFEQI VIFSEPLDKK
KGFSMPGFLF KNSIKEPLPP SSPLQKGGSF WSSVPASPAS RPGSFTFPGD SDSLQRQARR
HGAPGKDADR MSTCSSASEQ SVQSTQSNGS ESSSSSSIST MLVTHDYTAV KEDEINVYQG
EVVQILASNQ QNMFLVFRAA TDQCPAAEGW IPGFVLGHTS AVIMENPDGT LKKSTSWHTA
LRLRKKSEKK DKDGKREGKL ENGYRKSREG LSNKVSVKLL NPNYIYDVPP EFVIPLSEVT
CEAGETVVLR CRVCGRPKAS ITWKGPEHNT LSNDGHYSIS YSDLGEAALK IVGVTTEDDG
IYTCIAVNDM GSASSSASLR VLGPGSDGIV VTWKDNFDCF YSEVAELGRG RFSVVKKCDQ
KGTKRAVATK FVNKKLMKRD QVTHELGILQ NLQHPLLGSR WNLFSLFSPI AGPSALPSLP
RRCVLGRGRV SGPGPASQPR LLARLCCLKG RRGVVPRRCS DIGSGVRRAD QGRLLDCVVR
WGNLTEGKIR AYLGEVLEAV RYLHNCRIAH LDLKPENILV DQSSAKPTIK LADFGDAVQL
NTTYHIHPLL GNPEFAAPEI ILGNPVSLTS DTWSVGVLAY VLLSGVSPFL DDSVEETCLN
ICRLDFSFPE DYFQGVSQRA KDFVCFLLHE DPAKRPSAAS ALQERWLQAG HGHGKGAGVL
DTSRLTSFIE RRKHQNDVRP IRSMKNFLQS RLLPRV
//
