ID G3T1Y5_LOXAF Unreviewed; 955 AA.
AC G3T1Y5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=ERN1 {ECO:0000313|Ensembl:ENSLAFP00000007139.4};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000007139.4, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000007139.4, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007139.4,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000007139.4}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000007139.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; G3T1Y5; -.
DR STRING; 9785.ENSLAFP00000007139; -.
DR Ensembl; ENSLAFT00000008505.4; ENSLAFP00000007139.4; ENSLAFG00000008504.4.
DR eggNOG; KOG1027; Eukaryota.
DR GeneTree; ENSGT00940000159761; -.
DR HOGENOM; CLU_004875_1_1_1; -.
DR InParanoid; G3T1Y5; -.
DR OMA; NYWVERF; -.
DR TreeFam; TF313986; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:1990597; C:AIP1-IRE1 complex; IEA:Ensembl.
DR GO; GO:1990630; C:IRE1-RACK1-PP2A complex; IEA:Ensembl.
DR GO; GO:1990604; C:IRE1-TRAF2-ASK1 complex; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005637; C:nuclear inner membrane; IEA:Ensembl.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:Ensembl.
DR GO; GO:0051879; F:Hsp90 protein binding; IEA:Ensembl.
DR GO; GO:0000287; F:magnesium ion binding; IEA:Ensembl.
DR GO; GO:0005161; F:platelet-derived growth factor receptor binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:RNA endonuclease activity; IEA:Ensembl.
DR GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0035924; P:cellular response to vascular endothelial growth factor stimulus; IEA:Ensembl.
DR GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:1901142; P:insulin metabolic process; IEA:Ensembl.
DR GO; GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; IEA:Ensembl.
DR GO; GO:0036498; P:IRE1-mediated unfolded protein response; IEA:Ensembl.
DR GO; GO:0070054; P:mRNA splicing, via endonucleolytic cleavage and ligation; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:1900103; P:positive regulation of endoplasmic reticulum unfolded protein response; IEA:Ensembl.
DR GO; GO:0033120; P:positive regulation of RNA splicing; IEA:Ensembl.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; IEA:Ensembl.
DR CDD; cd09769; Luminal_IRE1; 1.
DR CDD; cd10422; RNase_Ire1; 1.
DR CDD; cd13982; STKc_IRE1; 1.
DR Gene3D; 1.20.1440.180; KEN domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR045133; IRE1/2-like.
DR InterPro; IPR010513; KEN_dom.
DR InterPro; IPR038357; KEN_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR018391; PQQ_beta_propeller_repeat.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13954; IRE1-RELATED; 1.
DR PANTHER; PTHR13954:SF17; SERINE_THREONINE-PROTEIN KINASE_ENDORIBONUCLEASE IRE1; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF06479; Ribonuc_2-5A; 1.
DR SMART; SM00564; PQQ; 5.
DR SMART; SM00580; PUG; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 1.
DR PROSITE; PS51392; KEN; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 549..810
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 813..941
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 477..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 955 AA; 107759 MW; F767F314063AA791 CRC64;
GSTSTVTLPE TLLFVSTLDG SLHAVSKRTG SIKWTLKEDP VLQVPTHVEE PAFLPDPNDG
SLYTLGGKNN EGLTKLPFTI PELVQASPCR SSDGILYMGK KQDIWYVIDL LTGEKQQTLS
SAFAESLCPS TSLLYLGRTE YTITMYDTKN RELRWNATYF DYAASLPEDD MDYKMSHFVS
NGDGLVVTVD SESGDVLWIQ NYASPVVAFY VWQREGLRKV MHINVAVETL RYLTFMSGEV
GRITKWKYPF PKETEAKSKL TPTLYVGKYS TSLYASPSMV HEGVAVVPRG STLPLLEGPQ
TDGVTIGDKG ECVITPSTDL KFDPGLKGKN KLNYLRNYWL LIGHHETPLS ASTKMLERFP
NNLPKHRENV IPADSEKKSF EEVINLVDQT SETAPTTVTQ DVEEKFTHAP AKPEAPVDSM
LKDMATIILS TFLLIGWVAF IITYPLSMHQ QQQLQHQQFQ KELEKIQLLQ QQQLPFHSPV
DPAQDTELLD ISGPYSESSG TSSPSMSPRA SNHSLHMSGS ASKAGISPSL DQDDEDEETS
MVLVGKISFC PKDVLGHGAE GTIVYRGMFD NRDVAVKRIL PECFSFADRE VQLLRESDEH
PNVIRYFCTE RDRQFQYIAI ELCAATLQEY VEQKDFAHLG LEPITLLQQT TSGLAHLHSL
NIVHRDLKPH NILLSMPNAH GRIKAMISDF GLCKKLAVGR HSFSRRSGVP GTEGWIAPEM
LSEDCKENPT YTVDIFSAGC VFYYVISEGS HPFGKSLQRQ ANILLGAYSL DCLHQEKHED
VIARELIEKM IAMDPQKRPS AKHVLKHPFF WGLEKQLQFF QDVSDRIEKE SLDSPIVKQL
ERGGRAVVKM DWKENITVPL QTDLRKFRTY KGGSVRDLLR AMRNKKHHYR ELPAEVRETL
GSLPDDFVRY FTSRFPHLLL HTYRALELCS HERLFQPYYC HEPPEPQPAL PPDAL
//
