ID G3WME2_SARHA Unreviewed; 980 AA.
AC G3WME2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 2.
DT 27-MAR-2024, entry version 68.
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:ENSSHAP00000016597.2};
OS Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000016597.2, ECO:0000313|Proteomes:UP000007648};
RN [1] {ECO:0000313|Ensembl:ENSSHAP00000016597.2, ECO:0000313|Proteomes:UP000007648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA Jones M.E., Schuster S.C.;
RT "Genetic diversity and population structure of the endangered marsupial
RT Sarcophilus harrisii (Tasmanian devil).";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN [2] {ECO:0000313|Ensembl:ENSSHAP00000016597.2}
RP IDENTIFICATION.
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; G3WME2; -.
DR STRING; 9305.ENSSHAP00000016597; -.
DR Ensembl; ENSSHAT00000016737.2; ENSSHAP00000016597.2; ENSSHAG00000014118.2.
DR eggNOG; KOG1027; Eukaryota.
DR GeneTree; ENSGT00940000159761; -.
DR HOGENOM; CLU_004875_1_1_1; -.
DR InParanoid; G3WME2; -.
DR TreeFam; TF313986; -.
DR Proteomes; UP000007648; 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:UP000007648};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..980
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5029847635"
FT DOMAIN 574..835
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 838..966
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 504..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 110934 MW; EFEC84089B453A9C CRC64;
MPVPLRRLLQ LLALLLLPLP GPGSFGSTST VTLPETLLFV STLDGSLHAV SKRTGSTKWT
LKEDPVLQVP THVEEPAFLP DPNDGSLYTL GGKNNEGLTK LPFTIPELVQ ASPCRSSDGI
LYMGKKQDIW YVVDLMTGEK QQTLSSAFAE SLCPSTSLLY LGRTEYTITM YDTKNRELRW
NATYFDYAAN VPEEDMEYKM SHFVSNGDGL VVTVDSESGD VLWIQNYASP VVAFYIWHRE
GLQKVMHTNV GVETLRYLTF MSGEVGRITK WKYPFPKETE TKSKLTPTLY VGRYSTSLYA
SPSMVHEGVA IVPRGSAFPQ LEGPQTDGVT IKNNEECVIT PSIDLNIDFG IKGKNKLNYW
TNYWLLIGHH EIPLSASTTV LEKFPNKLPR HRENVIHADS EKSFEEKVIK IVDRDTEEPT
PATHQDIEFT RTPVKTEAAV DSILKDMATI ILCTFLLIGW VAFVITYPMS MHQQQQLQHQ
QFQRQLEERI QLLQQQQLPF QTPGDLAQDS DFLDTSAGLH SESSAPSSPN MSPKGSNHSQ
HSSNSASKVS GSITTEQDED DEETSMVVVG KISFCPKDVL GHGAEGTIVY RGMFDNRAVA
VKRILPECFS FADREVQLLR ESDEHPNVIR YFCTERDRQF QYIAIELCAA TLQEYVEQKD
FAHLGLEPIT LLQQTTSGLA YLHSLNIVHR DLKPHNILLS MPNAHGKIKA MISDFGLCKK
LAVGRHSFSR RSGVPGTEGW IAPEMLSEDC KENPTYTVDI FSAGCVFYYV ISDGNHPFGK
SLQRQANILL GAYSLNCLHP EKHEDIVAHE LIEKMIAMDP QKRPSAKHVL KHPFFWGLEK
QLQFFQDVSD RIEKEALDGP IVKQLERGGR MVVKMDWREN ITVPLQTDLR KFRTYKGGSV
RDLLRAMRNK KHHYRELPED VQETLGSIPD DFVRYFTSRF PHLLSHTYRA MELCSHERLF
QPYYFQEATE LDPPVTNDGL
//
