ID U6D4D5_NEOVI Unreviewed; 932 AA.
AC U6D4D5;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE Flags: Fragment;
GN Name=ERN1 {ECO:0000313|EMBL:CCP77466.1};
OS Neovison vison (American mink) (Mustela vison).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Neogale.
OX NCBI_TaxID=452646 {ECO:0000313|EMBL:CCP77466.1};
RN [1] {ECO:0000313|EMBL:CCP77466.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Pool of brain {ECO:0000313|EMBL:CCP77466.1};
RA Anistoroaei R., Christensen K.;
RT "An American mink transcriptome.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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 EMBL; HAAF01005642; CCP77466.1; -; mRNA.
DR AlphaFoldDB; U6D4D5; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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:0004521; F:RNA endonuclease activity; IEA:InterPro.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0010468; P:regulation of gene expression; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
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 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CCP77466.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..932
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004668031"
FT DOMAIN 564..825
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 828..932
FT /note="KEN"
FT /evidence="ECO:0000259|PROSITE:PS51392"
FT REGION 491..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..540
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCP77466.1"
FT NON_TER 932
FT /evidence="ECO:0000313|EMBL:CCP77466.1"
SQ SEQUENCE 932 AA; 104713 MW; 0FA55AA0F83611BB CRC64;
LLVLLALPLP RPGVLGRPST VTLPETLLFV STLDGSLHAV SKRTGSIKWT LKEDPVLQVP
THVEEPAFLP DPNDGSLYTL GGKNNEGLTK LPFTIPELVQ ASPCRSSEGI LYMGKKQDIW
YVIDLLTGEK QQTLSSAFAD SLCPSTSLLY LGRTEYTITM YDTKTRELRW NATYFDYAAS
LPEDDGDYKM SHFVSNGDGL VVTVDSESGD VLWIQNYASP VVAFYVWQRE GLKKVLHINV
AVETLRYLTF MSGEVGRITK WKYPFPKETE AKSKLTPTLY VGKYSTSLYA SPSMVHDGVA
VVPRGSTLPL LEGPQTDGVT IGDKGECVIT PSTDVNFDPG LKGKNKLNYL RNYWLLIGHH
ETPLSASTKM LERFPNNLPK HRENVIPADS EKKSFEEVIN LVDQTSENAP TTISQDVEEK
YERAPAKPEA PMDSVLKDIA TIILSTFLLI GWVAFIITYP LSMHQQQQLQ HQQFQKELEK
IQLLQQQQLP FHPPGDVAQD AEPLDSSGLY SESSGTSSPS TSPRASNHSL HSSGSASRPG
SGPFPEQDDD DEETNMVIVG KISFCPKDVL GHGAEGTIVY RGMFDNRDVA VKRILPECFS
FADREVQLLR ESDEHPNVIR YFCTERDRQF QYIAIELCAA TLQEYVEQKD FAHLGLEPIT
LLQQTTSGLA HLHSLNIVHR DLKPHNILLS MPNAHGRIKA MISDFGLCKK LAVGRHSFSR
RSGVPGTEGW IAPEMLSEDC KDNPTYTVDI FSAGCVFYYV ISEGSHPFGK SLQRQANILL
GAYSLDCLHP EKHEDVIARE LIENMIAMEP QKRPSAKHVL KHPFFWSLEK QLQFFQDVSD
RIEKESLDGP IVKQLERGGR AVVKMDWREN ITVPLQTDLR KFRTYKGGSV RDLLRAMRNK
KHHYRELPTE VRETLGSLPD DFVRYFTSRF PP
//