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Database: UniProt
Entry: U6D4D5_NEOVI
LinkDB: U6D4D5_NEOVI
Original site: U6D4D5_NEOVI 
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
//
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