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Database: UniProt
Entry: L5KL93_PTEAL
LinkDB: L5KL93_PTEAL
Original site: L5KL93_PTEAL 
ID   L5KL93_PTEAL            Unreviewed;       664 AA.
AC   L5KL93;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Serine/threonine-protein kinase/endoribonuclease IRE2 {ECO:0000313|EMBL:ELK12097.1};
GN   ORFNames=PAL_GLEAN10004943 {ECO:0000313|EMBL:ELK12097.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK12097.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
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; KB030664; ELK12097.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5KL93; -.
DR   STRING; 9402.L5KL93; -.
DR   InParanoid; L5KL93; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
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-EC.
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; 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   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   PANTHER; PTHR13954; IRE1-RELATED; 1.
DR   PANTHER; PTHR13954:SF15; SERINE_THREONINE-PROTEIN KINASE_ENDORIBONUCLEASE IRE2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF06479; Ribonuc_2-5A; 1.
DR   SMART; SM00564; PQQ; 1.
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, ECO:0000313|EMBL:ELK12097.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
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..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..664
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003969256"
FT   DOMAIN          258..519
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          522..650
FT                   /note="KEN"
FT                   /evidence="ECO:0000259|PROSITE:PS51392"
FT   REGION          161..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   664 AA;  72518 MW;  5F63190416121137 CRC64;
     MEIAAGGSSR WPPLALQLQL AALLGTLAPQ AQTLRPESLL LVSTLDGSLH ALSKQTGDLK
     WTLKDDPAIQ GPTYVTEMTL YVGKDEAGFY VSKALVHTGV ALVPRGLTLA SMDGPTTDEV
     TLQVSGEREG SPSTAVRYPS GSVALPSQWL LIGHHEPPPV LHTTMLRVHP TPGSGTPETR
     PSASMQPPAL FTEQQQQQLA EKQQQAPLKP AHPPLNSQNV PSQPSGVTPQ DKKRLQSPSE
     PTEDPEAEQL TVVGKISFNP RDVLGRGAGG TFVFRGQFEG RAVAVKRLLR ECFSLVRREV
     ELLQESDRHP NVLRYFCTER GPQFHYIALE LCRASLQEYV ENPELDRWGL EPVTALQQLT
     SGLAHLHSLH IVHRDLKPAN ILISGPDSQG QGRVVLSDFG LCKKLPAGHC SFSLHSGVPG
     TEGWMAPELL QLQPPESPTS AVDVFSAGCV FYYVLSGGGH PFGESLYRQA NILAGAPRLA
     HLEEEAHDQV VARSLVEAML SPLPQARPSA PQMLAHPFFW SRAKQLQFFQ DVSDWLEKEP
     EQAPLVVALE AGGSAVVRGD WHKHISAPLQ TDLRRFRTYQ GTSVRDLLRA VRNKRHHYRE
     LPAELRQALG HVPDGFIQYF TARFPRLLLH THQAMSSCAS ESLFRPYYPP AAGAGGPSLG
     AAGS
//
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