ID A0A1U7SXL2_ALLSI Unreviewed; 953 AA.
AC A0A1U7SXL2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 2.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=PRKR-like endoplasmic reticulum kinase {ECO:0000256|ARBA:ARBA00041500};
GN Name=EIF2AK3 {ECO:0000313|RefSeq:XP_006038551.2};
OS Alligator sinensis (Chinese alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=38654 {ECO:0000313|Proteomes:UP000189705, ECO:0000313|RefSeq:XP_006038551.2};
RN [1] {ECO:0000313|RefSeq:XP_006038551.2}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_006038551.2; XM_006038489.3.
DR AlphaFoldDB; A0A1U7SXL2; -.
DR KEGG; asn:102370127; -.
DR Proteomes; UP000189705; Unplaced.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0070887; P:cellular response to chemical stimulus; IEA:UniProt.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0034976; P:response to endoplasmic reticulum stress; IEA:UniProt.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR CDD; cd09768; Luminal_EIF2AK3; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11042:SF166; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE 3; 1.
DR PANTHER; PTHR11042; EUKARYOTIC TRANSLATION INITIATION FACTOR 2-ALPHA KINASE EIF2-ALPHA KINASE -RELATED; 1.
DR Pfam; PF00069; Pkinase; 2.
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; PS00107; PROTEIN_KINASE_ATP; 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, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Initiation factor {ECO:0000313|RefSeq:XP_006038551.2};
KW Kinase {ECO:0000313|RefSeq:XP_006038551.2};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Protein biosynthesis {ECO:0000313|RefSeq:XP_006038551.2};
KW Reference proteome {ECO:0000313|Proteomes:UP000189705};
KW Stress response {ECO:0000256|ARBA:ARBA00023016};
KW Transferase {ECO:0000313|RefSeq:XP_006038551.2};
KW Translation regulation {ECO:0000256|ARBA:ARBA00022845};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Unfolded protein response {ECO:0000256|ARBA:ARBA00023230}.
FT DOMAIN 440..922
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 661..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..721
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 953 AA; 108863 MW; 487426C113267B4F CRC64;
MIIPSLDGDL FQWDRDRESM EAVPFTVESL LESSYKFGED VVLVGGKSLT TYGLSSYSGK
VKYICSSVGC RRWDEDETDQ EDTLLLHRTQ KTVRAVGPRS GNEKWNFSVG HFELRYVPDI
ESRVGYIESN FKSSINKEET KIISDVEEQE AVMKDTVIKV SVADWKVMAF NKQGGHLEWE
YQFCTPIASA WLVKDGKVVP ISLFDDTSYS SDSEILEDEE DLVEAARGAT ESSVYLGMYR
GQLYLQSSVR ISEKFPTNPK ALESRNDNAI IPLPKIKWKP LIHSPSRTPV LVGSDEFDKC
LSNDKYSHEE YSNGALSVLQ YPYDNGYYLP YHKTERNKRS TQITIRFFDN MNYKNIRKKD
PVLLLHWWKE IIGTILFCIV TTTFIVRRLF HPHPHSRQRK ESETQCQTDN KYESIGGESK
DNSWSDIKNS GYVSRYLTDF EPIQCLGRGG FGVVFEARNK VDDCNYAIKR IRLPNRELAR
EKVMREVKAL AKLEHPGIVR YFNAWLEAPP ERWQEKMDEL WLKDDGTDWL LSSPSPMDGP
SFKIRTEPFT SKEHVEVITA SSQRVQSFSV GIACGQSDSS GSQFSPLEFS AADNRDFHKS
GDPMLNLQDS VLTDCDVEDS IDENDPGHSF ELCPPTMATV CLRERTSSSI VFEDSGCDNA
SAKEDNKIDT SHDDSLSEEK ATNTKDTDNR KSPSQSSLSI SPPRPTSLSL DLSKNTAKNV
KPSSPKVYLY IQMQLCRKEN LKDWMSRRCS IEERERTECL QIFLQIAEAV QFLHNKGLMH
RDLKPSNIFF TMDDIVKIGD FGLVTAMDQD EEEESVLTPM PAYARHTGQV GTKLYMSPEQ
IYGNTYSHKV DIFSLGLILF ELLYPFSTQM ERIKTLSEVR SLKFPLLFTQ KCSQEYAMVK
HMLSTNPIER PEAEDIIENP VFEDLELPTK TVLRQRSRTM SSSGNKHSRQ PSK
//