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Database: UniProt
Entry: A0A1U7SXL2_ALLSI
LinkDB: A0A1U7SXL2_ALLSI
Original site: A0A1U7SXL2_ALLSI 
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}.
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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
//
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