GCN1_HUMAN
ID GCN1_HUMAN Reviewed; 2671 AA.
AC Q92616; A8KAY1; O95001; O95651; Q6P2S3; Q86X65; Q8N5I5; Q8WU80; Q99736;
AC Q9UE60;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 7.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=eIF-2-alpha kinase activator GCN1 {ECO:0000250|UniProtKB:E9PVA8};
DE AltName: Full=GCN1 eIF-2-alpha kinase activator homolog {ECO:0000312|HGNC:HGNC:4199};
DE AltName: Full=GCN1-like protein 1 {ECO:0000250|UniProtKB:E9PVA8};
DE AltName: Full=General control of amino-acid synthesis 1-like protein 1 {ECO:0000250|UniProtKB:E9PVA8};
DE AltName: Full=Translational activator GCN1 {ECO:0000250|UniProtKB:E9PVA8};
DE Short=HsGCN1;
GN Name=GCN1 {ECO:0000312|HGNC:HGNC:4199};
GN Synonyms=GCN1L1 {ECO:0000250|UniProtKB:E9PVA8}, KIAA0219;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Liver, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 2-13; 69-87; 221-229; 241-251; 314-323; 568-576;
RP 617-635; 822-829; 1201-1208; 1485-1496; 1604-1622; 1735-1745; 1960-1973;
RP 2093-2107; 2151-2161; 2192-2199; 2402-2418 AND 2522-2530, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=B-cell lymphoma;
RA Bienvenut W.V.;
RL Submitted (MAR-2005) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-359 AND 1678-2671.
RA Yamagata K., Oda N., Furuta H., Vaxillaire M., Southam L., Boriraj V.,
RA Chen X., Oda Y., Takeda J., Yamada S., Nishigori H., Lebeau M.M.,
RA Lathrop M., Cox R.D., Bell G.I.;
RT "Transcription map of the 5cM region surrounding the hepatocyte nuclear
RT factor-1a/MODY3 gene on chromosome 12.";
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 842-2671, AND TISSUE SPECIFICITY.
RC TISSUE=Skeletal muscle;
RX PubMed=9234705; DOI=10.1128/mcb.17.8.4474;
RA Marton M.J., Vazquez de Aldana C.R., Qiu H., Chakraburtty K.,
RA Hinnebusch A.G.;
RT "Evidence that GCN1 and GCN20, translational regulators of GCN4, function
RT on elongating ribosomes in activation of eIF2alpha kinase GCN2.";
RL Mol. Cell. Biol. 17:4474-4489(1997).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-786, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-729; SER-786 AND SER-2276,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Acts as a positive activator of the EIF2AK4/GCN2 protein
CC kinase activity in response to amino acid starvation. Forms a complex
CC with EIF2AK4/GCN2 on translating ribosomes; during this process, GCN1
CC seems to act as a chaperone to facilitate delivery of uncharged tRNAs
CC that enter the A site of ribosomes to the tRNA-binding domain of
CC EIF2AK4/GCN2, and hence stimulating EIF2AK4/GCN2 kinase activity.
CC Participates in the repression of global protein synthesis and in gene-
CC specific mRNA translation activation, such as the transcriptional
CC activator ATF4, by promoting the EIF2AK4/GCN2-mediated phosphorylation
CC of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on
CC 'Ser-52', and hence allowing ATF4-mediated reprogramming of amino acid
CC biosynthetic gene expression to alleviate nutrient depletion.
CC {ECO:0000250|UniProtKB:E9PVA8, ECO:0000250|UniProtKB:P33892}.
CC -!- SUBUNIT: Interacts with EIF2AK4/GCN2; this interaction stimulates the
CC EIF2AK4/GCN2 kinase activity and is impaired by IMPACT upon a variety
CC of stress conditions, such as amino acid depletion, UV-C irradiation,
CC proteasome inhibitor treatment and glucose deprivation. Interacts with
CC IMPACT; this prevents the interaction of GCN1 with EIF2AK4/GCN2 and
CC inhibits EIF2AK4/GCN2 kinase activity. {ECO:0000250|UniProtKB:E9PVA8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:E9PVA8}.
CC Note=Associates with ribosomes in undifferentiated neuroblastoma cells
CC and increases after neuronal differentiation.
CC {ECO:0000250|UniProtKB:E9PVA8}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:9039502). Expressed
CC in skeletal muscules, ovary and testis (PubMed:9234705).
CC {ECO:0000269|PubMed:9039502, ECO:0000269|PubMed:9234705}.
CC -!- SIMILARITY: Belongs to the GCN1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC51648.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA13209.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D86973; BAA13209.2; ALT_INIT; mRNA.
DR EMBL; AC004812; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF459556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF511175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC004263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC021129; AAH21129.1; -; mRNA.
DR EMBL; BC032335; AAH32335.1; -; mRNA.
DR EMBL; BC046177; AAH46177.1; -; mRNA.
DR EMBL; BC064346; AAH64346.1; -; mRNA.
DR EMBL; BC153881; AAI53882.1; -; mRNA.
DR EMBL; U88836; AAD00655.1; -; mRNA.
DR EMBL; U88837; AAD00656.1; -; mRNA.
DR EMBL; U77700; AAC51648.1; ALT_FRAME; mRNA.
DR CCDS; CCDS41847.1; -.
DR RefSeq; NP_006827.1; NM_006836.1.
DR AlphaFoldDB; Q92616; -.
DR BioGRID; 116181; 258.
DR CORUM; Q92616; -.
DR IntAct; Q92616; 114.
DR MINT; Q92616; -.
DR STRING; 9606.ENSP00000300648; -.
DR ChEMBL; CHEMBL3706558; -.
DR CarbonylDB; Q92616; -.
DR GlyGen; Q92616; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92616; -.
DR MetOSite; Q92616; -.
DR PhosphoSitePlus; Q92616; -.
DR SwissPalm; Q92616; -.
DR BioMuta; GCN1; -.
DR DMDM; 296439506; -.
DR EPD; Q92616; -.
DR jPOST; Q92616; -.
DR MassIVE; Q92616; -.
DR MaxQB; Q92616; -.
DR PaxDb; Q92616; -.
DR PeptideAtlas; Q92616; -.
DR PRIDE; Q92616; -.
DR ProteomicsDB; 75364; -.
DR Antibodypedia; 9618; 80 antibodies from 15 providers.
DR DNASU; 10985; -.
DR Ensembl; ENST00000300648.7; ENSP00000300648.6; ENSG00000089154.11.
DR GeneID; 10985; -.
DR KEGG; hsa:10985; -.
DR MANE-Select; ENST00000300648.7; ENSP00000300648.6; NM_006836.2; NP_006827.1.
DR UCSC; uc001txo.4; human.
DR CTD; 10985; -.
DR DisGeNET; 10985; -.
DR GeneCards; GCN1; -.
DR HGNC; HGNC:4199; GCN1.
DR HPA; ENSG00000089154; Low tissue specificity.
DR MIM; 605614; gene.
DR neXtProt; NX_Q92616; -.
DR OpenTargets; ENSG00000089154; -.
DR PharmGKB; PA28616; -.
DR VEuPathDB; HostDB:ENSG00000089154; -.
DR eggNOG; KOG1242; Eukaryota.
DR GeneTree; ENSGT00940000153612; -.
DR HOGENOM; CLU_000504_2_2_1; -.
DR InParanoid; Q92616; -.
DR OrthoDB; 160593at2759; -.
DR PhylomeDB; Q92616; -.
DR TreeFam; TF105398; -.
DR PathwayCommons; Q92616; -.
DR Reactome; R-HSA-9633012; Response of EIF2AK4 (GCN2) to amino acid deficiency.
DR SignaLink; Q92616; -.
DR BioGRID-ORCS; 10985; 339 hits in 1090 CRISPR screens.
DR ChiTaRS; GCN1; human.
DR GeneWiki; GCN1L1; -.
DR GenomeRNAi; 10985; -.
DR Pharos; Q92616; Tbio.
DR PRO; PR:Q92616; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q92616; protein.
DR Bgee; ENSG00000089154; Expressed in ventricular zone and 211 other tissues.
DR Genevisible; Q92616; HS.
DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005844; C:polysome; ISS:UniProtKB.
DR GO; GO:0005840; C:ribosome; NAS:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0019887; F:protein kinase regulator activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008135; F:translation factor activity, RNA binding; NAS:UniProtKB.
DR GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
DR GO; GO:1990253; P:cellular response to leucine starvation; ISS:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IEA:InterPro.
DR GO; GO:0036003; P:positive regulation of transcription from RNA polymerase II promoter in response to stress; ISS:UniProtKB.
DR GO; GO:0006417; P:regulation of translation; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 7.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR033173; Gcn1.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR034085; TOG.
DR PANTHER; PTHR23346:SF7; PTHR23346:SF7; 1.
DR SMART; SM01349; TOG; 1.
DR SUPFAM; SSF48371; SSF48371; 5.
DR PROSITE; PS50077; HEAT_REPEAT; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Phosphoprotein; Reference proteome; Repeat; Stress response;
KW Translation regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052, ECO:0000269|Ref.5,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895"
FT CHAIN 2..2671
FT /note="eIF-2-alpha kinase activator GCN1"
FT /id="PRO_0000087443"
FT REPEAT 140..178
FT /note="HEAT 1"
FT /evidence="ECO:0000255"
FT REPEAT 257..293
FT /note="HEAT 2"
FT /evidence="ECO:0000255"
FT REPEAT 294..331
FT /note="HEAT 3"
FT /evidence="ECO:0000255"
FT REPEAT 385..423
FT /note="HEAT 4"
FT /evidence="ECO:0000255"
FT REPEAT 425..459
FT /note="HEAT 5"
FT /evidence="ECO:0000255"
FT REPEAT 460..503
FT /note="HEAT 6"
FT /evidence="ECO:0000255"
FT REPEAT 560..597
FT /note="HEAT 7"
FT /evidence="ECO:0000255"
FT REPEAT 599..636
FT /note="HEAT 8"
FT /evidence="ECO:0000255"
FT REPEAT 697..732
FT /note="HEAT 9"
FT /evidence="ECO:0000255"
FT REPEAT 733..770
FT /note="HEAT 10"
FT /evidence="ECO:0000255"
FT REPEAT 879..925
FT /note="HEAT 11"
FT /evidence="ECO:0000255"
FT REPEAT 979..1016
FT /note="HEAT 12"
FT /evidence="ECO:0000255"
FT REPEAT 1035..1072
FT /note="HEAT 13"
FT /evidence="ECO:0000255"
FT REPEAT 1078..1115
FT /note="HEAT 14"
FT /evidence="ECO:0000255"
FT REPEAT 1155..1192
FT /note="HEAT 15"
FT /evidence="ECO:0000255"
FT REPEAT 1210..1250
FT /note="HEAT 16"
FT /evidence="ECO:0000255"
FT REPEAT 1251..1289
FT /note="HEAT 17"
FT /evidence="ECO:0000255"
FT REPEAT 1290..1332
FT /note="HEAT 18"
FT /evidence="ECO:0000255"
FT REPEAT 1335..1372
FT /note="HEAT 19"
FT /evidence="ECO:0000255"
FT REPEAT 1374..1410
FT /note="HEAT 20"
FT /evidence="ECO:0000255"
FT REPEAT 1413..1451
FT /note="HEAT 21"
FT /evidence="ECO:0000255"
FT REPEAT 1455..1492
FT /note="HEAT 22"
FT /evidence="ECO:0000255"
FT REPEAT 1493..1530
FT /note="HEAT 23"
FT /evidence="ECO:0000255"
FT REPEAT 1534..1571
FT /note="HEAT 24"
FT /evidence="ECO:0000255"
FT REPEAT 1573..1609
FT /note="HEAT 25"
FT /evidence="ECO:0000255"
FT REPEAT 1611..1648
FT /note="HEAT 26"
FT /evidence="ECO:0000255"
FT REPEAT 1653..1690
FT /note="HEAT 27"
FT /evidence="ECO:0000255"
FT REPEAT 1692..1729
FT /note="HEAT 28"
FT /evidence="ECO:0000255"
FT REPEAT 1731..1769
FT /note="HEAT 29"
FT /evidence="ECO:0000255"
FT REPEAT 1773..1810
FT /note="HEAT 30"
FT /evidence="ECO:0000255"
FT REPEAT 1812..1848
FT /note="HEAT 31"
FT /evidence="ECO:0000255"
FT REPEAT 1921..1958
FT /note="HEAT 32"
FT /evidence="ECO:0000255"
FT REPEAT 1959..1996
FT /note="HEAT 33"
FT /evidence="ECO:0000255"
FT REPEAT 2001..2038
FT /note="HEAT 34"
FT /evidence="ECO:0000255"
FT REPEAT 2039..2076
FT /note="HEAT 35"
FT /evidence="ECO:0000255"
FT REPEAT 2078..2106
FT /note="HEAT 36"
FT /evidence="ECO:0000255"
FT REPEAT 2107..2146
FT /note="HEAT 37"
FT /evidence="ECO:0000255"
FT REPEAT 2147..2184
FT /note="HEAT 38"
FT /evidence="ECO:0000255"
FT REPEAT 2188..2225
FT /note="HEAT 39"
FT /evidence="ECO:0000255"
FT REPEAT 2259..2296
FT /note="HEAT 40"
FT /evidence="ECO:0000255"
FT REPEAT 2301..2338
FT /note="HEAT 41"
FT /evidence="ECO:0000255"
FT REPEAT 2339..2380
FT /note="HEAT 42"
FT /evidence="ECO:0000255"
FT REPEAT 2382..2417
FT /note="HEAT 43"
FT /evidence="ECO:0000255"
FT REPEAT 2422..2459
FT /note="HEAT 44"
FT /evidence="ECO:0000255"
FT REPEAT 2546..2583
FT /note="HEAT 45"
FT /evidence="ECO:0000255"
FT REPEAT 2588..2625
FT /note="HEAT 46"
FT /evidence="ECO:0000255"
FT REPEAT 2627..2661
FT /note="HEAT 47; degenerate"
FT /evidence="ECO:0000255"
FT COILED 804..863
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:25489052, ECO:0000269|Ref.5,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895"
FT MOD_RES 729
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 2276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 2155
FT /note="D -> Y (in dbSNP:rs3864938)"
FT /id="VAR_062228"
FT CONFLICT 292
FT /note="L -> F (in Ref. 1; BAA13209 and 4; AAI53882)"
FT /evidence="ECO:0000305"
FT CONFLICT 842
FT /note="A -> G (in Ref. 7; AAC51648)"
FT /evidence="ECO:0000305"
FT CONFLICT 1584
FT /note="A -> V (in Ref. 7; AAC51648)"
FT /evidence="ECO:0000305"
FT CONFLICT 1683
FT /note="A -> V (in Ref. 7; AAC51648)"
FT /evidence="ECO:0000305"
FT CONFLICT 1760
FT /note="F -> S (in Ref. 6; AAD00655)"
FT /evidence="ECO:0000305"
FT CONFLICT 2298
FT /note="A -> V (in Ref. 7; AAC51648)"
FT /evidence="ECO:0000305"
FT CONFLICT 2486
FT /note="S -> T (in Ref. 6; AAD00655)"
FT /evidence="ECO:0000305"
FT CONFLICT 2549
FT /note="A -> R (in Ref. 7; AAC51648)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2671 AA; 292710 MW; FC34F505103A0158 CRC64;
MAADTQVSET LKRFAGKVTT ASVKERREIL SELGKCVAGK DLPEGAVKGL CKLFCLTLHR
YRDAASRRAL QAAIQQLAEA QPEATAKNLL HSLQSSGIGS KAGVPSKSSG SAALLALTWT
CLLVRIVFPS RAKRQGDIWN KLVEVQCLLL LEVLGGSHKH AVDGAVKKLT KLWKENPGLV
EQYLSAILSL EPNQNYAGML GLLVQFCTSH KEMDVVSQHK SALLDFYMKN ILMSKVKPPK
YLLDSCAPLL RYLSHSEFKD LILPTIQKSL LRSPENVIET ISSLLASVTL DLSQYAMDIV
KGLAGHLKSN SPRLMDEAVL ALRNLARQCS DSSAMESLTK HLFAILGGSE GKLTVVAQKM
SVLSGIGSVS HHVVSGPSSQ VLNGIVAELF IPFLQQEVHE GTLVHAVSVL ALWCNRFTME
VPKKLTEWFK KAFSLKTSTS AVRHAYLQCM LASYRGDTLL QALDLLPLLI QTVEKAASQS
TQVPTITEGV AAALLLLKLS VADSQAEAKL SSFWQLIVDE KKQVFTSEKF LVMASEDALC
TVLHLTERLF LDHPHRLTGN KVQQYHRALV AVLLSRTWHV RRQAQQTVRK LLSSLGGFKL
AHGLLEELKT VLSSHKVLPL EALVTDAGEV TEAGKAYVPP RVLQEALCVI SGVPGLKGDV
TDTEQLAQEM LIISHHPSLV AVQSGLWPAL LARMKIDPEA FITRHLDQII PRMTTQSPLN
QSSMNAMGSL SVLSPDRVLP QLISTITASV QNPALRLVTR EEFAIMQTPA GELYDKSIIQ
SAQQDSIKKA NMKRENKAYS FKEQIIELEL KEEIKKKKGI KEEVQLTSKQ KEMLQAQLDR
EAQVRRRLQE LDGELEAALG LLDIILAKNP SGLTQYIPVL VDSFLPLLKS PLAAPRIKNP
FLSLAACVMP SRLKALGTLV SHVTLRLLKP ECVLDKSWCQ EELSVAVKRA VMLLHTHTIT
SRVGKGEPGA APLSAPAFSL VFPFLKMVLT EMPHHSEEEE EWMAQILQIL TVQAQLRASP
NTPPGRVDEN GPELLPRVAM LRLLTWVIGT GSPRLQVLAS DTLTTLCASS SGDDGCAFAE
QEEVDVLLCA LQSPCASVRE TVLRGLMELH MVLPAPDTDE KNGLNLLRRL WVVKFDKEEE
IRKLAERLWS MMGLDLQPDL CSLLIDDVIY HEAAVRQAGA EALSQAVARY QRQAAEVMGR
LMEIYQEKLY RPPPVLDALG RVISESPPDQ WEARCGLALA LNKLSQYLDS SQVKPLFQFF
VPDALNDRHP DVRKCMLDAA LATLNTHGKE NVNSLLPVFE EFLKNAPNDA SYDAVRQSVV
VLMGSLAKHL DKSDPKVKPI VAKLIAALST PSQQVQESVA SCLPPLVPAI KEDAGGMIQR
LMQQLLESDK YAERKGAAYG LAGLVKGLGI LSLKQQEMMA ALTDAIQDKK NFRRREGALF
AFEMLCTMLG KLFEPYVVHV LPHLLLCFGD GNQYVREAAD DCAKAVMSNL SAHGVKLVLP
SLLAALEEES WRTKAGSVEL LGAMAYCAPK QLSSCLPNIV PKLTEVLTDS HVKVQKAGQQ
ALRQIGSVIR NPEILAIAPV LLDALTDPSR KTQKCLQTLL DTKFVHFIDA PSLALIMPIV
QRAFQDRSTD TRKMAAQIIG NMYSLTDQKD LAPYLPSVTP GLKASLLDPV PEVRTVSAKA
LGAMVKGMGE SCFEDLLPWL METLTYEQSS VDRSGAAQGL AEVMAGLGVE KLEKLMPEIV
ATASKVDIAP HVRDGYIMMF NYLPITFGDK FTPYVGPIIP CILKALADEN EFVRDTALRA
GQRVISMYAE TAIALLLPQL EQGLFDDLWR IRFSSVQLLG DLLFHISGVT GKMTTETASE
DDNFGTAQSN KAIITALGVE RRNRVLAGLY MGRSDTQLVV RQASLHVWKI VVSNTPRTLR
EILPTLFGLL LGFLASTCAD KRTIAARTLG DLVRKLGEKI LPEIIPILEE GLRSQKSDER
QGVCIGLSEI MKSTSRDAVL YFSESLVPTA RKALCDPLEE VREAAAKTFE QLHSTIGHQA
LEDILPFLLK QLDDEEVSEF ALDGLKQVMA IKSRVVLPYL VPKLTTPPVN TRVLAFLSSV
AGDALTRHLG VILPAVMLAL KEKLGTPDEQ LEMANCQAVI LSVEDDTGHR IIIEDLLEAT
RSPEVGMRQA AAIILNIYCS RSKADYTSHL RSLVSGLIRL FNDSSPVVLE ESWDALNAIT
KKLDAGNQLA LIEELHKEIR LIGNESKGEH VPGFCLPKKG VTSILPVLRE GVLTGSPEQK
EEAAKALGLV IRLTSADALR PSVVSITGPL IRILGDRFSW NVKAALLETL SLLLAKVGIA
LKPFLPQLQT TFTKALQDSN RGVRLKAADA LGKLISIHIK VDPLFTELLN GIRAMEDPGV
RDTMLQALRF VIQGAGAKVD AVIRKNIVSL LLSMLGHDED NTRISSAGCL GELCAFLTEE
ELSAVLQQCL LADVSGIDWM VRHGRSLALS VAVNVAPGRL CAGRYSSDVQ EMILSSATAD
RIPIAVSGVR GMGFLMRHHI ETGGGQLPAK LSSLFVKCLQ NPSSDIRLVA EKMIWWANKD
PLPPLDPQAI KPILKALLDN TKDKNTVVRA YSDQAIVNLL KMRQGEEVFQ SLSKILDVAS
LEVLNEVNRR SLKKLASQAD STEQVDDTIL T
