ULK2_HUMAN
ID ULK2_HUMAN Reviewed; 1036 AA.
AC Q8IYT8; A8MY69; O75119;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Serine/threonine-protein kinase ULK2;
DE EC=2.7.11.1;
DE AltName: Full=Unc-51-like kinase 2;
GN Name=ULK2; Synonyms=KIAA0623;
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 VARIANT MET-370.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-370.
RC TISSUE=Testis;
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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, AUTOPHOSPHORYLATION, INTERACTION WITH
RP ATG13, DOMAIN, AND MUTAGENESIS OF LYS-39.
RX PubMed=18936157; DOI=10.1128/mcb.01082-08;
RA Chan E.Y.W., Longatti A., McKnight N.C., Tooze S.A.;
RT "Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-
RT terminal domains using an Atg13-independent mechanism.";
RL Mol. Cell. Biol. 29:157-171(2009).
RN [5]
RP FUNCTION.
RX PubMed=21460635; DOI=10.4161/auto.7.7.15450;
RA Lee E.J., Tournier C.;
RT "The requirement of uncoordinated 51-like kinase 1 (ULK1) and ULK2 in the
RT regulation of autophagy.";
RL Autophagy 7:689-695(2011).
RN [6]
RP FUNCTION IN PHOSPHORYLATION OF AMPK.
RX PubMed=21460634; DOI=10.4161/auto.7.7.15451;
RA Loffler A.S., Alers S., Dieterle A.M., Keppeler H., Franz-Wachtel M.,
RA Kundu M., Campbell D.G., Wesselborg S., Alessi D.R., Stork B.;
RT "Ulk1-mediated phosphorylation of AMPK constitutes a negative regulatory
RT feedback loop.";
RL Autophagy 7:696-706(2011).
RN [7]
RP FUNCTION, AND INTERACTION WITH RPTOR.
RX PubMed=21795849; DOI=10.4161/auto.7.10.16660;
RA Jung C.H., Seo M., Otto N.M., Kim D.H.;
RT "ULK1 inhibits the kinase activity of mTORC1 and cell proliferation.";
RL Autophagy 7:1212-1221(2011).
RN [8]
RP FUNCTION.
RX PubMed=21690395; DOI=10.1073/pnas.1107969108;
RA Cheong H., Lindsten T., Wu J., Lu C., Thompson C.B.;
RT "Ammonia-induced autophagy is independent of ULK1/ULK2 kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:11121-11126(2011).
RN [9]
RP PHOSPHORYLATION BY AMPK.
RX PubMed=21205641; DOI=10.1126/science.1196371;
RA Egan D.F., Shackelford D.B., Mihaylova M.M., Gelino S., Kohnz R.A.,
RA Mair W., Vasquez D.S., Joshi A., Gwinn D.M., Taylor R., Asara J.M.,
RA Fitzpatrick J., Dillin A., Viollet B., Kundu M., Hansen M., Shaw R.J.;
RT "Phosphorylation of ULK1 (hATG1) by AMP-activated protein kinase connects
RT energy sensing to mitophagy.";
RL Science 331:456-461(2011).
RN [10]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-242; GLU-627; VAL-662; ARG-752 AND
RP GLU-842.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Serine/threonine-protein kinase involved in autophagy in
CC response to starvation. Acts upstream of phosphatidylinositol 3-kinase
CC PIK3C3 to regulate the formation of autophagophores, the precursors of
CC autophagosomes. Part of regulatory feedback loops in autophagy: acts
CC both as a downstream effector and a negative regulator of mammalian
CC target of rapamycin complex 1 (mTORC1) via interaction with RPTOR.
CC Activated via phosphorylation by AMPK, also acts as a negative
CC regulator of AMPK through phosphorylation of the AMPK subunits PRKAA1,
CC PRKAB2 and PRKAG1. May phosphorylate ATG13/KIAA0652, FRS2, FRS3 and
CC RPTOR; however such data need additional evidences. Not involved in
CC ammonia-induced autophagy or in autophagic response of cerebellar
CC granule neurons (CGN) to low potassium concentration. Plays a role
CC early in neuronal differentiation and is required for granule cell axon
CC formation: may govern axon formation via Ras-like GTPase signaling and
CC through regulation of the Rab5-mediated endocytic pathways within
CC developing axons. {ECO:0000269|PubMed:18936157,
CC ECO:0000269|PubMed:21460634, ECO:0000269|PubMed:21460635,
CC ECO:0000269|PubMed:21690395, ECO:0000269|PubMed:21795849}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts with SYNGAP1 (By similarity). Component of a complex
CC consisting of ATG13/KIAA0652, ULK1 and RB1CC1/FIP200. Interacts (via C-
CC terminus) with ATG13/KIAA0652. Associates with the mammalian target of
CC rapamycin complex 1 (mTORC1) through an interaction with RPTOR.
CC {ECO:0000250, ECO:0000269|PubMed:18936157,
CC ECO:0000269|PubMed:21795849}.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane
CC {ECO:0000269|PubMed:18936157}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18936157}. Note=Localizes to pre-autophagosomal
CC membrane.
CC -!- DOMAIN: The CTD-like region mediates membrane-binding and incorporation
CC into large protein complexes. {ECO:0000269|PubMed:18936157}.
CC -!- PTM: Autophosphorylated. In response to nutrient limitation, probably
CC phosphorylated and activated by AMPK, leading to activate autophagy.
CC {ECO:0000269|PubMed:21205641}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31598.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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 EMBL; AB014523; BAA31598.2; ALT_INIT; mRNA.
DR EMBL; AC005722; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034988; AAH34988.1; -; mRNA.
DR CCDS; CCDS11213.1; -.
DR RefSeq; NP_001136082.1; NM_001142610.1.
DR RefSeq; NP_055498.3; NM_014683.3.
DR PDB; 6QAT; X-ray; 2.77 A; A/B/C/D=1-276.
DR PDB; 6QAU; X-ray; 2.48 A; A/B/C=1-276.
DR PDB; 6QAV; X-ray; 2.05 A; A/B/C/D=1-276.
DR PDB; 6YID; X-ray; 2.70 A; A/B/C/D=1-276.
DR PDBsum; 6QAT; -.
DR PDBsum; 6QAU; -.
DR PDBsum; 6QAV; -.
DR PDBsum; 6YID; -.
DR AlphaFoldDB; Q8IYT8; -.
DR SMR; Q8IYT8; -.
DR BioGRID; 115058; 24.
DR CORUM; Q8IYT8; -.
DR IntAct; Q8IYT8; 52.
DR STRING; 9606.ENSP00000378914; -.
DR BindingDB; Q8IYT8; -.
DR ChEMBL; CHEMBL5435; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q8IYT8; -.
DR GuidetoPHARMACOLOGY; 2272; -.
DR GlyGen; Q8IYT8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IYT8; -.
DR PhosphoSitePlus; Q8IYT8; -.
DR BioMuta; ULK2; -.
DR DMDM; 296453001; -.
DR EPD; Q8IYT8; -.
DR jPOST; Q8IYT8; -.
DR MassIVE; Q8IYT8; -.
DR MaxQB; Q8IYT8; -.
DR PaxDb; Q8IYT8; -.
DR PeptideAtlas; Q8IYT8; -.
DR PRIDE; Q8IYT8; -.
DR ProteomicsDB; 71237; -.
DR Antibodypedia; 2063; 570 antibodies from 32 providers.
DR DNASU; 9706; -.
DR Ensembl; ENST00000361658.6; ENSP00000354877.2; ENSG00000083290.20.
DR Ensembl; ENST00000395544.9; ENSP00000378914.4; ENSG00000083290.20.
DR GeneID; 9706; -.
DR KEGG; hsa:9706; -.
DR MANE-Select; ENST00000395544.9; ENSP00000378914.4; NM_014683.4; NP_055498.3.
DR UCSC; uc002gwm.5; human.
DR CTD; 9706; -.
DR DisGeNET; 9706; -.
DR GeneCards; ULK2; -.
DR HGNC; HGNC:13480; ULK2.
DR HPA; ENSG00000083290; Low tissue specificity.
DR MIM; 608650; gene.
DR neXtProt; NX_Q8IYT8; -.
DR OpenTargets; ENSG00000083290; -.
DR PharmGKB; PA37780; -.
DR VEuPathDB; HostDB:ENSG00000083290; -.
DR eggNOG; KOG0595; Eukaryota.
DR GeneTree; ENSGT00940000157588; -.
DR HOGENOM; CLU_011264_0_0_1; -.
DR InParanoid; Q8IYT8; -.
DR OMA; RIKIVCE; -.
DR OrthoDB; 1198291at2759; -.
DR PhylomeDB; Q8IYT8; -.
DR TreeFam; TF324551; -.
DR PathwayCommons; Q8IYT8; -.
DR SignaLink; Q8IYT8; -.
DR SIGNOR; Q8IYT8; -.
DR BioGRID-ORCS; 9706; 15 hits in 1106 CRISPR screens.
DR ChiTaRS; ULK2; human.
DR GenomeRNAi; 9706; -.
DR Pharos; Q8IYT8; Tchem.
DR PRO; PR:Q8IYT8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IYT8; protein.
DR Bgee; ENSG00000083290; Expressed in cortical plate and 198 other tissues.
DR ExpressionAtlas; Q8IYT8; baseline and differential.
DR Genevisible; Q8IYT8; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IDA:GO_Central.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0048675; P:axon extension; IBA:GO_Central.
DR GO; GO:0048668; P:collateral sprouting; IEA:Ensembl.
DR GO; GO:0044805; P:late nucleophagy; IBA:GO_Central.
DR GO; GO:0048671; P:negative regulation of collateral sprouting; IBA:GO_Central.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0034727; P:piecemeal microautophagy of the nucleus; IBA:GO_Central.
DR GO; GO:0010508; P:positive regulation of autophagy; IBA:GO_Central.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0042594; P:response to starvation; ISS:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR016237; Ser/Thr_kin_STPK_Ulk-1/2.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR022708; Ser/Thr_kinase_C.
DR PANTHER; PTHR24348; PTHR24348; 1.
DR Pfam; PF12063; DUF3543; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000580; Ser/Thr_PK_STPK_ULK-1/2; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Autophagy; Cytoplasmic vesicle; Kinase;
KW Membrane; Neurogenesis; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1036
FT /note="Serine/threonine-protein kinase ULK2"
FT /id="PRO_0000086782"
FT DOMAIN 9..271
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 319..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 656..695
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..1036
FT /note="CTD-like region"
FT COMPBIAS 418..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 15..23
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY01"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY01"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9QY01"
FT VARIANT 242
FT /note="P -> S (in dbSNP:rs34670978)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041281"
FT VARIANT 370
FT /note="V -> M (in dbSNP:rs150122)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_055287"
FT VARIANT 533
FT /note="T -> I (in dbSNP:rs4462660)"
FT /id="VAR_055288"
FT VARIANT 627
FT /note="G -> E (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041282"
FT VARIANT 662
FT /note="A -> V (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041283"
FT VARIANT 752
FT /note="G -> R (in dbSNP:rs55730189)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041284"
FT VARIANT 842
FT /note="D -> E (in dbSNP:rs35107651)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041285"
FT MUTAGEN 39
FT /note="K->R: Decreased kinase activity and decreased
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:18936157"
FT CONFLICT 935
FT /note="C -> R (in Ref. 1; BAA31598)"
FT /evidence="ECO:0000305"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:6QAV"
FT STRAND 7..17
FT /evidence="ECO:0007829|PDB:6QAV"
FT STRAND 19..31
FT /evidence="ECO:0007829|PDB:6QAV"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:6QAV"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 56..62
FT /evidence="ECO:0007829|PDB:6QAV"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:6QAV"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 93..100
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 105..125
FT /evidence="ECO:0007829|PDB:6QAV"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:6QAV"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:6QAV"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 183..186
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6QAV"
FT TURN 191..194
FT /evidence="ECO:0007829|PDB:6QAU"
FT HELIX 195..209
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 242..251
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:6QAV"
FT HELIX 262..266
FT /evidence="ECO:0007829|PDB:6QAV"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:6QAV"
SQ SEQUENCE 1036 AA; 112694 MW; D311F01FA058CBBC CRC64;
MEVVGDFEYS KRDLVGHGAF AVVFRGRHRQ KTDWEVAIKS INKKNLSKSQ ILLGKEIKIL
KELQHENIVA LYDVQELPNS VFLVMEYCNG GDLADYLQAK GTLSEDTIRV FLHQIAAAMR
ILHSKGIIHR DLKPQNILLS YANRRKSSVS GIRIKIADFG FARYLHSNMM AATLCGSPMY
MAPEVIMSQH YDAKADLWSI GTVIYQCLVG KPPFQANSPQ DLRMFYEKNR SLMPSIPRET
SPYLANLLLG LLQRNQKDRM DFEAFFSHPF LEQGPVKKSC PVPVPMYSGS VSGSSCGSSP
SCRFASPPSL PDMQHIQEEN LSSPPLGPPN YLQVSKDSAS TSSKNSSCDT DDFVLVPHNI
SSDHSCDMPV GTAGRRASNE FLVCGGQCQP TVSPHSETAP IPVPTQIRNY QRIEQNLTST
ASSGTNVHGS PRSAVVRRSN TSPMGFLRPG SCSPVPADTA QTVGRRLSTG SSRPYSPSPL
VGTIPEQFSQ CCCGHPQGHD SRSRNSSGSP VPQAQSPQSL LSGARLQSAP TLTDIYQNKQ
KLRKQHSDPV CPSHTGAGYS YSPQPSRPGS LGTSPTKHLG SSPRSSDWFF KTPLPTIIGS
PTKTTAPFKI PKTQASSNLL ALVTRHGPAE EQSKDGNEPR ECAHCLLVQG SERQRAEQQS
KAVFGRSVST GKLSDQQGKT PICRHQGSTD SLNTERPMDI APAGACGGVL APPAGTAASS
KAVLFTVGSP PHSAAAPTCT HMFLRTRTTS VGPSNSGGSL CAMSGRVCVG SPPGPGFGSS
PPGAEAAPSL RYVPYGASPP SLEGLITFEA PELPEETLME REHTDTLRHL NVMLMFTECV
LDLTAMRGGN PELCTSAVSL YQIQESVVVD QISQLSKDWG RVEQLVLYMK AAQLLAASLH
LAKAQIKSGK LSPSTAVKQV VKNLNERYKF CITMCKKLTE KLNRFFSDKQ RFIDEINSVT
AEKLIYNCAV EMVQSAALDE MFQQTEDIVY RYHKAALLLE GLSRILQDPA DIENVHKYKC
SIERRLSALC HSTATV
