ID KI18A_HUMAN Reviewed; 898 AA.
AC Q8NI77; Q4VPE3; Q86VS5; Q9H0F3;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 2.
DT 27-MAR-2024, entry version 175.
DE RecName: Full=Kinesin-like protein KIF18A;
DE AltName: Full=Marrow stromal KIF18A;
DE Short=MS-KIF18A;
GN Name=KIF18A; ORFNames=OK/SW-cl.108;
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 [MRNA], VARIANT VAL-735, AND SUBCELLULAR LOCATION.
RC TISSUE=Bone marrow stroma;
RX PubMed=15878648; DOI=10.1016/j.gene.2005.02.009;
RA Luboshits G., Benayahu D.;
RT "MS-KIF18A, new kinesin; structure and cellular expression.";
RL Gene 351:19-28(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon adenocarcinoma;
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that are recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-735.
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 [5]
RP FUNCTION.
RX PubMed=17346968; DOI=10.1016/j.cub.2007.02.036;
RA Mayr M.I., Huemmer S., Bormann J., Gruener T., Adio S., Woehlke G.,
RA Mayer T.U.;
RT "The human kinesin Kif18A is a motile microtubule depolymerase essential
RT for chromosome congression.";
RL Curr. Biol. 17:488-498(2007).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH ESR1.
RX PubMed=17006958; DOI=10.1002/jcb.21000;
RA Luboshits G., Benayahu D.;
RT "MS-KIF18A, a kinesin, is associated with estrogen receptor.";
RL J. Cell. Biochem. 100:693-702(2007).
RN [7]
RP FUNCTION.
RX PubMed=18267093; DOI=10.1016/j.devcel.2007.11.014;
RA Stumpff J., von Dassow G., Wagenbach M., Asbury C., Wordeman L.;
RT "The kinesin-8 motor Kif18A suppresses kinetochore movements to control
RT mitotic chromosome alignment.";
RL Dev. Cell 14:252-262(2008).
RN [8]
RP SUBCELLULAR LOCATION, ASSOCIATION WITH MICROTUBULES, PHOSPHORYLATION,
RP GLYCOSYLATION, AND UBIQUITINATION.
RX PubMed=18680169; DOI=10.1002/jcp.21525;
RA Zusev M., Benayahu D.;
RT "New insights on cellular distribution, microtubule interactions and post-
RT translational modifications of MS-KIF18A.";
RL J. Cell. Physiol. 217:618-625(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP FUNCTION.
RX PubMed=18513970; DOI=10.1016/j.tcb.2008.05.003;
RA Gardner M.K., Odde D.J., Bloom K.;
RT "Kinesin-8 molecular motors: putting the brakes on chromosome
RT oscillations.";
RL Trends Cell Biol. 18:307-310(2008).
RN [11]
RP FUNCTION, AND INTERACTION WITH CENPE.
RX PubMed=19625775; DOI=10.4161/cc.8.16.9366;
RA Huang Y., Yao Y., Xu H.-Z., Wang Z.-G., Lu L., Dai W.;
RT "Defects in chromosome congression and mitotic progression in KIF18A-
RT deficient cells are partly mediated through impaired functions of CENP-E.";
RL Cell Cycle 8:2643-2649(2009).
RN [12]
RP INDUCTION, AND INTERACTION WITH ESR1.
RX PubMed=19636373; DOI=10.1371/journal.pone.0006407;
RA Zusev M., Benayahu D.;
RT "The regulation of MS-KIF18A expression and cross talk with estrogen
RT receptor.";
RL PLoS ONE 4:E6407-E6407(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-695 AND SER-838, AND
RP 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-24, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-683; LYS-794; LYS-868 AND
RP LYS-874, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Microtubule-depolymerizing kinesin which plays a role in
CC chromosome congression by reducing the amplitude of preanaphase
CC oscillations and slowing poleward movement during anaphase, thus
CC suppressing chromosome movements. May stabilize the CENPE-BUB1B complex
CC at the kinetochores during early mitosis and maintains CENPE levels at
CC kinetochores during chromosome congression.
CC {ECO:0000269|PubMed:17346968, ECO:0000269|PubMed:18267093,
CC ECO:0000269|PubMed:18513970, ECO:0000269|PubMed:19625775}.
CC -!- SUBUNIT: Interacts with CENPE and ESR1. {ECO:0000269|PubMed:17006958,
CC ECO:0000269|PubMed:19625775, ECO:0000269|PubMed:19636373}.
CC -!- INTERACTION:
CC Q8NI77; Q9UJX5: ANAPC4; NbExp=2; IntAct=EBI-355426, EBI-2554854;
CC Q8NI77; P62136: PPP1CA; NbExp=3; IntAct=EBI-355426, EBI-357253;
CC -!- SUBCELLULAR LOCATION: Cell projection, ruffle. Cytoplasm. Nucleus.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
CC -!- INDUCTION: By estrogen. {ECO:0000269|PubMed:19636373}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:18680169}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:18680169}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Kinesin family. {ECO:0000255|PROSITE-ProRule:PRU00283}.
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; AY791349; AAX16185.1; -; mRNA.
DR EMBL; AB062483; BAB93508.1; -; mRNA.
DR EMBL; AL136819; CAB66753.1; -; mRNA.
DR EMBL; BC048347; AAH48347.1; -; mRNA.
DR CCDS; CCDS7867.1; -.
DR RefSeq; NP_112494.3; NM_031217.3.
DR RefSeq; XP_016873868.1; XM_017018379.1.
DR PDB; 3LRE; X-ray; 2.20 A; A/B=1-355.
DR PDB; 5OAM; EM; 5.50 A; K=1-374.
DR PDB; 5OCU; EM; 5.20 A; K=1-374.
DR PDB; 5OGC; EM; 4.80 A; K=1-374.
DR PDB; 7RSI; EM; 4.90 A; C=1-353.
DR PDBsum; 3LRE; -.
DR PDBsum; 5OAM; -.
DR PDBsum; 5OCU; -.
DR PDBsum; 5OGC; -.
DR PDBsum; 7RSI; -.
DR AlphaFoldDB; Q8NI77; -.
DR EMDB; EMD-24672; -.
DR EMDB; EMD-3778; -.
DR EMDB; EMD-3780; -.
DR EMDB; EMD-3803; -.
DR SMR; Q8NI77; -.
DR BioGRID; 123630; 56.
DR ELM; Q8NI77; -.
DR IntAct; Q8NI77; 38.
DR MINT; Q8NI77; -.
DR STRING; 9606.ENSP00000263181; -.
DR BindingDB; Q8NI77; -.
DR ChEMBL; CHEMBL4523403; -.
DR GlyGen; Q8NI77; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NI77; -.
DR PhosphoSitePlus; Q8NI77; -.
DR BioMuta; KIF18A; -.
DR DMDM; 66774137; -.
DR EPD; Q8NI77; -.
DR jPOST; Q8NI77; -.
DR MassIVE; Q8NI77; -.
DR MaxQB; Q8NI77; -.
DR PaxDb; 9606-ENSP00000263181; -.
DR PeptideAtlas; Q8NI77; -.
DR ProteomicsDB; 73837; -.
DR Pumba; Q8NI77; -.
DR Antibodypedia; 25467; 168 antibodies from 26 providers.
DR DNASU; 81930; -.
DR Ensembl; ENST00000263181.7; ENSP00000263181.6; ENSG00000121621.7.
DR GeneID; 81930; -.
DR KEGG; hsa:81930; -.
DR MANE-Select; ENST00000263181.7; ENSP00000263181.6; NM_031217.4; NP_112494.3.
DR UCSC; uc001msc.3; human.
DR AGR; HGNC:29441; -.
DR CTD; 81930; -.
DR DisGeNET; 81930; -.
DR GeneCards; KIF18A; -.
DR HGNC; HGNC:29441; KIF18A.
DR HPA; ENSG00000121621; Group enriched (bone marrow, lymphoid tissue, testis).
DR MIM; 611271; gene.
DR neXtProt; NX_Q8NI77; -.
DR OpenTargets; ENSG00000121621; -.
DR PharmGKB; PA134951326; -.
DR VEuPathDB; HostDB:ENSG00000121621; -.
DR eggNOG; KOG0242; Eukaryota.
DR GeneTree; ENSGT00940000159058; -.
DR HOGENOM; CLU_001485_21_5_1; -.
DR InParanoid; Q8NI77; -.
DR OMA; NCLKMLC; -.
DR OrthoDB; 239968at2759; -.
DR PhylomeDB; Q8NI77; -.
DR TreeFam; TF105231; -.
DR BRENDA; 5.6.1.3; 2681.
DR BRENDA; 5.6.1.4; 2681.
DR PathwayCommons; Q8NI77; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR Reactome; R-HSA-983189; Kinesins.
DR SignaLink; Q8NI77; -.
DR SIGNOR; Q8NI77; -.
DR BioGRID-ORCS; 81930; 698 hits in 1169 CRISPR screens.
DR ChiTaRS; KIF18A; human.
DR EvolutionaryTrace; Q8NI77; -.
DR GeneWiki; KIF18A; -.
DR GenomeRNAi; 81930; -.
DR Pharos; Q8NI77; Tchem.
DR PRO; PR:Q8NI77; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NI77; Protein.
DR Bgee; ENSG00000121621; Expressed in ventricular zone and 113 other cell types or tissues.
DR Genevisible; Q8NI77; HS.
DR GO; GO:0005901; C:caveola; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005871; C:kinesin complex; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IEA:Ensembl.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:LIFEdb.
DR GO; GO:0061673; C:mitotic spindle astral microtubule; IBA:GO_Central.
DR GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IPI:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR GO; GO:0051010; F:microtubule plus-end binding; IDA:UniProtKB.
DR GO; GO:0008574; F:plus-end-directed microtubule motor activity; IDA:UniProtKB.
DR GO; GO:0070463; F:tubulin-dependent ATPase activity; IDA:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0007140; P:male meiotic nuclear division; IEA:Ensembl.
DR GO; GO:0007019; P:microtubule depolymerization; IDA:UniProtKB.
DR GO; GO:0007018; P:microtubule-based movement; IBA:GO_Central.
DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; IDA:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR CDD; cd01370; KISc_KIP3_like; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR InterPro; IPR027640; Kinesin-like_fam.
DR InterPro; IPR019821; Kinesin_motor_CS.
DR InterPro; IPR001752; Kinesin_motor_dom.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR47968; CENTROMERE PROTEIN E; 1.
DR PANTHER; PTHR47968:SF13; KINESIN-LIKE PROTEIN; 1.
DR Pfam; PF00225; Kinesin; 1.
DR PRINTS; PR00380; KINESINHEAVY.
DR SMART; SM00129; KISc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00411; KINESIN_MOTOR_1; 1.
DR PROSITE; PS50067; KINESIN_MOTOR_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell projection; Coiled coil; Cytoplasm;
KW Cytoskeleton; Glycoprotein; Isopeptide bond; Microtubule; Motor protein;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..898
FT /note="Kinesin-like protein KIF18A"
FT /id="PRO_0000125458"
FT DOMAIN 11..355
FT /note="Kinesin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT REGION 667..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 368..453
FT /evidence="ECO:0000255"
FT COMPBIAS 830..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..871
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 113..120
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00283"
FT MOD_RES 674
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 24
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297"
FT CROSSLNK 683
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 794
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 868
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 874
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 273
FT /note="T -> A (in dbSNP:rs12272419)"
FT /id="VAR_049701"
FT VARIANT 334
FT /note="P -> S (in dbSNP:rs34913484)"
FT /id="VAR_049702"
FT VARIANT 735
FT /note="I -> V (in dbSNP:rs10458896)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15878648"
FT /id="VAR_038354"
FT CONFLICT 621
FT /note="A -> G (in Ref. 2; BAB93508)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="P -> S (in Ref. 2; BAB93508)"
FT /evidence="ECO:0000305"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:3LRE"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 107..112
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 132..146
FT /evidence="ECO:0007829|PDB:3LRE"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 151..163
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 200..212
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 229..240
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 252..258
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 283..295
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 311..315
FT /evidence="ECO:0007829|PDB:3LRE"
FT TURN 316..319
FT /evidence="ECO:0007829|PDB:3LRE"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:3LRE"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:3LRE"
SQ SEQUENCE 898 AA; 102281 MW; 6DFD904378BF9B27 CRC64;
MSVTEEDLCH HMKVVVRVRP ENTKEKAAGF HKVVHVVDKH ILVFDPKQEE VSFFHGKKTT
NQNVIKKQNK DLKFVFDAVF DETSTQSEVF EHTTKPILRS FLNGYNCTVL AYGATGAGKT
HTMLGSADEP GVMYLTMLHL YKCMDEIKEE KICSTAVSYL EVYNEQIRDL LVNSGPLAVR
EDTQKGVVVH GLTLHQPKSS EEILHLLDNG NKNRTQHPTD MNATSSRSHA VFQIYLRQQD
KTASINQNVR IAKMSLIDLA GSERASTSGA KGTRFVEGTN INRSLLALGN VINALADSKR
KNQHIPYRNS KLTRLLKDSL GGNCQTIMIA AVSPSSVFYD DTYNTLKYAN RAKDIKSSLK
SNVLNVNNHI TQYVKICNEQ KAEILLLKEK LKAYEEQKAF TNENDQAKLM ISNPQEKEIE
RFQEILNCLF QNREEIRQEY LKLEMLLKEN ELKSFYQQQC HKQIEMMCSE DKVEKATGKR
DHRLAMLKTR RSYLEKRREE ELKQFDENTN WLHRVEKEMG LLSQNGHIPK ELKKDLHCHH
LHLQNKDLKA QIRHMMDLAC LQEQQHRQTE AVLNALLPTL RKQYCTLKEA GLSNAAFESD
FKEIEHLVER KKVVVWADQT AEQPKQNDLP GISVLMTFPQ LGPVQPIPCC SSSGGTNLVK
IPTEKRTRRK LMPSPLKGQH TLKSPPSQSV QLNDSLSKEL QPIVYTPEDC RKAFQNPSTV
TLMKPSSFTT SFQAISSNIN SDNCLKMLCE VAIPHNRRKE CGQEDLDSTF TICEDIKSSK
CKLPEQESLP NDNKDILQRL DPSSFSTKHS MPVPSMVPSY MAMTTAAKRK RKLTSSTSNS
SLTADVNSGF AKRVRQDNSS EKHLQENKPT MEHKRNICKI NPSMVRKFGR NISKGNLR
//
