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}.
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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   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.
DR   Genevisible; Q8NI77; HS.
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
//