KLHL2_HUMAN
ID KLHL2_HUMAN Reviewed; 593 AA.
AC O95198; A6NCM7; B2RD18; B4DFH7; F5H6M3; Q8N484; Q8TBH5;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 2.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Kelch-like protein 2;
DE AltName: Full=Actin-binding protein Mayven;
GN Name=KLHL2;
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] (ISOFORM 1), SUBUNIT, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=10397770; DOI=10.1091/mbc.10.7.2361;
RA Soltysik-Espanola M.B., Rogers R.A., Jiang S., Kim T.A., Gaedigk R.,
RA White R.A., Avraham H., Avraham S.;
RT "Characterization of Mayven, a novel actin-binding protein predominantly
RT expressed in brain.";
RL Mol. Biol. Cell 10:2361-2375(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
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 INTERACTION WITH KLHL12.
RX PubMed=15383316; DOI=10.1016/j.yexcr.2004.06.023;
RA Mai A., Jung S.K., Yonehara S.;
RT "hDKIR, a human homologue of the Drosophila kelch protein, involved in a
RT ring-like structure.";
RL Exp. Cell Res. 300:72-83(2004).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH FYN.
RX PubMed=15715669; DOI=10.1111/j.1471-4159.2004.02946.x;
RA Jiang S., Avraham H.K., Park S.Y., Kim T.A., Bu X., Seng S., Avraham S.;
RT "Process elongation of oligodendrocytes is promoted by the Kelch-related
RT actin-binding protein Mayven.";
RL J. Neurochem. 92:1191-1203(2005).
RN [7]
RP FUNCTION.
RX PubMed=23838290; DOI=10.1016/j.bbrc.2013.06.104;
RA Takahashi D., Mori T., Wakabayashi M., Mori Y., Susa K., Zeniya M.,
RA Sohara E., Rai T., Sasaki S., Uchida S.;
RT "KLHL2 interacts with and ubiquitinates WNK kinases.";
RL Biochem. Biophys. Res. Commun. 437:457-462(2013).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF 294-591.
RX PubMed=23349464; DOI=10.1074/jbc.m112.437996;
RA Canning P., Cooper C.D., Krojer T., Murray J.W., Pike A.C., Chaikuad A.,
RA Keates T., Thangaratnarajah C., Hojzan V., Marsden B.D., Gileadi O.,
RA Knapp S., von Delft F., Bullock A.N.;
RT "Structural basis for Cul3 assembly with the BTB-Kelch family of E3
RT ubiquitin ligases.";
RL J. Biol. Chem. 288:7803-7814(2013).
CC -!- FUNCTION: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex that mediates the ubiquitination of
CC target proteins, such as NPTXR, leading most often to their proteasomal
CC degradation (By similarity). Responsible for degradative ubiquitination
CC of the WNK kinases WNK1, WNK3 and WNK4. Plays a role in the
CC reorganization of the actin cytoskeleton. Promotes growth of cell
CC projections in oligodendrocyte precursors. {ECO:0000250,
CC ECO:0000269|PubMed:15715669, ECO:0000269|PubMed:23838290}.
CC -!- SUBUNIT: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3
CC ubiquitin-protein ligase complex. Interacts with NPTXR and CUL3 (By
CC similarity). Binds actin. Interacts with KLHL12. Interacts (via N-
CC terminus) with FYN (via SH3 domain). {ECO:0000250,
CC ECO:0000269|PubMed:10397770, ECO:0000269|PubMed:15383316,
CC ECO:0000269|PubMed:15715669}.
CC -!- INTERACTION:
CC O95198; P50895: BCAM; NbExp=6; IntAct=EBI-746999, EBI-10212133;
CC O95198; Q13895: BYSL; NbExp=3; IntAct=EBI-746999, EBI-358049;
CC O95198; Q9H1P6: C20orf85; NbExp=3; IntAct=EBI-746999, EBI-12155483;
CC O95198; Q86WV7: CCDC43; NbExp=5; IntAct=EBI-746999, EBI-10260148;
CC O95198; Q96MW1: CCDC43; NbExp=3; IntAct=EBI-746999, EBI-9247198;
CC O95198; Q16543: CDC37; NbExp=3; IntAct=EBI-746999, EBI-295634;
CC O95198; P49760: CLK2; NbExp=6; IntAct=EBI-746999, EBI-750020;
CC O95198; Q13618: CUL3; NbExp=5; IntAct=EBI-746999, EBI-456129;
CC O95198; Q9HCG8: CWC22; NbExp=3; IntAct=EBI-746999, EBI-373289;
CC O95198; Q14241: ELOA; NbExp=3; IntAct=EBI-746999, EBI-742350;
CC O95198; Q14145: KEAP1; NbExp=3; IntAct=EBI-746999, EBI-751001;
CC O95198; Q53G59: KLHL12; NbExp=5; IntAct=EBI-746999, EBI-740929;
CC O95198; O95198: KLHL2; NbExp=5; IntAct=EBI-746999, EBI-746999;
CC O95198; Q9UH77: KLHL3; NbExp=3; IntAct=EBI-746999, EBI-8524663;
CC O95198; P55081: MFAP1; NbExp=3; IntAct=EBI-746999, EBI-1048159;
CC O95198; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-746999, EBI-3911716;
CC O95198; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-746999, EBI-741158;
CC O95198; Q6TGC4: PADI6; NbExp=3; IntAct=EBI-746999, EBI-10892722;
CC O95198; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-746999, EBI-14066006;
CC O95198; Q9BUI4: POLR3C; NbExp=3; IntAct=EBI-746999, EBI-5452779;
CC O95198; O00560: SDCBP; NbExp=3; IntAct=EBI-746999, EBI-727004;
CC O95198; Q96EY4: TMA16; NbExp=7; IntAct=EBI-746999, EBI-1045338;
CC O95198; O14787: TNPO2; NbExp=4; IntAct=EBI-746999, EBI-431907;
CC O95198; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-746999, EBI-9867283;
CC O95198; O95881: TXNDC12; NbExp=4; IntAct=EBI-746999, EBI-2564581;
CC O95198; Q5TZN3: UBE2C; NbExp=3; IntAct=EBI-746999, EBI-10247554;
CC O95198; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-746999, EBI-10180829;
CC O95198; Q8NC26: ZNF114; NbExp=8; IntAct=EBI-746999, EBI-10265237;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell projection, ruffle.
CC Cell projection {ECO:0000250}. Cell projection, lamellipodium
CC {ECO:0000250}. Cytoplasm, cytosol. Note=A proportion colocalizes with
CC the actin cytoskeleton. When over-expressed, colocalizes with NPTXR in
CC perinuclear aggresomes (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95198-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95198-2; Sequence=VSP_042837;
CC Name=3;
CC IsoId=O95198-3; Sequence=VSP_047004;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Detected throughout the brain.
CC {ECO:0000269|PubMed:10397770}.
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; AF059569; AAC67502.1; -; mRNA.
DR EMBL; AK294103; BAG57438.1; -; mRNA.
DR EMBL; AK315372; BAG37765.1; -; mRNA.
DR EMBL; AC012504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC055120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107059; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022503; AAH22503.1; -; mRNA.
DR EMBL; BC036468; AAH36468.1; -; mRNA.
DR CCDS; CCDS34094.1; -. [O95198-1]
DR CCDS; CCDS54815.1; -. [O95198-2]
DR CCDS; CCDS54816.1; -. [O95198-3]
DR RefSeq; NP_001154993.1; NM_001161521.1. [O95198-2]
DR RefSeq; NP_001154994.1; NM_001161522.1. [O95198-3]
DR RefSeq; NP_001317952.1; NM_001331023.1.
DR RefSeq; NP_001317953.1; NM_001331024.1.
DR RefSeq; NP_009177.3; NM_007246.3. [O95198-1]
DR RefSeq; XP_016863165.1; XM_017007676.1. [O95198-3]
DR PDB; 2XN4; X-ray; 1.99 A; A/B=294-591.
DR PDB; 4CHB; X-ray; 1.56 A; A/B=294-591.
DR PDBsum; 2XN4; -.
DR PDBsum; 4CHB; -.
DR AlphaFoldDB; O95198; -.
DR SMR; O95198; -.
DR BioGRID; 116431; 107.
DR ELM; O95198; -.
DR IntAct; O95198; 30.
DR MINT; O95198; -.
DR STRING; 9606.ENSP00000424198; -.
DR TCDB; 8.A.160.1.4; the catenin (catenin) family.
DR iPTMnet; O95198; -.
DR PhosphoSitePlus; O95198; -.
DR BioMuta; KLHL2; -.
DR EPD; O95198; -.
DR MassIVE; O95198; -.
DR PaxDb; O95198; -.
DR PeptideAtlas; O95198; -.
DR PRIDE; O95198; -.
DR Antibodypedia; 28300; 306 antibodies from 23 providers.
DR DNASU; 11275; -.
DR Ensembl; ENST00000226725.11; ENSP00000226725.6; ENSG00000109466.14. [O95198-1]
DR Ensembl; ENST00000514860.5; ENSP00000424198.1; ENSG00000109466.14. [O95198-2]
DR Ensembl; ENST00000538127.5; ENSP00000437526.1; ENSG00000109466.14. [O95198-3]
DR GeneID; 11275; -.
DR KEGG; hsa:11275; -.
DR MANE-Select; ENST00000226725.11; ENSP00000226725.6; NM_007246.4; NP_009177.3.
DR UCSC; uc003irb.4; human. [O95198-1]
DR CTD; 11275; -.
DR DisGeNET; 11275; -.
DR GeneCards; KLHL2; -.
DR HGNC; HGNC:6353; KLHL2.
DR HPA; ENSG00000109466; Tissue enhanced (brain).
DR MIM; 605774; gene.
DR neXtProt; NX_O95198; -.
DR OpenTargets; ENSG00000109466; -.
DR PharmGKB; PA30143; -.
DR VEuPathDB; HostDB:ENSG00000109466; -.
DR eggNOG; KOG4441; Eukaryota.
DR GeneTree; ENSGT00940000156434; -.
DR HOGENOM; CLU_004253_14_2_1; -.
DR InParanoid; O95198; -.
DR OMA; PSCMSTG; -.
DR OrthoDB; 635140at2759; -.
DR PhylomeDB; O95198; -.
DR TreeFam; TF329218; -.
DR PathwayCommons; O95198; -.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; O95198; -.
DR BioGRID-ORCS; 11275; 10 hits in 1113 CRISPR screens.
DR ChiTaRS; KLHL2; human.
DR EvolutionaryTrace; O95198; -.
DR GenomeRNAi; 11275; -.
DR Pharos; O95198; Tbio.
DR PRO; PR:O95198; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O95198; protein.
DR Bgee; ENSG00000109466; Expressed in Brodmann (1909) area 23 and 197 other tissues.
DR ExpressionAtlas; O95198; baseline and differential.
DR Genevisible; O95198; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:UniProtKB.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR CDD; cd18338; BTB_POZ_KLHL2_Mayven; 1.
DR Gene3D; 2.120.10.80; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR017096; BTB-kelch_protein.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR044072; KLHL2_BTB/POZ.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF01344; Kelch_1; 6.
DR PIRSF; PIRSF037037; Kelch-like_protein_gigaxonin; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00612; Kelch; 6.
DR SUPFAM; SSF117281; SSF117281; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
DR PROSITE; PS50097; BTB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; Cell projection;
KW Cytoplasm; Cytoskeleton; Kelch repeat; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..593
FT /note="Kelch-like protein 2"
FT /id="PRO_0000119101"
FT DOMAIN 56..123
FT /note="BTB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT REPEAT 308..353
FT /note="Kelch 1"
FT REPEAT 354..400
FT /note="Kelch 2"
FT REPEAT 402..447
FT /note="Kelch 3"
FT REPEAT 449..496
FT /note="Kelch 4"
FT REPEAT 497..543
FT /note="Kelch 5"
FT REPEAT 545..591
FT /note="Kelch 6"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_047004"
FT VAR_SEQ 1..9
FT /note="METPPLPPA -> MVWLEARPQILFV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042837"
FT CONFLICT 273
FT /note="D -> N (in Ref. 1; AAC67502)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="R -> G (in Ref. 4; AAH36468)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="G -> V (in Ref. 4; AAH22503)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="C -> Y (in Ref. 1; AAC67502)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="P -> R (in Ref. 2; BAG37765 and 4; AAH22503)"
FT /evidence="ECO:0000305"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 315..320
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:4CHB"
FT TURN 328..331
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 347..351
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:4CHB"
FT TURN 375..378
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 410..413
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:4CHB"
FT TURN 422..425
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 441..445
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 448..452
FT /evidence="ECO:0007829|PDB:4CHB"
FT TURN 457..460
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:4CHB"
FT TURN 471..474
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 490..494
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 497..501
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 504..509
FT /evidence="ECO:0007829|PDB:2XN4"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:4CHB"
FT TURN 518..520
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 523..525
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 537..541
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 544..548
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 553..556
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:4CHB"
FT TURN 565..568
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 569..572
FT /evidence="ECO:0007829|PDB:4CHB"
FT STRAND 585..590
FT /evidence="ECO:0007829|PDB:4CHB"
SQ SEQUENCE 593 AA; 65975 MW; 397AE02E69E56A18 CRC64;
METPPLPPAC TKQGHQKPLD SKDDNTEKHC PVTVNPWHMK KAFKVMNELR SQNLLCDVTI
VAEDMEISAH RVVLAACSPY FHAMFTGEMS ESRAKRVRIK EVDGWTLRML IDYVYTAEIQ
VTEENVQVLL PAAGLLQLQD VKKTCCEFLE SQLHPVNCLG IRAFADMHAC TDLLNKANTY
AEQHFADVVL SEEFLNLGIE QVCSLISSDK LTISSEEKVF EAVIAWVNHD KDVRQEFMAR
LMEHVRLPLL PREYLVQRVE EEALVKNSSA CKDYLIEAMK YHLLPTEQRI LMKSVRTRLR
TPMNLPKLMV VVGGQAPKAI RSVECYDFKE ERWHQVAELP SRRCRAGMVY MAGLVFAVGG
FNGSLRVRTV DSYDPVKDQW TSVANMRDRR STLGAAVLNG LLYAVGGFDG STGLSSVEAY
NIKSNEWFHV APMNTRRSSV GVGVVGGLLY AVGGYDGASR QCLSTVECYN ATTNEWTYIA
EMSTRRSGAG VGVLNNLLYA VGGHDGPLVR KSVEVYDPTT NAWRQVADMN MCRRNAGVCA
VNGLLYVVGG DDGSCNLASV EYYNPTTDKW TVVSSCMSTG RSYAGVTVID KPL
