ID   MT21D_HUMAN             Reviewed;         229 AA.
AC   Q9H867; B7ZLA3; B7ZLA4; Q2M2X3; Q86T12;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 2.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Protein N-lysine methyltransferase METTL21D;
DE            EC=2.1.1.- {ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634};
DE   AltName: Full=Methyltransferase-like protein 21D;
DE   AltName: Full=VCP lysine methyltransferase;
DE            Short=VCP-KMT;
DE   AltName: Full=Valosin-containing protein lysine methyltransferase;
GN   Name=VCPKMT; Synonyms=C14orf138, METTL21D;
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] (ISOFORMS 1 AND 2).
RC   TISSUE=Prostate, and Retinoblastoma;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=T-cell;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA   Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA   Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA   Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA   Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA   Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA   Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA   Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA   Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA   Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA   Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA   Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA   Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA   Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
RC   TISSUE=Brain, and 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, CATALYTIC ACTIVITY, INTERACTION WITH ALKBH6, AND MUTAGENESIS OF
RP   ASP-96 AND ASP-144.
RX   PubMed=22948820; DOI=10.1038/ncomms2041;
RA   Kernstock S., Davydova E., Jakobsson M., Moen A., Pettersen S.,
RA   Maelandsmo G.M., Egge-Jacobsen W., Falnes P.O.;
RT   "Lysine methylation of VCP by a member of a novel human protein
RT   methyltransferase family.";
RL   Nat. Commun. 3:1038-1038(2012).
RN   [6]
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=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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
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   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ASPSCR1 AND UBXN6,
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-73.
RX   PubMed=23349634; DOI=10.1371/journal.pgen.1003210;
RA   Cloutier P., Lavallee-Adam M., Faubert D., Blanchette M., Coulombe B.;
RT   "A newly uncovered group of distantly related lysine methyltransferases
RT   preferentially interact with molecular chaperones to regulate their
RT   activity.";
RL   PLoS Genet. 9:E1003210-E1003210(2013).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 7-229 IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE.
RA   Zeng H., Dong A., Fenner M., Bountra C., Arrowsmith C.H., Edwards A.M.,
RA   Brown P.J., Wu H.;
RT   "The crystal structure of human methyltransferase-like protein 21D in
RT   complex with SAM.";
RL   Submitted (JUN-2013) to the PDB data bank.
CC   -!- FUNCTION: Protein N-lysine methyltransferase that specifically
CC       trimethylates 'Lys-315' of VCP/p97; this modification may decrease VCP
CC       ATPase activity. {ECO:0000269|PubMed:22948820,
CC       ECO:0000269|PubMed:23349634}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:54192, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:13826, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961;
CC         Evidence={ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54193;
CC         Evidence={ECO:0000305|PubMed:22948820};
CC   -!- SUBUNIT: Interacts with ALKBH6. Interacts with ASPSCR1 and UBXN6;
CC       interaction with ASPSCR1, but not with UBXN6, enhances VCP methylation.
CC       {ECO:0000269|PubMed:22948820, ECO:0000269|PubMed:23349634}.
CC   -!- INTERACTION:
CC       Q9H867; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-18393784, EBI-11530605;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23349634}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=4;
CC         IsoId=Q9H867-4; Sequence=Displayed;
CC       Name=1;
CC         IsoId=Q9H867-1; Sequence=VSP_026586, VSP_026587;
CC       Name=2;
CC         IsoId=Q9H867-2; Sequence=VSP_008814, VSP_008816;
CC       Name=3;
CC         IsoId=Q9H867-3; Sequence=VSP_008815;
CC       Name=5;
CC         IsoId=Q9H867-5; Sequence=VSP_043258;
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. METTL21
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAD62329.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK023982; BAB14752.1; -; mRNA.
DR   EMBL; AK129564; BAC85183.1; -; mRNA.
DR   EMBL; BX247997; CAD62329.1; ALT_INIT; mRNA.
DR   EMBL; AL109758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC027585; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC105118; AAI05119.1; -; mRNA.
DR   EMBL; BC143673; AAI43674.1; -; mRNA.
DR   EMBL; BC143674; AAI43675.1; -; mRNA.
DR   CCDS; CCDS41951.1; -. [Q9H867-5]
DR   CCDS; CCDS9696.2; -. [Q9H867-4]
DR   RefSeq; NP_001035752.1; NM_001040662.1. [Q9H867-5]
DR   RefSeq; NP_078834.2; NM_024558.2. [Q9H867-4]
DR   PDB; 4LG1; X-ray; 1.80 A; A/B/C=7-229.
DR   PDB; 7OAT; X-ray; 3.00 A; C=7-229.
DR   PDB; 8HL6; X-ray; 1.80 A; A=1-229.
DR   PDB; 8HL7; X-ray; 2.80 A; A=16-222.
DR   PDBsum; 4LG1; -.
DR   PDBsum; 7OAT; -.
DR   PDBsum; 8HL6; -.
DR   PDBsum; 8HL7; -.
DR   AlphaFoldDB; Q9H867; -.
DR   SMR; Q9H867; -.
DR   BioGRID; 122744; 17.
DR   IntAct; Q9H867; 3.
DR   STRING; 9606.ENSP00000379201; -.
DR   ChEMBL; CHEMBL3588742; -.
DR   iPTMnet; Q9H867; -.
DR   PhosphoSitePlus; Q9H867; -.
DR   BioMuta; VCPKMT; -.
DR   DMDM; 152031572; -.
DR   EPD; Q9H867; -.
DR   MassIVE; Q9H867; -.
DR   MaxQB; Q9H867; -.
DR   PaxDb; 9606-ENSP00000379201; -.
DR   PeptideAtlas; Q9H867; -.
DR   ProteomicsDB; 81183; -. [Q9H867-4]
DR   ProteomicsDB; 81184; -. [Q9H867-1]
DR   ProteomicsDB; 81185; -. [Q9H867-2]
DR   ProteomicsDB; 81186; -. [Q9H867-3]
DR   ProteomicsDB; 81187; -. [Q9H867-5]
DR   Pumba; Q9H867; -.
DR   Antibodypedia; 10369; 36 antibodies from 12 providers.
DR   DNASU; 79609; -.
DR   Ensembl; ENST00000395859.2; ENSP00000379200.2; ENSG00000100483.14. [Q9H867-5]
DR   Ensembl; ENST00000395860.7; ENSP00000379201.2; ENSG00000100483.14. [Q9H867-4]
DR   Ensembl; ENST00000491402.5; ENSP00000437113.1; ENSG00000100483.14. [Q9H867-1]
DR   GeneID; 79609; -.
DR   KEGG; hsa:79609; -.
DR   MANE-Select; ENST00000395860.7; ENSP00000379201.2; NM_024558.3; NP_078834.2.
DR   UCSC; uc001wxo.2; human. [Q9H867-4]
DR   AGR; HGNC:20352; -.
DR   CTD; 79609; -.
DR   GeneCards; VCPKMT; -.
DR   HGNC; HGNC:20352; VCPKMT.
DR   HPA; ENSG00000100483; Low tissue specificity.
DR   MIM; 615260; gene.
DR   neXtProt; NX_Q9H867; -.
DR   OpenTargets; ENSG00000100483; -.
DR   PharmGKB; PA134866014; -.
DR   VEuPathDB; HostDB:ENSG00000100483; -.
DR   eggNOG; KOG2793; Eukaryota.
DR   GeneTree; ENSGT00940000157135; -.
DR   HOGENOM; CLU_1890393_0_0_1; -.
DR   InParanoid; Q9H867; -.
DR   OMA; IYITDQE; -.
DR   OrthoDB; 153402at2759; -.
DR   PhylomeDB; Q9H867; -.
DR   TreeFam; TF352990; -.
DR   PathwayCommons; Q9H867; -.
DR   Reactome; R-HSA-8876725; Protein methylation.
DR   SignaLink; Q9H867; -.
DR   SIGNOR; Q9H867; -.
DR   BioGRID-ORCS; 79609; 21 hits in 1133 CRISPR screens.
DR   ChiTaRS; VCPKMT; human.
DR   GenomeRNAi; 79609; -.
DR   Pharos; Q9H867; Tbio.
DR   PRO; PR:Q9H867; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; Q9H867; Protein.
DR   Bgee; ENSG00000100483; Expressed in endothelial cell and 191 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR   GO; GO:0051117; F:ATPase binding; IPI:UniProtKB.
DR   GO; GO:0042054; F:histone methyltransferase activity; IEA:RHEA.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0032780; P:negative regulation of ATP-dependent activity; IMP:UniProtKB.
DR   GO; GO:0018022; P:peptidyl-lysine methylation; IMP:UniProtKB.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; IDA:UniProtKB.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR019410; Methyltransf_16.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR14614; HEPATOCELLULAR CARCINOMA-ASSOCIATED ANTIGEN; 1.
DR   PANTHER; PTHR14614:SF158; PROTEIN N-LYSINE METHYLTRANSFERASE METTL21D; 1.
DR   Pfam; PF10294; Methyltransf_16; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   Genevisible; Q9H867; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW   Methyltransferase; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..229
FT                   /note="Protein N-lysine methyltransferase METTL21D"
FT                   /id="PRO_0000089937"
FT   BINDING         43
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         75..77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         96
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         126
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         143
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.9"
FT   BINDING         148
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000269|Ref.9"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         8
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..89
FT                   /note="MADTLESSLEDPLRSFVRVLEKRDGTVLRLQQYSSGGVGCVVWDAAIVLSKY
FT                   LETPEFSGDGAHALSRRSVLELGSGTGAVGLMAATLG -> MWGRLLQAFPPVPTPQST
FT                   LFYR (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_008814"
FT   VAR_SEQ         90..229
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_008815"
FT   VAR_SEQ         123..144
FT                   /note="VLKWGEEIEGFPSPPDFILMAD -> GGRNRRLSFSTRLHTDGRLHIL (in
FT                   isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026586"
FT   VAR_SEQ         145..229
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_026587"
FT   VAR_SEQ         191..229
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_008816"
FT   VAR_SEQ         191..225
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043258"
FT   VARIANT         63
FT                   /note="A -> D (in dbSNP:rs11157729)"
FT                   /id="VAR_059621"
FT   MUTAGEN         73
FT                   /note="E->Q: Loss of methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:23349634"
FT   MUTAGEN         96
FT                   /note="D->A,V: Loss of methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:22948820"
FT   MUTAGEN         144
FT                   /note="D->V: Loss of methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:22948820"
FT   STRAND          8..10
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   HELIX           12..16
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          17..21
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          27..33
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          35..37
FT                   /evidence="ECO:0007829|PDB:8HL6"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:8HL7"
FT   HELIX           44..53
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   HELIX           56..59
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          61..63
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   TURN            65..68
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   HELIX           80..86
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          91..96
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   HELIX           101..110
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          116..123
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          138..144
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   HELIX           149..151
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   HELIX           153..162
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          168..174
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   HELIX           181..192
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   TURN            193..195
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          196..200
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   HELIX           203..205
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          208..210
FT                   /evidence="ECO:0007829|PDB:4LG1"
FT   STRAND          215..222
FT                   /evidence="ECO:0007829|PDB:4LG1"
SQ   SEQUENCE   229 AA;  25807 MW;  73B22FC1D14F12C7 CRC64;
     MADTLESSLE DPLRSFVRVL EKRDGTVLRL QQYSSGGVGC VVWDAAIVLS KYLETPEFSG
     DGAHALSRRS VLELGSGTGA VGLMAATLGA DVVVTDLEEL QDLLKMNINM NKHLVTGSVQ
     AKVLKWGEEI EGFPSPPDFI LMADCIYYEE SLEPLLKTLK DISGFETCII CCYEQRTMGK
     NPEIEKKYFE LLQLDFDFEK IPLEKHDEEY RSEDIHIIYI RKKKSKFPS
//