MT21D_HUMAN
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 03-AUG-2022, entry version 150.
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 PDBsum; 4LG1; -.
DR AlphaFoldDB; Q9H867; -.
DR SMR; Q9H867; -.
DR BioGRID; 122744; 16.
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; Q9H867; -.
DR PeptideAtlas; Q9H867; -.
DR PRIDE; 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 Antibodypedia; 10369; 23 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 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; RFMKMAK; -.
DR OrthoDB; 1494909at2759; -.
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; 19 hits in 1055 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 189 other tissues.
DR Genevisible; Q9H867; HS.
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: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 GO; GO:0006479; P:protein methylation; TAS:Reactome.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR019410; Methyltransf_16.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR14614; PTHR14614; 1.
DR Pfam; PF10294; Methyltransf_16; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
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 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
