GenomeNet

Database: UniProt/SWISS-PROT
Entry: KMT5C_HUMAN
LinkDB: KMT5C_HUMAN
Original site: KMT5C_HUMAN 
ID   KMT5C_HUMAN             Reviewed;         462 AA.
AC   Q86Y97; Q8WZ10; Q9BRZ6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   07-OCT-2020, entry version 146.
DE   RecName: Full=Histone-lysine N-methyltransferase KMT5C {ECO:0000305};
DE   AltName: Full=Lysine N-methyltransferase 5C;
DE   AltName: Full=Lysine-specific methyltransferase 5C {ECO:0000312|HGNC:HGNC:28405};
DE   AltName: Full=Suppressor of variegation 4-20 homolog 2;
DE            Short=Su(var)4-20 homolog 2;
DE            Short=Suv4-20h2;
DE   AltName: Full=[histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B {ECO:0000305};
DE            EC=2.1.1.362 {ECO:0000269|PubMed:24396869, ECO:0000269|PubMed:28114273};
DE   AltName: Full=[histone H4]-lysine20 N-methyltransferase KMT5B {ECO:0000305};
DE            EC=2.1.1.361 {ECO:0000269|PubMed:24396869};
GN   Name=KMT5C {ECO:0000312|HGNC:HGNC:28405}; Synonyms=SUV420H2;
GN   ORFNames=PP7130;
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 GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Cervix;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-129 (ISOFORM 1).
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-416, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-416 AND THR-422, AND
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   [6]
RP   CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND FUNCTION.
RX   PubMed=28114273; DOI=10.1038/nchembio.2282;
RA   Bromberg K.D., Mitchell T.R., Upadhyay A.K., Jakob C.G., Jhala M.A.,
RA   Comess K.M., Lasko L.M., Li C., Tuzon C.T., Dai Y., Li F., Eram M.S.,
RA   Nuber A., Soni N.B., Manaves V., Algire M.A., Sweis R.F., Torrent M.,
RA   Schotta G., Sun C., Michaelides M.R., Shoemaker A.R., Arrowsmith C.H.,
RA   Brown P.J., Santhakumar V., Martin A., Rice J.C., Chiang G.G., Vedadi M.,
RA   Barsyte-Lovejoy D., Pappano W.N.;
RT   "The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic
RT   integrity.";
RL   Nat. Chem. Biol. 13:317-324(2017).
RN   [7] {ECO:0000244|PDB:3RQ4}
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-248 IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE AND ZINC, CATALYTIC ACTIVITY, FUNCTION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=24396869; DOI=10.1016/j.febslet.2013.10.020;
RA   Wu H., Siarheyeva A., Zeng H., Lam R., Dong A., Wu X.H., Li Y.,
RA   Schapira M., Vedadi M., Min J.;
RT   "Crystal structures of the human histone H4K20 methyltransferases SUV420H1
RT   and SUV420H2.";
RL   FEBS Lett. 587:3859-3868(2013).
CC   -!- FUNCTION: Histone methyltransferase that specifically methylates
CC       monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2)
CC       of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2)
CC       and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription
CC       and maintenance of genome integrity (PubMed:24396869, PubMed:28114273).
CC       In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4
CC       and nucleosomes (PubMed:24396869). H4 'Lys-20' trimethylation
CC       represents a specific tag for epigenetic transcriptional repression.
CC       Mainly functions in pericentric heterochromatin regions, thereby
CC       playing a central role in the establishment of constitutive
CC       heterochromatin in these regions. KMT5C is targeted to histone H3 via
CC       its interaction with RB1 family proteins (RB1, RBL1 and RBL2) (By
CC       similarity). Facilitates TP53BP1 foci formation upon DNA damage and
CC       proficient non-homologous end-joining (NHEJ)-directed DNA repair by
CC       catalyzing the di- and trimethylation of 'Lys-20' of histone H4
CC       (PubMed:28114273). May play a role in class switch reconbination by
CC       catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By
CC       similarity). {ECO:0000250|UniProtKB:Q6Q783,
CC       ECO:0000269|PubMed:24396869, ECO:0000269|PubMed:28114273}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC         = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-
CC         COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; EC=2.1.1.362;
CC         Evidence={ECO:0000269|PubMed:24396869, ECO:0000269|PubMed:28114273};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC         Evidence={ECO:0000269|PubMed:28114273};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC         methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4]
CC         + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61992, Rhea:RHEA-
CC         COMP:15556, Rhea:RHEA-COMP:15998, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC         ChEBI:CHEBI:61976; Evidence={ECO:0000269|PubMed:28114273};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61993;
CC         Evidence={ECO:0000269|PubMed:28114273};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC         Evidence={ECO:0000269|PubMed:24396869};
CC   -!- ACTIVITY REGULATION: Inhibited by 6,7-Dichloro-N-cyclopentyl-4-
CC       (pyridin-4-yl)phthalazin-1-amine (A-196) with an IC(50) of 144 nM.
CC       {ECO:0000269|PubMed:28114273}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=21 uM for H4K20me0 {ECO:0000269|PubMed:24396869};
CC         KM=16 uM for H4K20me1 {ECO:0000269|PubMed:24396869};
CC         KM=0.5 uM for nucleosome {ECO:0000269|PubMed:24396869};
CC       pH dependence:
CC         Optimum pH is 8. {ECO:0000269|PubMed:24396869};
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with HP1 proteins CBX1,
CC       CBX3 and CBX5. Interacts with RB1 family proteins RB1, RBL1 and RBL2
CC       (By similarity). {ECO:0000250|UniProtKB:Q6Q783}.
CC   -!- INTERACTION:
CC       Q86Y97; Q13185: CBX3; NbExp=2; IntAct=EBI-7960569, EBI-78176;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}.
CC       Note=Associated with pericentric heterochromatin. CBX1 and CBX5 are
CC       required for the localization to pericentric heterochromatin (By
CC       similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q86Y97-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86Y97-2; Sequence=VSP_043947, VSP_043948;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. Histone-lysine methyltransferase family. Suvar4-20
CC       subfamily. {ECO:0000255|PROSITE-ProRule:PRU00903}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH05842.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=AAL55766.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
DR   EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005842; AAH05842.1; ALT_SEQ; mRNA.
DR   EMBL; BC019313; AAH19313.1; -; mRNA.
DR   EMBL; BC044889; AAH44889.1; -; mRNA.
DR   EMBL; AF289582; AAL55766.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS12922.1; -. [Q86Y97-1]
DR   RefSeq; NP_116090.2; NM_032701.3. [Q86Y97-1]
DR   RefSeq; XP_005259395.1; XM_005259338.3.
DR   RefSeq; XP_006723505.1; XM_006723442.3.
DR   RefSeq; XP_011525717.1; XM_011527415.2. [Q86Y97-1]
DR   PDB; 3RQ4; X-ray; 1.80 A; A=2-248.
DR   PDBsum; 3RQ4; -.
DR   SMR; Q86Y97; -.
DR   BioGRID; 124257; 12.
DR   IntAct; Q86Y97; 5.
DR   MINT; Q86Y97; -.
DR   STRING; 9606.ENSP00000255613; -.
DR   BindingDB; Q86Y97; -.
DR   ChEMBL; CHEMBL2321644; -.
DR   GuidetoPHARMACOLOGY; 2718; -.
DR   iPTMnet; Q86Y97; -.
DR   PhosphoSitePlus; Q86Y97; -.
DR   BioMuta; KMT5C; -.
DR   DMDM; 74727906; -.
DR   EPD; Q86Y97; -.
DR   jPOST; Q86Y97; -.
DR   MassIVE; Q86Y97; -.
DR   MaxQB; Q86Y97; -.
DR   PaxDb; Q86Y97; -.
DR   PeptideAtlas; Q86Y97; -.
DR   PRIDE; Q86Y97; -.
DR   ProteomicsDB; 70387; -. [Q86Y97-1]
DR   ProteomicsDB; 70388; -. [Q86Y97-2]
DR   ABCD; Q86Y97; 1 sequenced antibody.
DR   Antibodypedia; 46420; 61 antibodies.
DR   Ensembl; ENST00000255613; ENSP00000255613; ENSG00000133247. [Q86Y97-1]
DR   Ensembl; ENST00000445196; ENSP00000397296; ENSG00000133247. [Q86Y97-2]
DR   Ensembl; ENST00000592631; ENSP00000467499; ENSG00000133247. [Q86Y97-2]
DR   GeneID; 84787; -.
DR   KEGG; hsa:84787; -.
DR   UCSC; uc002qkj.5; human. [Q86Y97-1]
DR   CTD; 84787; -.
DR   DisGeNET; 84787; -.
DR   EuPathDB; HostDB:ENSG00000133247.13; -.
DR   GeneCards; KMT5C; -.
DR   HGNC; HGNC:28405; KMT5C.
DR   HPA; ENSG00000133247; Low tissue specificity.
DR   MIM; 613198; gene.
DR   neXtProt; NX_Q86Y97; -.
DR   OpenTargets; ENSG00000133247; -.
DR   PharmGKB; PA134934307; -.
DR   eggNOG; KOG2589; Eukaryota.
DR   GeneTree; ENSGT00940000161700; -.
DR   HOGENOM; CLU_040002_0_0_1; -.
DR   InParanoid; Q86Y97; -.
DR   KO; K11429; -.
DR   OMA; LHRWGGC; -.
DR   OrthoDB; 236983at2759; -.
DR   PhylomeDB; Q86Y97; -.
DR   TreeFam; TF106433; -.
DR   BioCyc; MetaCyc:HS13469-MONOMER; -.
DR   PathwayCommons; Q86Y97; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   BioGRID-ORCS; 84787; 4 hits in 872 CRISPR screens.
DR   ChiTaRS; KMT5C; human.
DR   GenomeRNAi; 84787; -.
DR   Pharos; Q86Y97; Tchem.
DR   PRO; PR:Q86Y97; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q86Y97; protein.
DR   Bgee; ENSG00000133247; Expressed in layer of synovial tissue and 220 other tissues.
DR   ExpressionAtlas; Q86Y97; baseline and differential.
DR   Genevisible; Q86Y97; HS.
DR   GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IEA:Ensembl.
DR   GO; GO:0005720; C:nuclear heterochromatin; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005721; C:pericentric heterochromatin; IDA:BHF-UCL.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; IBA:GO_Central.
DR   GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IMP:UniProtKB.
DR   GO; GO:0045830; P:positive regulation of isotype switching; ISS:UniProtKB.
DR   Gene3D; 1.10.10.1700; -; 1.
DR   InterPro; IPR041938; Hist-Lys_N-MTase_N.
DR   InterPro; IPR025790; Hist-Lys_N-MTase_Suvar4-20.
DR   InterPro; IPR039977; KMT5B/KMT5C/SET9.
DR   InterPro; IPR001214; SET_dom.
DR   PANTHER; PTHR12977; PTHR12977; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW   Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc.
FT   CHAIN           1..462
FT                   /note="Histone-lysine N-methyltransferase KMT5C"
FT                   /id="PRO_0000281793"
FT   DOMAIN          104..218
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   REGION          114..117
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   REGION          182..183
FT                   /note="S-adenosyl-L-methionine binding"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   REGION          346..435
FT                   /note="Required for heterochromatin localization"
FT                   /evidence="ECO:0000250"
FT   METAL           185
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   METAL           229
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   METAL           231
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   METAL           234
FT                   /note="Zinc"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   BINDING         32
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   BINDING         121
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   BINDING         160
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   BINDING         169
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   BINDING         230
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen"
FT                   /evidence="ECO:0000244|PDB:3RQ4,
FT                   ECO:0000269|PubMed:24396869"
FT   MOD_RES         416
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:19690332,
FT                   ECO:0000244|PubMed:20068231"
FT   MOD_RES         422
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:20068231"
FT   VAR_SEQ         37..97
FT                   /note="SPVPPLRRQQHLRSALETFLRQRDLEAAYRALTLGGWTARYFQSRGPRQEAA
FT                   LKTHVYRYL -> RSIATSVPSCRKVALPSCPARATPWRPTGPRSCPLVLGKRMRSWSC
FT                   WWAALQSCGRQMRGC (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043947"
FT   VAR_SEQ         98..462
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_043948"
FT   HELIX           8..27
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   HELIX           45..58
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   HELIX           61..69
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   TURN            70..78
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   HELIX           83..99
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   HELIX           102..104
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   STRAND          106..110
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   STRAND          121..127
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   STRAND          134..144
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   HELIX           147..152
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   TURN            155..157
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   STRAND          162..165
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   TURN            166..169
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   STRAND          170..176
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   HELIX           177..180
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   STRAND          188..194
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   TURN            195..197
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   STRAND          198..205
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   STRAND          221..223
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   HELIX           224..226
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   HELIX           232..237
FT                   /evidence="ECO:0000244|PDB:3RQ4"
FT   HELIX           240..242
FT                   /evidence="ECO:0000244|PDB:3RQ4"
SQ   SEQUENCE   462 AA;  52113 MW;  6814F7BDFA109070 CRC64;
     MGPDRVTARE LCENDDLATS LVLDPYLGFR THKMNVSPVP PLRRQQHLRS ALETFLRQRD
     LEAAYRALTL GGWTARYFQS RGPRQEAALK THVYRYLRAF LPESGFTILP CTRYSMETNG
     AKIVSTRAWK KNEKLELLVG CIAELREADE GLLRAGENDF SIMYSTRKRS AQLWLGPAAF
     INHDCKPNCK FVPADGNAAC VKVLRDIEPG DEVTCFYGEG FFGEKNEHCE CHTCERKGEG
     AFRTRPREPA LPPRPLDKYQ LRETKRRLQQ GLDSGSRQGL LGPRACVHPS PLRRDPFCAA
     CQPLRLPACS ARPDTSPLWL QWLPQPQPRV RPRKRRRPRP RRAPVLSTHH AARVSLHRWG
     GCGPHCRLRG EALVALGQPP HARWAPQQDW HWARRYGLPY VVRVDLRRLA PAPPATPAPA
     GTPGPILIPK QALAFAPFSP PKRLRLVVSH GSIDLDVGGE EL
//
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