CDKN3_HUMAN
ID CDKN3_HUMAN Reviewed; 212 AA.
AC Q16667; Q53ZU6; Q5U0M4; Q6P1N8; Q99585; Q9BPW7; Q9BY36; Q9C042; Q9C046;
AC Q9C047; Q9C049; Q9C051; Q9C053;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Cyclin-dependent kinase inhibitor 3 {ECO:0000305};
DE EC=3.1.3.16 {ECO:0000269|PubMed:7569954};
DE EC=3.1.3.48 {ECO:0000269|PubMed:8127873, ECO:0000269|PubMed:8242750};
DE AltName: Full=CDK2-associated dual-specificity phosphatase;
DE AltName: Full=Cyclin-dependent kinase interactor 1;
DE AltName: Full=Cyclin-dependent kinase-interacting protein 2;
DE AltName: Full=Kinase-associated phosphatase;
GN Name=CDKN3 {ECO:0000312|HGNC:HGNC:1791}; Synonyms=CDI1, CIP2, KAP;
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), FUNCTION, CATALYTIC ACTIVITY, AND
RP INTERACTION WITH CDK1; CDK2 AND CDK3.
RX PubMed=8242750; DOI=10.1016/0092-8674(93)90498-f;
RA Gyuris J., Golemis E., Chertkov H., Brent R.;
RT "Cdi1, a human G1 and S phase protein phosphatase that associates with
RT Cdk2.";
RL Cell 75:791-803(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, AND
RP INTERACTION WITH CDK1 AND CDK2.
RX PubMed=8127873; DOI=10.1073/pnas.91.5.1731;
RA Hannon G.J., Casso D., Beach D.;
RT "KAP: a dual specificity phosphatase that interacts with cyclin-dependent
RT kinases.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1731-1735(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANTS HCC ARG-31;
RP LEU-78; TYR-79; LYS-91; VAL-94; PHE-95; VAL-108; SER-187 AND ILE-195.
RX PubMed=10987270;
RA Yeh C.-T., Lu S.-C., Chen T.-C., Peng C.-Y., Liaw Y.-F.;
RT "Aberrant transcripts of the cyclin-dependent kinase-associated protein
RT phosphatase in hepatocellular carcinoma.";
RL Cancer Res. 60:4697-4700(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CDK2.
RX PubMed=12745075; DOI=10.1016/s0006-291x(03)00757-5;
RA Yeh C.-T., Lu S.-C., Chao C.-H., Chao M.-L.;
RT "Abolishment of the interaction between cyclin-dependent kinase 2 and Cdk-
RT associated protein phosphatase by a truncated KAP mutant.";
RL Biochem. Biophys. Res. Commun. 305:311-314(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Harper W., Elledge S.J.;
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Schupp I.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Retinoblastoma;
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 [12]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=7569954; DOI=10.1126/science.270.5233.90;
RA Poon R.Y.C., Hunter T.;
RT "Dephosphorylation of Cdk2 Thr160 by the cyclin-dependent kinase-
RT interacting phosphatase KAP in the absence of cyclin.";
RL Science 270:90-93(1995).
RN [13]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=10669749; DOI=10.1128/mcb.20.5.1723-1732.2000;
RA Lee S.W., Reimer C.L., Fang L., Iruela-Arispe M.L., Aaronson S.A.;
RT "Overexpression of kinase-associated phosphatase (KAP) in breast and
RT prostate cancer and inhibition of the transformed phenotype by antisense
RT KAP expression.";
RL Mol. Cell. Biol. 20:1723-1732(2000).
RN [14]
RP INTERACTION WITH MS4A3.
RX PubMed=11781350; DOI=10.1172/jci14025;
RA Donato J.-L., Ko J., Kutok J.L., Cheng T., Shirakawa T., Mao X.-Q.,
RA Beach D., Scadden D.T., Sayegh M.H., Adra C.N.;
RT "Human HTm4 is a hematopoietic cell cycle regulator.";
RL J. Clin. Invest. 109:51-58(2002).
RN [15]
RP INTERACTION WITH MS4A3.
RX PubMed=15671017; DOI=10.1074/jbc.m413437200;
RA Chinami M., Yano Y., Yang X., Salahuddin S., Moriyama K., Shiroishi M.,
RA Turner H., Shirakawa T., Adra C.N.;
RT "Binding of HTm4 to cyclin-dependent kinase (Cdk)-associated phosphatase
RT (KAP).Cdk2.cyclin A complex enhances the phosphatase activity of KAP,
RT dissociates cyclin A, and facilitates KAP dephosphorylation of Cdk2.";
RL J. Biol. Chem. 280:17235-17242(2005).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH THR-160
RP PHOSPHORYLATED CDK2.
RX PubMed=11463386; DOI=10.1016/s1097-2765(01)00208-8;
RA Song H., Hanlon N., Brown N.R., Noble M.E.M., Johnson L.N., Barford D.;
RT "Phosphoprotein-protein interactions revealed by the crystal structure of
RT kinase-associated phosphatase in complex with phosphoCDK2.";
RL Mol. Cell 7:615-626(2001).
CC -!- FUNCTION: May play a role in cell cycle regulation. Dual specificity CC
CC phosphatase active toward substrates containing either phosphotyrosine
CC or phosphoserine residues (PubMed:8127873, PubMed:8242750).
CC Dephosphorylates CDK2 at 'Thr-160' in a cyclin-dependent manner
CC (PubMed:7569954). {ECO:0000269|PubMed:7569954,
CC ECO:0000269|PubMed:8127873, ECO:0000269|PubMed:8242750}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:8127873,
CC ECO:0000269|PubMed:8242750};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10685;
CC Evidence={ECO:0000305|PubMed:8242750};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:7569954};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:47005;
CC Evidence={ECO:0000305|PubMed:7569954};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:8127873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20630;
CC Evidence={ECO:0000305|PubMed:8127873};
CC -!- SUBUNIT: Interacts with cyclin-dependent kinases such as CDK1, CDK2 and
CC CDK3. Does not interact with CDK4. Interacts (via C-terminus) with
CC phosphorylated CDK2 (via C-terminal helix). Interacts with MS4A3 (via
CC C-terminus); the interaction enhances CDKN3 enzymatic activity.
CC {ECO:0000269|PubMed:11463386, ECO:0000269|PubMed:11781350,
CC ECO:0000269|PubMed:12745075, ECO:0000269|PubMed:15671017,
CC ECO:0000269|PubMed:8127873, ECO:0000269|PubMed:8242750}.
CC -!- INTERACTION:
CC Q16667; P24941: CDK2; NbExp=7; IntAct=EBI-1031527, EBI-375096;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:10669749}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16667-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16667-2; Sequence=VSP_036613;
CC -!- INDUCTION: Up-regulated in breast and prostate cancer cells.
CC {ECO:0000269|PubMed:10669749}.
CC -!- DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary
CC malignant neoplasm of epithelial liver cells. The major risk factors
CC for HCC are chronic hepatitis B virus (HBV) infection, chronic
CC hepatitis C virus (HCV) infection, prolonged dietary aflatoxin
CC exposure, alcoholic cirrhosis, and cirrhosis due to other causes.
CC {ECO:0000269|PubMed:10987270}. Note=The gene represented in this entry
CC may be involved in disease pathogenesis.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/cdkn3/";
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DR EMBL; U02681; AAC04932.1; -; mRNA.
DR EMBL; L27711; AAA66496.1; -; mRNA.
DR EMBL; AF213033; AAK06365.1; -; mRNA.
DR EMBL; AF213036; AAK06368.1; -; mRNA.
DR EMBL; AF213038; AAK06370.1; -; mRNA.
DR EMBL; AF213039; AAK06371.1; -; mRNA.
DR EMBL; AF213041; AAK06373.1; -; mRNA.
DR EMBL; AF213042; AAK06374.1; -; mRNA.
DR EMBL; AF213046; AAK06377.1; -; mRNA.
DR EMBL; AF213047; AAK06378.1; -; mRNA.
DR EMBL; AF213049; AAK06380.1; -; mRNA.
DR EMBL; AF213053; AAK06384.1; -; mRNA.
DR EMBL; AY257474; AAP13062.1; -; mRNA.
DR EMBL; L25876; AAA60222.1; -; mRNA.
DR EMBL; EF560750; ABQ59060.1; -; mRNA.
DR EMBL; CR407666; CAG28594.1; -; mRNA.
DR EMBL; BT019451; AAV38258.1; -; mRNA.
DR EMBL; AY194117; AAN86348.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW80632.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW80634.1; -; Genomic_DNA.
DR EMBL; BC064965; AAH64965.1; -; mRNA.
DR CCDS; CCDS45109.1; -. [Q16667-2]
DR CCDS; CCDS9716.1; -. [Q16667-1]
DR PIR; A49436; A49436.
DR RefSeq; NP_001124323.1; NM_001130851.1. [Q16667-2]
DR RefSeq; NP_005183.2; NM_005192.3. [Q16667-1]
DR PDB; 1FPZ; X-ray; 2.00 A; A/B/C/D/E/F=1-212.
DR PDB; 1FQ1; X-ray; 3.00 A; A=1-212.
DR PDBsum; 1FPZ; -.
DR PDBsum; 1FQ1; -.
DR AlphaFoldDB; Q16667; -.
DR SMR; Q16667; -.
DR BioGRID; 107467; 52.
DR DIP; DIP-245N; -.
DR IntAct; Q16667; 10.
DR MINT; Q16667; -.
DR STRING; 9606.ENSP00000335357; -.
DR DEPOD; CDKN3; -.
DR iPTMnet; Q16667; -.
DR PhosphoSitePlus; Q16667; -.
DR BioMuta; CDKN3; -.
DR DMDM; 2499769; -.
DR EPD; Q16667; -.
DR jPOST; Q16667; -.
DR MassIVE; Q16667; -.
DR MaxQB; Q16667; -.
DR PaxDb; Q16667; -.
DR PeptideAtlas; Q16667; -.
DR PRIDE; Q16667; -.
DR ProteomicsDB; 61026; -. [Q16667-1]
DR ProteomicsDB; 61027; -. [Q16667-2]
DR Antibodypedia; 3940; 532 antibodies from 31 providers.
DR DNASU; 1033; -.
DR Ensembl; ENST00000335183.11; ENSP00000335357.6; ENSG00000100526.21. [Q16667-1]
DR Ensembl; ENST00000442975.6; ENSP00000415333.2; ENSG00000100526.21. [Q16667-2]
DR GeneID; 1033; -.
DR KEGG; hsa:1033; -.
DR MANE-Select; ENST00000335183.11; ENSP00000335357.6; NM_005192.4; NP_005183.2.
DR UCSC; uc001xap.4; human. [Q16667-1]
DR CTD; 1033; -.
DR DisGeNET; 1033; -.
DR GeneCards; CDKN3; -.
DR HGNC; HGNC:1791; CDKN3.
DR HPA; ENSG00000100526; Tissue enriched (testis).
DR MalaCards; CDKN3; -.
DR MIM; 114550; phenotype.
DR MIM; 123832; gene.
DR neXtProt; NX_Q16667; -.
DR OpenTargets; ENSG00000100526; -.
DR PharmGKB; PA26324; -.
DR VEuPathDB; HostDB:ENSG00000100526; -.
DR eggNOG; KOG1720; Eukaryota.
DR GeneTree; ENSGT00390000004717; -.
DR InParanoid; Q16667; -.
DR OMA; PFHISWL; -.
DR OrthoDB; 1539111at2759; -.
DR PhylomeDB; Q16667; -.
DR TreeFam; TF101040; -.
DR PathwayCommons; Q16667; -.
DR SignaLink; Q16667; -.
DR SIGNOR; Q16667; -.
DR BioGRID-ORCS; 1033; 5 hits in 1093 CRISPR screens.
DR ChiTaRS; CDKN3; human.
DR EvolutionaryTrace; Q16667; -.
DR GeneWiki; CDKN3; -.
DR GenomeRNAi; 1033; -.
DR Pharos; Q16667; Tbio.
DR PRO; PR:Q16667; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q16667; protein.
DR Bgee; ENSG00000100526; Expressed in left testis and 140 other tissues.
DR ExpressionAtlas; Q16667; baseline and differential.
DR Genevisible; Q16667; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:MGI.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:MGI.
DR GO; GO:0008138; F:protein tyrosine/serine/threonine phosphatase activity; TAS:ProtInc.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:ProtInc.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:ProtInc.
DR Gene3D; 3.90.190.10; -; 1.
DR IDEAL; IID00605; -.
DR InterPro; IPR008425; CDK_inhib_3.
DR InterPro; IPR022778; CDKN3.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR020422; TYR_PHOSPHATASE_DUAL_dom.
DR Pfam; PF05706; CDKN3; 1.
DR PIRSF; PIRSF037322; CDKN3; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; SSF52799; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cytoplasm; Disease variant;
KW Hydrolase; Protein phosphatase; Reference proteome.
FT CHAIN 1..212
FT /note="Cyclin-dependent kinase inhibitor 3"
FT /id="PRO_0000094949"
FT DOMAIN 33..201
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 1..34
FT /note="Interaction with CDK2"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 140
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT VAR_SEQ 11..50
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10987270,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_036613"
FT VARIANT 31
FT /note="W -> R (in HCC; patient BX-01)"
FT /evidence="ECO:0000269|PubMed:10987270"
FT /id="VAR_013842"
FT VARIANT 78
FT /note="F -> L (in HCC; patient T9)"
FT /evidence="ECO:0000269|PubMed:10987270"
FT /id="VAR_013843"
FT VARIANT 79
FT /note="C -> Y (in HCC; patient BX-01)"
FT /evidence="ECO:0000269|PubMed:10987270"
FT /id="VAR_013844"
FT VARIANT 91
FT /note="N -> K (in HCC; patient BX-10; dbSNP:rs760687800)"
FT /evidence="ECO:0000269|PubMed:10987270"
FT /id="VAR_013845"
FT VARIANT 94
FT /note="D -> V (in HCC; patient NT1)"
FT /evidence="ECO:0000269|PubMed:10987270"
FT /id="VAR_013846"
FT VARIANT 95
FT /note="L -> F (in HCC; patient BX-05)"
FT /evidence="ECO:0000269|PubMed:10987270"
FT /id="VAR_013847"
FT VARIANT 108
FT /note="I -> V (in HCC; patient T9; dbSNP:rs144479038)"
FT /evidence="ECO:0000269|PubMed:10987270"
FT /id="VAR_013848"
FT VARIANT 159
FT /note="S -> F (in dbSNP:rs1803843)"
FT /id="VAR_051769"
FT VARIANT 187
FT /note="N -> S (in HCC; patient NT4)"
FT /evidence="ECO:0000269|PubMed:10987270"
FT /id="VAR_013849"
FT VARIANT 195
FT /note="K -> I (in HCC; patient NT4)"
FT /evidence="ECO:0000269|PubMed:10987270"
FT /id="VAR_013850"
FT CONFLICT 2
FT /note="K -> E (in Ref. 1; AAC04932 and 8; AAV38258)"
FT /evidence="ECO:0000305"
FT CONFLICT 10
FT /note="S -> G (in Ref. 3; AAK06380)"
FT /evidence="ECO:0000305"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:1FPZ"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:1FPZ"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:1FPZ"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:1FPZ"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:1FPZ"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:1FPZ"
FT HELIX 92..98
FT /evidence="ECO:0007829|PDB:1FPZ"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:1FPZ"
FT HELIX 116..131
FT /evidence="ECO:0007829|PDB:1FPZ"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1FPZ"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:1FPZ"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:1FPZ"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1FQ1"
FT HELIX 164..175
FT /evidence="ECO:0007829|PDB:1FPZ"
FT HELIX 183..189
FT /evidence="ECO:0007829|PDB:1FPZ"
FT HELIX 192..197
FT /evidence="ECO:0007829|PDB:1FPZ"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:1FQ1"
SQ SEQUENCE 212 AA; 23805 MW; D87FAC8E28F6525F CRC64;
MKPPSSIQTS EFDSSDEEPI EDEQTPIHIS WLSLSRVNCS QFLGLCALPG CKFKDVRRNV
QKDTEELKSC GIQDIFVFCT RGELSKYRVP NLLDLYQQCG IITHHHPIAD GGTPDIASCC
EIMEELTTCL KNYRKTLIHC YGGLGRSCLV AACLLLYLSD TISPEQAIDS LRDLRGSGAI
QTIKQYNYLH EFRDKLAAHL SSRDSQSRSV SR
