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 27-MAR-2024, entry version 206. 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/"; 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; 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; 9606-ENSP00000335357; -. DR PeptideAtlas; Q16667; -. DR ProteomicsDB; 61026; -. [Q16667-1] DR ProteomicsDB; 61027; -. [Q16667-2] DR Pumba; Q16667; -. DR Antibodypedia; 3940; 582 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 AGR; HGNC:1791; -. 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; CRYKDIR; -. DR OrthoDB; 5479521at2759; -. DR PhylomeDB; Q16667; -. DR TreeFam; TF101040; -. DR PathwayCommons; Q16667; -. DR SignaLink; Q16667; -. DR SIGNOR; Q16667; -. DR BioGRID-ORCS; 1033; 6 hits in 1172 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 142 other cell types or tissues. DR ExpressionAtlas; Q16667; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. 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:0016311; P:dephosphorylation; IEA:InterPro. 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: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 CDD; cd14505; CDKN3-like; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 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 PANTHER; PTHR23339:SF98; CYCLIN-DEPENDENT KINASE INHIBITOR 3-RELATED; 1. DR PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1. DR Pfam; PF05706; CDKN3; 1. DR PIRSF; PIRSF037322; CDKN3; 1. DR SMART; SM00404; PTPc_motif; 1. DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1. DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1. DR PROSITE; PS50054; TYR_PHOSPHATASE_DUAL; 1. DR Genevisible; Q16667; HS. 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 //