ID ZCC17_HUMAN Reviewed; 241 AA. AC Q9NP64; B4DY38; D3DPN4; Q6PKH4; Q9NYG4; Q9P0M8; DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 188. DE RecName: Full=Zinc finger CCHC domain-containing protein 17; DE AltName: Full=Nucleolar protein of 40 kDa {ECO:0000303|PubMed:12893261}; DE Short=pNO40 {ECO:0000303|PubMed:12893261}; DE AltName: Full=Pnn-interacting nucleolar protein; DE AltName: Full=Putative S1 RNA-binding domain protein; DE Short=PS1D protein; GN Name=ZCCHC17; Synonyms=PS1D; ORFNames=HSPC243, HSPC251, LDC4; 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] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, RP SUBCELLULAR LOCATION, AND INTERACTION WITH PNN. RC TISSUE=Kidney; RX PubMed=12893261; DOI=10.1016/s0006-291x(03)01208-7; RA Chang W.-L., Lee D.-C., Leu S., Huang Y.-M., Lu M.-C., Ouyang P.; RT "Molecular characterization of a novel nucleolar protein, pNO40."; RL Biochem. Biophys. Res. Commun. 307:569-577(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Placenta, Retinoblastoma, Teratocarcinoma, and Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney, Muscle, and Uterus; 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY RP 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-183, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; 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 [11] RP STRUCTURE BY NMR OF 1-106. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the S1 RNA binding domain of human hypothetical RT protein FLJ11067."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- SUBUNIT: Interacts with PNN. Associates with the 60S ribosomal subunit CC (By similarity). {ECO:0000250}. CC -!- INTERACTION: CC Q9NP64; Q9BXS5: AP1M1; NbExp=7; IntAct=EBI-746345, EBI-541426; CC Q9NP64; Q08426: EHHADH; NbExp=3; IntAct=EBI-746345, EBI-2339219; CC Q9NP64; P22607: FGFR3; NbExp=3; IntAct=EBI-746345, EBI-348399; CC Q9NP64; Q14957: GRIN2C; NbExp=3; IntAct=EBI-746345, EBI-8285963; CC Q9NP64; P06396: GSN; NbExp=3; IntAct=EBI-746345, EBI-351506; CC Q9NP64; Q6NYC1: JMJD6; NbExp=2; IntAct=EBI-746345, EBI-8464037; CC Q9NP64; Q9BS40: LXN; NbExp=3; IntAct=EBI-746345, EBI-1044504; CC Q9NP64; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-746345, EBI-741158; CC Q9NP64; P78317: RNF4; NbExp=3; IntAct=EBI-746345, EBI-2340927; CC Q9NP64; O00560: SDCBP; NbExp=8; IntAct=EBI-746345, EBI-727004; CC Q9NP64; Q9H190: SDCBP2; NbExp=8; IntAct=EBI-746345, EBI-742426; CC Q9NP64; A0MZ66-4: SHTN1; NbExp=3; IntAct=EBI-746345, EBI-12097232; CC Q9NP64; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-746345, EBI-741480; CC Q9NP64; Q9NP64: ZCCHC17; NbExp=3; IntAct=EBI-746345, EBI-746345; CC Q9NP64; P17020: ZNF16; NbExp=3; IntAct=EBI-746345, EBI-3921553; CC Q9NP64; Q9Y649; NbExp=3; IntAct=EBI-746345, EBI-25900580; CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12893261}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=hpNO40; CC IsoId=Q9NP64-1; Sequence=Displayed; CC Name=2; Synonyms=hpNO40s; CC IsoId=Q9NP64-2; Sequence=VSP_015308; CC Name=3; CC IsoId=Q9NP64-3; Sequence=VSP_054531; CC -!- SEQUENCE CAUTION: CC Sequence=AAF36171.1; Type=Frameshift; Evidence={ECO:0000305}; 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; AF247661; AAF72518.3; -; mRNA. DR EMBL; AF151077; AAF36163.1; -; mRNA. DR EMBL; AF151085; AAF36171.1; ALT_FRAME; mRNA. DR EMBL; AK001929; BAA91984.1; -; mRNA. DR EMBL; AK022506; BAB14066.1; -; mRNA. DR EMBL; AK024049; BAB14799.1; -; mRNA. DR EMBL; AK302248; BAG63600.1; -; mRNA. DR EMBL; AL451070; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471059; EAX07620.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07621.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07622.1; -; Genomic_DNA. DR EMBL; CH471059; EAX07624.1; -; Genomic_DNA. DR EMBL; BC000685; AAH00685.1; -; mRNA. DR EMBL; BC007446; AAH07446.1; -; mRNA. DR EMBL; BC050609; AAH50609.1; -; mRNA. DR CCDS; CCDS341.1; -. [Q9NP64-1] DR CCDS; CCDS60061.1; -. [Q9NP64-3] DR RefSeq; NP_001269495.1; NM_001282566.1. DR RefSeq; NP_001269496.1; NM_001282567.1. DR RefSeq; NP_001269497.1; NM_001282568.1. [Q9NP64-1] DR RefSeq; NP_001269498.1; NM_001282569.1. [Q9NP64-3] DR RefSeq; NP_001269499.1; NM_001282570.1. [Q9NP64-2] DR RefSeq; NP_001269500.1; NM_001282571.1. DR RefSeq; NP_001269501.1; NM_001282572.1. DR RefSeq; NP_001269502.1; NM_001282573.1. DR RefSeq; NP_001269503.1; NM_001282574.1. DR RefSeq; NP_057589.2; NM_016505.3. [Q9NP64-1] DR RefSeq; XP_006710744.1; XM_006710681.3. DR RefSeq; XP_011539869.1; XM_011541567.2. DR PDB; 2CQO; NMR; -; A=1-106. DR PDBsum; 2CQO; -. DR AlphaFoldDB; Q9NP64; -. DR SMR; Q9NP64; -. DR BioGRID; 119598; 111. DR IntAct; Q9NP64; 68. DR MINT; Q9NP64; -. DR STRING; 9606.ENSP00000480986; -. DR iPTMnet; Q9NP64; -. DR MetOSite; Q9NP64; -. DR PhosphoSitePlus; Q9NP64; -. DR SwissPalm; Q9NP64; -. DR BioMuta; ZCCHC17; -. DR DMDM; 73921227; -. DR EPD; Q9NP64; -. DR jPOST; Q9NP64; -. DR MassIVE; Q9NP64; -. DR MaxQB; Q9NP64; -. DR PaxDb; 9606-ENSP00000480986; -. DR PeptideAtlas; Q9NP64; -. DR ProteomicsDB; 5494; -. DR ProteomicsDB; 81894; -. [Q9NP64-1] DR ProteomicsDB; 81895; -. [Q9NP64-2] DR Pumba; Q9NP64; -. DR Antibodypedia; 31100; 222 antibodies from 23 providers. DR DNASU; 51538; -. DR Ensembl; ENST00000344147.10; ENSP00000343557.5; ENSG00000121766.16. [Q9NP64-1] DR Ensembl; ENST00000373714.5; ENSP00000362819.1; ENSG00000121766.16. [Q9NP64-1] DR Ensembl; ENST00000546109.5; ENSP00000444742.1; ENSG00000121766.16. [Q9NP64-3] DR GeneID; 51538; -. DR KEGG; hsa:51538; -. DR MANE-Select; ENST00000344147.10; ENSP00000343557.5; NM_016505.4; NP_057589.2. DR UCSC; uc001bsp.3; human. [Q9NP64-1] DR AGR; HGNC:30246; -. DR CTD; 51538; -. DR DisGeNET; 51538; -. DR GeneCards; ZCCHC17; -. DR HGNC; HGNC:30246; ZCCHC17. DR HPA; ENSG00000121766; Tissue enhanced (brain). DR MIM; 619744; gene. DR neXtProt; NX_Q9NP64; -. DR OpenTargets; ENSG00000121766; -. DR PharmGKB; PA142670539; -. DR VEuPathDB; HostDB:ENSG00000121766; -. DR eggNOG; KOG0922; Eukaryota. DR GeneTree; ENSGT00510000047363; -. DR InParanoid; Q9NP64; -. DR OrthoDB; 3396261at2759; -. DR PhylomeDB; Q9NP64; -. DR TreeFam; TF332136; -. DR PathwayCommons; Q9NP64; -. DR SignaLink; Q9NP64; -. DR BioGRID-ORCS; 51538; 5 hits in 1154 CRISPR screens. DR ChiTaRS; ZCCHC17; human. DR EvolutionaryTrace; Q9NP64; -. DR GeneWiki; ZCCHC17; -. DR GenomeRNAi; 51538; -. DR Pharos; Q9NP64; Tbio. DR PRO; PR:Q9NP64; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9NP64; Protein. DR Bgee; ENSG00000121766; Expressed in C1 segment of cervical spinal cord and 184 other cell types or tissues. DR ExpressionAtlas; Q9NP64; baseline and differential. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IEA:Ensembl. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0043489; P:RNA stabilization; IBA:GO_Central. DR CDD; cd05686; S1_pNO40; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR003029; S1_domain. DR InterPro; IPR047913; ZCCHC17_S1. DR InterPro; IPR001878; Znf_CCHC. DR PANTHER; PTHR15838; NUCLEOLAR PROTEIN OF 40 KDA; 1. DR PANTHER; PTHR15838:SF1; ZINC FINGER CCHC DOMAIN-CONTAINING PROTEIN 17; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50126; S1; 1. DR PROSITE; PS50158; ZF_CCHC; 1. DR Genevisible; Q9NP64; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Ribonucleoprotein; Zinc; Zinc-finger. FT CHAIN 1..241 FT /note="Zinc finger CCHC domain-containing protein 17" FT /id="PRO_0000096902" FT DOMAIN 16..88 FT /note="S1 motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00180" FT ZN_FING 131..148 FT /note="CCHC-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047" FT REGION 161..241 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 161..183 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 198..219 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..241 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 114 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 144 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9ESX4" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..24 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12893261" FT /id="VSP_015308" FT VAR_SEQ 1..22 FT /note="MNSGRPETMENLPALYTIFQGE -> MKQLIEDTEKNKVY (in isoform FT 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_054531" FT CONFLICT 217 FT /note="R -> G (in Ref. 2; AAF36171)" FT /evidence="ECO:0000305" FT STRAND 18..27 FT /evidence="ECO:0007829|PDB:2CQO" FT STRAND 30..34 FT /evidence="ECO:0007829|PDB:2CQO" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:2CQO" FT HELIX 46..49 FT /evidence="ECO:0007829|PDB:2CQO" FT HELIX 57..60 FT /evidence="ECO:0007829|PDB:2CQO" FT STRAND 66..76 FT /evidence="ECO:0007829|PDB:2CQO" FT STRAND 81..87 FT /evidence="ECO:0007829|PDB:2CQO" FT STRAND 92..94 FT /evidence="ECO:0007829|PDB:2CQO" SQ SEQUENCE 241 AA; 27570 MW; DA1B039DAC5F4A1D CRC64; MNSGRPETME NLPALYTIFQ GEVAMVTDYG AFIKIPGCRK QGLVHRTHMS SCRVDKPSEI VDVGDKVWVK LIGREMKNDR IKVSLSMKVV NQGTGKDLDP NNVIIEQEER RRRSFQDYTG QKITLEAVLN TTCKKCGCKG HFAKDCFMQP GGTKYSLIPD EEEEKEEAKS AEFEKPDPTR NPSRKRKKEK KKKKHRDRKS SDSDSSDSES DTGKRARHTS KDSKAAKKKK KKKKHKKKHK E //