CPSF4_HUMAN
ID CPSF4_HUMAN Reviewed; 269 AA.
AC O95639; D6W5S8; Q6FGE6; Q86TF8; Q9BTW6;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 4;
DE AltName: Full=Cleavage and polyadenylation specificity factor 30 kDa subunit;
DE Short=CPSF 30 kDa subunit;
DE AltName: Full=NS1 effector domain-binding protein 1;
DE Short=Neb-1;
DE AltName: Full=No arches homolog;
GN Name=CPSF4; Synonyms=CPSF30, NAR, NEB1;
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).
RA Kawakami K., Gaiano N., Grosshans D., Scherer S., Tsui L.-C., Hopkins N.;
RT "Assignment of the human homolog of the zebrafish essential gene no arches
RT to 7q22.1.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P.,
RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y.,
RA LaBaer J.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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] (ISOFORMS 2 AND 3).
RC TISSUE=Eye, and PNS;
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 FUNCTION.
RX PubMed=9224719; DOI=10.1101/gad.11.13.1703;
RA Barabino S.M.L., Huebner W., Jenny A., Minvielle-Sebastia L., Keller W.;
RT "The 30-kD subunit of mammalian cleavage and polyadenylation specificity
RT factor and its yeast homolog are RNA-binding zinc finger proteins.";
RL Genes Dev. 11:1703-1716(1997).
RN [8]
RP INTERACTION WITH INFLUENZA A VIRUS NS1 PROTEIN (MICROBIAL INFECTION).
RX PubMed=9651582; DOI=10.1016/s1097-2765(00)80099-4;
RA Nemeroff M.E., Barabino S.M.L., Li Y., Keller W., Krug R.M.;
RT "Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of
RT CPSF and inhibits 3'end formation of cellular pre-mRNAs.";
RL Mol. Cell 1:991-1000(1998).
RN [9]
RP FUNCTION IN PRE-MRNA 3'-END PROCESSING, IDENTIFICATION IN THE CPSF COMPLEX,
RP AND INTERACTION WITH FIP1L1.
RX PubMed=14749727; DOI=10.1038/sj.emboj.7600070;
RA Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.;
RT "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and
RT stimulates poly(A) polymerase.";
RL EMBO J. 23:616-626(2004).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-212, AND
RP IDENTIFICATION BY 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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 AND SER-212, AND
RP IDENTIFICATION BY 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 [13]
RP IDENTIFICATION IN THE CPSF COMPLEX.
RX PubMed=21102410; DOI=10.1038/emboj.2010.287;
RA Laishram R.S., Anderson R.A.;
RT "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF
RT interaction and specificity toward the pre-mRNA.";
RL EMBO J. 29:4132-4145(2010).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212, 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200; SER-212 AND SER-267, 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 [17]
RP STRUCTURE BY NMR OF 61-126.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of CCCH-type zinc-finger domain 2 in cleavage and
RT polyadenylation specificity factor.";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex that play a key role in pre-mRNA 3'-end
CC formation, recognizing the AAUAAA signal sequence and interacting with
CC poly(A) polymerase and other factors to bring about cleavage and
CC poly(A) addition. CPSF4 binds RNA polymers with a preference for
CC poly(U). {ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:9224719}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC FIP1L1. Interacts with FIP1L1. {ECO:0000269|PubMed:14749727,
CC ECO:0000269|PubMed:21102410}.
CC -!- SUBUNIT: (Microbial infection) Interacts with influenza A virus NS1
CC blocks processing of pre-mRNAs, thereby preventing nuclear export of
CC host cell mRNAs. {ECO:0000269|PubMed:9651582}.
CC -!- INTERACTION:
CC O95639; Q6P1J9: CDC73; NbExp=3; IntAct=EBI-725860, EBI-930143;
CC O95639; P50222: MEOX2; NbExp=3; IntAct=EBI-725860, EBI-748397;
CC O95639; I6T1Z2: NS1; Xeno; NbExp=5; IntAct=EBI-725860, EBI-12561553;
CC O95639; Q194T2: NS1; Xeno; NbExp=5; IntAct=EBI-725860, EBI-11515076;
CC O95639-1; P03495: NS; Xeno; NbExp=4; IntAct=EBI-15725265, EBI-2548993;
CC O95639-2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-13063650, EBI-10172526;
CC O95639-2; P15173: MYOG; NbExp=3; IntAct=EBI-13063650, EBI-3906629;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95639-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95639-2; Sequence=VSP_008601;
CC Name=3;
CC IsoId=O95639-3; Sequence=VSP_008602;
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CPSF4/YTH1 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/cpsf4/";
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DR EMBL; U79569; AAD00321.1; -; mRNA.
DR EMBL; CR542161; CAG46958.1; -; mRNA.
DR EMBL; EF191081; ABN05292.1; -; Genomic_DNA.
DR EMBL; CH236956; EAL23878.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76667.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76668.1; -; Genomic_DNA.
DR EMBL; BC003101; AAH03101.1; -; mRNA.
DR EMBL; BC050738; AAH50738.1; -; mRNA.
DR CCDS; CCDS47652.1; -. [O95639-2]
DR CCDS; CCDS5664.1; -. [O95639-1]
DR RefSeq; NP_001075028.1; NM_001081559.2. [O95639-2]
DR RefSeq; NP_001305089.1; NM_001318160.1. [O95639-3]
DR RefSeq; NP_001305090.1; NM_001318161.1.
DR RefSeq; NP_001305091.1; NM_001318162.1.
DR RefSeq; NP_006684.1; NM_006693.3. [O95639-1]
DR PDB; 2D9N; NMR; -; A=61-126.
DR PDB; 2RHK; X-ray; 1.95 A; C/D=61-121.
DR PDB; 6DNH; EM; 3.40 A; C=1-269.
DR PDB; 6FBS; EM; 3.07 A; C=1-178.
DR PDB; 6FUW; EM; 3.07 A; C=1-178.
DR PDB; 6URG; EM; 3.00 A; C=1-269.
DR PDB; 6URO; EM; 3.60 A; C=1-269.
DR PDB; 7K95; X-ray; 1.90 A; A=114-173.
DR PDBsum; 2D9N; -.
DR PDBsum; 2RHK; -.
DR PDBsum; 6DNH; -.
DR PDBsum; 6FBS; -.
DR PDBsum; 6FUW; -.
DR PDBsum; 6URG; -.
DR PDBsum; 6URO; -.
DR PDBsum; 7K95; -.
DR AlphaFoldDB; O95639; -.
DR SMR; O95639; -.
DR BioGRID; 116104; 77.
DR CORUM; O95639; -.
DR DIP; DIP-48675N; -.
DR IntAct; O95639; 47.
DR MINT; O95639; -.
DR STRING; 9606.ENSP00000292476; -.
DR iPTMnet; O95639; -.
DR MetOSite; O95639; -.
DR PhosphoSitePlus; O95639; -.
DR SwissPalm; O95639; -.
DR BioMuta; CPSF4; -.
DR EPD; O95639; -.
DR jPOST; O95639; -.
DR MassIVE; O95639; -.
DR MaxQB; O95639; -.
DR PaxDb; O95639; -.
DR PeptideAtlas; O95639; -.
DR PRIDE; O95639; -.
DR ProteomicsDB; 50970; -. [O95639-1]
DR ProteomicsDB; 50971; -. [O95639-2]
DR ProteomicsDB; 50972; -. [O95639-3]
DR Antibodypedia; 16165; 227 antibodies from 30 providers.
DR DNASU; 10898; -.
DR Ensembl; ENST00000292476.10; ENSP00000292476.5; ENSG00000160917.15. [O95639-1]
DR Ensembl; ENST00000436336.6; ENSP00000395311.2; ENSG00000160917.15. [O95639-2]
DR GeneID; 10898; -.
DR KEGG; hsa:10898; -.
DR MANE-Select; ENST00000292476.10; ENSP00000292476.5; NM_006693.4; NP_006684.1.
DR UCSC; uc003uqi.4; human. [O95639-1]
DR CTD; 10898; -.
DR DisGeNET; 10898; -.
DR GeneCards; CPSF4; -.
DR HGNC; HGNC:2327; CPSF4.
DR HPA; ENSG00000160917; Low tissue specificity.
DR MIM; 603052; gene.
DR neXtProt; NX_O95639; -.
DR OpenTargets; ENSG00000160917; -.
DR PharmGKB; PA26844; -.
DR VEuPathDB; HostDB:ENSG00000160917; -.
DR eggNOG; KOG1040; Eukaryota.
DR GeneTree; ENSGT00940000155520; -.
DR HOGENOM; CLU_024513_0_1_1; -.
DR InParanoid; O95639; -.
DR OMA; NSCKQYV; -.
DR OrthoDB; 1472764at2759; -.
DR PhylomeDB; O95639; -.
DR TreeFam; TF314871; -.
DR PathwayCommons; O95639; -.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-168315; Inhibition of Host mRNA Processing and RNA Silencing.
DR Reactome; R-HSA-6784531; tRNA processing in the nucleus.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR SignaLink; O95639; -.
DR SIGNOR; O95639; -.
DR BioGRID-ORCS; 10898; 560 hits in 1097 CRISPR screens.
DR ChiTaRS; CPSF4; human.
DR EvolutionaryTrace; O95639; -.
DR GeneWiki; CPSF4; -.
DR GenomeRNAi; 10898; -.
DR Pharos; O95639; Tbio.
DR PRO; PR:O95639; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O95639; protein.
DR Bgee; ENSG00000160917; Expressed in secondary oocyte and 193 other tissues.
DR ExpressionAtlas; O95639; baseline and differential.
DR Genevisible; O95639; HS.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR InterPro; IPR045348; CPSF4/Yth1.
DR InterPro; IPR041686; Znf-CCCH_3.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR23102; PTHR23102; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF15663; zf-CCCH_3; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SMART; SM00356; ZnF_C3H1; 5.
DR SUPFAM; SSF57756; SSF57756; 1.
DR SUPFAM; SSF90229; SSF90229; 2.
DR PROSITE; PS50103; ZF_C3H1; 5.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Host-virus interaction; Metal-binding;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..269
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 4"
FT /id="PRO_0000074402"
FT ZN_FING 35..61
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 62..89
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 90..117
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 118..142
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 143..169
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 243..260
FT /note="CCHC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT REGION 173..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 191..216
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008602"
FT VAR_SEQ 191..215
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008601"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:6URG"
FT HELIX 14..18
FT /evidence="ECO:0007829|PDB:6URG"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:6URG"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:6URG"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:2RHK"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2RHK"
FT STRAND 82..85
FT /evidence="ECO:0007829|PDB:2RHK"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2D9N"
FT HELIX 97..102
FT /evidence="ECO:0007829|PDB:2RHK"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:2D9N"
FT HELIX 125..129
FT /evidence="ECO:0007829|PDB:7K95"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:7K95"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:7K95"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:7K95"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:7K95"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:7K95"
SQ SEQUENCE 269 AA; 30255 MW; 49444E3EB840464A CRC64;
MQEIIASVDH IKFDLEIAVE QQLGAQPLPF PGMDKSGAAV CEFFLKAACG KGGMCPFRHI
SGEKTVVCKH WLRGLCKKGD QCEFLHEYDM TKMPECYFYS KFGECSNKEC PFLHIDPESK
IKDCPWYDRG FCKHGPLCRH RHTRRVICVN YLVGFCPEGP SCKFMHPRFE LPMGTTEQPP
LPQQTQPPAK QSNNPPLQRS SSLIQLTSQN SSPNQQRTPQ VIGVMQSQNS SAGNRGPRPL
EQVTCYKCGE KGHYANRCTK GHLAFLSGQ
