CPSF1_HUMAN
ID CPSF1_HUMAN Reviewed; 1443 AA.
AC Q10570; Q96AF0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2002, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 1;
DE AltName: Full=Cleavage and polyadenylation specificity factor 160 kDa subunit;
DE Short=CPSF 160 kDa subunit;
GN Name=CPSF1; Synonyms=CPSF160;
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].
RX PubMed=7590244; DOI=10.1101/gad.9.21.2672;
RA Murthy K.G., Manley J.L.;
RT "The 160-kD subunit of human cleavage-polyadenylation specificity factor
RT coordinates pre-mRNA 3'-end formation.";
RL Genes Dev. 9:2672-2683(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas;
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 INTERACTION WITH SRRM1.
RX PubMed=11739730; DOI=10.1128/mcb.22.1.148-160.2002;
RA McCracken S., Lambermon M., Blencowe B.J.;
RT "SRm160 splicing coactivator promotes transcript 3'-end cleavage.";
RL Mol. Cell. Biol. 22:148-160(2002).
RN [4]
RP FUNCTION IN PRE-MRNA 3'-END PROCESSING, IDENTIFICATION IN THE CPSF COMPLEX,
RP IDENTIFICATION IN A COMPLEX WITH FIP1L1 AND PAPOLA, AND INTERACTION WITH
RP 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 [5]
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 [6]
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 [7]
RP IDENTIFICATION IN THE CPSF COMPLEX, AND INTERACTION WITH TUT1.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-766, AND IDENTIFICATION BY
RP 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 [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [11]
RP VARIANTS MYP27 5-TYR--PHE-1443 DEL; 620-GLN--PHE-1443 DEL AND TYR-1275,
RP INVOLVEMENT IN MYP27, AND TISSUE SPECIFICITY.
RX PubMed=30689892; DOI=10.1093/hmg/ddz029;
RA Ouyang J., Sun W., Xiao X., Li S., Jia X., Zhou L., Wang P., Zhang Q.;
RT "CPSF1 mutations are associated with early-onset high myopia and involved
RT in retinal ganglion cell axon projection.";
RL Hum. Mol. Genet. 28:1959-1970(2019).
CC -!- FUNCTION: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex that plays 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. This subunit is involved in the RNA recognition step
CC of the polyadenylation reaction (PubMed:14749727). May play a role in
CC eye morphogenesis and the development of retinal ganglion cell
CC projections to the midbrain (By similarity).
CC {ECO:0000250|UniProtKB:A0A0R4IC37, ECO:0000269|PubMed:14749727}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC FIP1L1. Found in a complex with CPSF1, FIP1L1 and PAPOLA. Interacts
CC with FIP1L1, TENT2/GLD2 and SRRM1. Interacts with TUT1; the interaction
CC is direct and mediates the recruitment of the CPSF complex on the 3'UTR
CC of selected pre-mRNAs. {ECO:0000269|PubMed:11739730,
CC ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:21102410}.
CC -!- INTERACTION:
CC Q10570; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-347859, EBI-742054;
CC Q10570; Q0VD86: INCA1; NbExp=3; IntAct=EBI-347859, EBI-6509505;
CC Q10570; P06748: NPM1; NbExp=2; IntAct=EBI-347859, EBI-78579;
CC Q10570; Q04864: REL; NbExp=3; IntAct=EBI-347859, EBI-307352;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm.
CC -!- TISSUE SPECIFICITY: Widely expressed, with high expression in the
CC retina. {ECO:0000269|PubMed:30689892}.
CC -!- PTM: The N-terminus is blocked.
CC -!- DISEASE: Myopia 27, autosomal dominant (MYP27) [MIM:618827]: A form of
CC myopia, a refractive error of the eye, in which parallel rays from a
CC distant object come to focus in front of the retina, vision being
CC better for near objects than for far. MYP27 patients are affected by
CC early-onset high myopia with increased axial lengths. Fundus changes
CC include optic nerve head crescent and tigroid appearance of the
CC posterior retina. {ECO:0000269|PubMed:30689892}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the CPSF1 family. {ECO:0000305}.
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DR EMBL; U37012; AAC50293.1; -; mRNA.
DR EMBL; BC017232; AAH17232.1; -; mRNA.
DR CCDS; CCDS34966.1; -.
DR RefSeq; NP_037423.2; NM_013291.2.
DR PDB; 6BLY; EM; 3.36 A; A=1-1443.
DR PDB; 6BM0; EM; 3.80 A; A=1-1443.
DR PDB; 6DNH; EM; 3.40 A; A=1-1443.
DR PDB; 6F9N; X-ray; 2.50 A; A=1-1443.
DR PDB; 6FBS; EM; 3.07 A; A=1-1443.
DR PDB; 6FUW; EM; 3.07 A; A=1-1443.
DR PDB; 6URG; EM; 3.00 A; A=1-1443.
DR PDB; 6URO; EM; 3.60 A; A=1-1443.
DR PDBsum; 6BLY; -.
DR PDBsum; 6BM0; -.
DR PDBsum; 6DNH; -.
DR PDBsum; 6F9N; -.
DR PDBsum; 6FBS; -.
DR PDBsum; 6FUW; -.
DR PDBsum; 6URG; -.
DR PDBsum; 6URO; -.
DR AlphaFoldDB; Q10570; -.
DR SMR; Q10570; -.
DR BioGRID; 118946; 206.
DR CORUM; Q10570; -.
DR DIP; DIP-32694N; -.
DR IntAct; Q10570; 51.
DR MINT; Q10570; -.
DR STRING; 9606.ENSP00000484669; -.
DR iPTMnet; Q10570; -.
DR PhosphoSitePlus; Q10570; -.
DR SwissPalm; Q10570; -.
DR BioMuta; CPSF1; -.
DR DMDM; 23503048; -.
DR EPD; Q10570; -.
DR jPOST; Q10570; -.
DR MassIVE; Q10570; -.
DR MaxQB; Q10570; -.
DR PaxDb; Q10570; -.
DR PeptideAtlas; Q10570; -.
DR PRIDE; Q10570; -.
DR ProteomicsDB; 58860; -.
DR Antibodypedia; 14844; 82 antibodies from 21 providers.
DR DNASU; 29894; -.
DR Ensembl; ENST00000616140.2; ENSP00000484669.1; ENSG00000071894.17.
DR Ensembl; ENST00000620219.4; ENSP00000478145.1; ENSG00000071894.17.
DR Ensembl; ENST00000643746.1; ENSP00000495102.1; ENSG00000285049.2.
DR Ensembl; ENST00000644539.2; ENSP00000495020.1; ENSG00000285049.2.
DR GeneID; 29894; -.
DR KEGG; hsa:29894; -.
DR MANE-Select; ENST00000616140.2; ENSP00000484669.1; NM_013291.3; NP_037423.2.
DR UCSC; uc003zcj.3; human.
DR CTD; 29894; -.
DR DisGeNET; 29894; -.
DR GeneCards; CPSF1; -.
DR HGNC; HGNC:2324; CPSF1.
DR HPA; ENSG00000071894; Low tissue specificity.
DR MalaCards; CPSF1; -.
DR MIM; 606027; gene.
DR MIM; 618827; phenotype.
DR neXtProt; NX_Q10570; -.
DR PharmGKB; PA26841; -.
DR VEuPathDB; HostDB:ENSG00000071894; -.
DR eggNOG; KOG1896; Eukaryota.
DR GeneTree; ENSGT00950000183151; -.
DR HOGENOM; CLU_002414_0_0_1; -.
DR InParanoid; Q10570; -.
DR OMA; PMTKFKL; -.
DR OrthoDB; 360328at2759; -.
DR PhylomeDB; Q10570; -.
DR TreeFam; TF314322; -.
DR PathwayCommons; Q10570; -.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
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; Q10570; -.
DR SIGNOR; Q10570; -.
DR BioGRID-ORCS; 29894; 642 hits in 1081 CRISPR screens.
DR ChiTaRS; CPSF1; human.
DR GeneWiki; CPSF1; -.
DR GenomeRNAi; 29894; -.
DR Pharos; Q10570; Tbio.
DR PRO; PR:Q10570; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q10570; protein.
DR Bgee; ENSG00000071894; Expressed in right testis and 93 other tissues.
DR ExpressionAtlas; Q10570; baseline and differential.
DR Genevisible; Q10570; HS.
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:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0035925; F:mRNA 3'-UTR AU-rich region binding; IDA:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IMP:UniProtKB.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IC:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF03178; CPSF_A; 1.
DR Pfam; PF10433; MMS1_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; mRNA processing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..1443
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 1"
FT /id="PRO_0000074387"
FT REGION 404..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..777
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 901..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 893..908
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 408..423
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 756
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9EPU4"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 5..1443
FT /note="Missing (in MYP27)"
FT /evidence="ECO:0000269|PubMed:30689892"
FT /id="VAR_083935"
FT VARIANT 620..1443
FT /note="Missing (in MYP27)"
FT /evidence="ECO:0000269|PubMed:30689892"
FT /id="VAR_083936"
FT VARIANT 1275
FT /note="D -> Y (in MYP27; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30689892"
FT /id="VAR_083937"
FT CONFLICT 12
FT /note="T -> P (in Ref. 1; AAC50293)"
FT /evidence="ECO:0000305"
FT CONFLICT 1318
FT /note="Missing (in Ref. 1; AAC50293)"
FT /evidence="ECO:0000305"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 65..73
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 90..98
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 110..113
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 114..122
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 129..131
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 196..198
FT /evidence="ECO:0007829|PDB:6URG"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:6URG"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 265..270
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 273..275
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 278..282
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 326..338
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 342..350
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 372..376
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 381..385
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 391..398
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 461..469
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 477..481
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 499..505
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 507..509
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 511..515
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 522..528
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 534..539
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 572..579
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 582..594
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 596..600
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 607..612
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 613..616
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 617..622
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 625..630
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 633..639
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 642..644
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 655..662
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 665..672
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 680..684
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 695..703
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 782..789
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 794..798
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 799..802
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 803..809
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 846..855
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 860..867
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 870..878
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 885..887
FT /evidence="ECO:0007829|PDB:6URG"
FT STRAND 890..894
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 930..935
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 937..939
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 942..945
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 947..949
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 951..954
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 962..965
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 972..978
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 981..983
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 986..991
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 994..1000
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1008..1011
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1013..1017
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1019..1028
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 1029..1032
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1033..1043
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1046..1048
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1052..1054
FT /evidence="ECO:0007829|PDB:6URG"
FT STRAND 1057..1059
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1070..1080
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 1081..1084
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1098..1109
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1116..1127
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1131..1133
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1136..1146
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 1155..1157
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1158..1170
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1172..1178
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1181..1186
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1189..1196
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1199..1207
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1212..1216
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1221..1229
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1231..1237
FT /evidence="ECO:0007829|PDB:6F9N"
FT TURN 1238..1241
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1242..1248
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1255..1262
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1268..1273
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1278..1282
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 1285..1287
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1288..1293
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1297..1302
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1308..1315
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1334..1340
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1345..1351
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 1353..1369
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 1373..1375
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 1378..1381
FT /evidence="ECO:0007829|PDB:6F9N"
FT STRAND 1383..1385
FT /evidence="ECO:0007829|PDB:6BLY"
FT STRAND 1398..1400
FT /evidence="ECO:0007829|PDB:6URG"
FT TURN 1402..1404
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 1405..1409
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 1412..1422
FT /evidence="ECO:0007829|PDB:6F9N"
FT HELIX 1426..1439
FT /evidence="ECO:0007829|PDB:6F9N"
SQ SEQUENCE 1443 AA; 160884 MW; 7E1DF4D8A93487A4 CRC64;
MYAVYKQAHP PTGLEFSMYC NFFNNSERNL VVAGTSQLYV YRLNRDAEAL TKNDRSTEGK
AHREKLELAA SFSFFGNVMS MASVQLAGAK RDALLLSFKD AKLSVVEYDP GTHDLKTLSL
HYFEEPELRD GFVQNVHTPR VRVDPDGRCA AMLVYGTRLV VLPFRRESLA EEHEGLVGEG
QRSSFLPSYI IDVRALDEKL LNIIDLQFLH GYYEPTLLIL FEPNQTWPGR VAVRQDTCSI
VAISLNITQK VHPVIWSLTS LPFDCTQALA VPKPIGGVVV FAVNSLLYLN QSVPPYGVAL
NSLTTGTTAF PLRTQEGVRI TLDCAQATFI SYDKMVISLK GGEIYVLTLI TDGMRSVRAF
HFDKAAASVL TTSMVTMEPG YLFLGSRLGN SLLLKYTEKL QEPPASAVRE AADKEEPPSK
KKRVDATAGW SAAGKSVPQD EVDEIEVYGS EAQSGTQLAT YSFEVCDSIL NIGPCANAAV
GEPAFLSEEF QNSPEPDLEI VVCSGHGKNG ALSVLQKSIR PQVVTTFELP GCYDMWTVIA
PVRKEEEDNP KGEGTEQEPS TTPEADDDGR RHGFLILSRE DSTMILQTGQ EIMELDTSGF
ATQGPTVFAG NIGDNRYIVQ VSPLGIRLLE GVNQLHFIPV DLGAPIVQCA VADPYVVIMS
AEGHVTMFLL KSDSYGGRHH RLALHKPPLH HQSKVITLCL YRDLSGMFTT ESRLGGARDE
LGGRSGPEAE GLGSETSPTV DDEEEMLYGD SGSLFSPSKE EARRSSQPPA DRDPAPFRAE
PTHWCLLVRE NGTMEIYQLP DWRLVFLVKN FPVGQRVLVD SSFGQPTTQG EARREEATRQ
GELPLVKEVL LVALGSRQSR PYLLVHVDQE LLIYEAFPHD SQLGQGNLKV RFKKVPHNIN
FREKKPKPSK KKAEGGGAEE GAGARGRVAR FRYFEDIYGY SGVFICGPSP HWLLVTGRGA
LRLHPMAIDG PVDSFAPFHN VNCPRGFLYF NRQGELRISV LPAYLSYDAP WPVRKIPLRC
TAHYVAYHVE SKVYAVATST NTPCARIPRM TGEEKEFETI ERDERYIHPQ QEAFSIQLIS
PVSWEAIPNA RIELQEWEHV TCMKTVSLRS EETVSGLKGY VAAGTCLMQG EEVTCRGRIL
IMDVIEVVPE PGQPLTKNKF KVLYEKEQKG PVTALCHCNG HLVSAIGQKI FLWSLRASEL
TGMAFIDTQL YIHQMISVKN FILAADVMKS ISLLRYQEES KTLSLVSRDA KPLEVYSVDF
MVDNAQLGFL VSDRDRNLMV YMYLPEAKES FGGMRLLRRA DFHVGAHVNT FWRTPCRGAT
EGLSKKSVVW ENKHITWFAT LDGGIGLLLP MQEKTYRRLL MLQNALTTML PHHAGLNPRA
FRMLHVDRRT LQNAVRNVLD GELLNRYLYL STMERSELAK KIGTTPDIIL DDLLETDRVT
AHF
