CPSF2_HUMAN
ID CPSF2_HUMAN Reviewed; 782 AA.
AC Q9P2I0; B3KME1; Q6NSJ1; Q9H3W7;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Cleavage and polyadenylation specificity factor subunit 2;
DE AltName: Full=Cleavage and polyadenylation specificity factor 100 kDa subunit;
DE Short=CPSF 100 kDa subunit;
GN Name=CPSF2; Synonyms=CPSF100, KIAA1367;
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 [LARGE SCALE MRNA].
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-782.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-782.
RC TISSUE=Lymph node;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP FUNCTION IN PRE-MRNA 3'-END PROCESSING, AND IDENTIFICATION IN THE CPSF
RP COMPLEX.
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, INTERACTION WITH CPSF3; CSTF2 AND SYMPK, AND MUTAGENESIS OF
RP HIS-67; ASP-289 AND ARG-543.
RX PubMed=18688255; DOI=10.1038/embor.2008.146;
RA Kolev N.G., Yario T.A., Benson E., Steitz J.A.;
RT "Conserved motifs in both CPSF73 and CPSF100 are required to assemble the
RT active endonuclease for histone mRNA 3'-end maturation.";
RL EMBO Rep. 9:1013-1018(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420; SER-423 AND
RP SER-660, AND 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420 AND SER-423, 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 [12]
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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420 AND SER-423, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
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. Involved in the histone 3' end pre-mRNA processing.
CC {ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:18688255}.
CC -!- SUBUNIT: Component of the cleavage and polyadenylation specificity
CC factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and
CC FIP1L1. Interacts with CPSF3, CSTF2 and SYMPK. Interacts with ZC3H3 (By
CC similarity). {ECO:0000250|UniProtKB:O35218,
CC ECO:0000269|PubMed:14749727, ECO:0000269|PubMed:18688255,
CC ECO:0000269|PubMed:21102410}.
CC -!- INTERACTION:
CC Q9P2I0; P33240: CSTF2; NbExp=2; IntAct=EBI-1043224, EBI-711360;
CC Q9P2I0; Q92797: SYMPK; NbExp=4; IntAct=EBI-1043224, EBI-1051992;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. RNA-
CC metabolizing metallo-beta-lactamase-like family. CPSF2/YSH1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AK001627; BAG50953.1; -; mRNA.
DR EMBL; CH471061; EAW81480.1; -; Genomic_DNA.
DR EMBL; BC070095; AAH70095.1; -; mRNA.
DR EMBL; AB037788; BAA92605.1; -; mRNA.
DR EMBL; AL442079; CAC09445.1; -; mRNA.
DR CCDS; CCDS9902.1; -.
DR RefSeq; NP_001309201.1; NM_001322272.1.
DR RefSeq; NP_059133.1; NM_017437.2.
DR PDB; 6URG; EM; 3.00 A; F=1-782.
DR PDB; 6V4X; EM; 3.20 A; I=1-782.
DR PDBsum; 6URG; -.
DR PDBsum; 6V4X; -.
DR AlphaFoldDB; Q9P2I0; -.
DR SMR; Q9P2I0; -.
DR BioGRID; 119826; 122.
DR CORUM; Q9P2I0; -.
DR DIP; DIP-42500N; -.
DR IntAct; Q9P2I0; 33.
DR MINT; Q9P2I0; -.
DR STRING; 9606.ENSP00000298875; -.
DR GlyGen; Q9P2I0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P2I0; -.
DR PhosphoSitePlus; Q9P2I0; -.
DR SwissPalm; Q9P2I0; -.
DR BioMuta; CPSF2; -.
DR DMDM; 51338827; -.
DR EPD; Q9P2I0; -.
DR jPOST; Q9P2I0; -.
DR MassIVE; Q9P2I0; -.
DR MaxQB; Q9P2I0; -.
DR PaxDb; Q9P2I0; -.
DR PeptideAtlas; Q9P2I0; -.
DR PRIDE; Q9P2I0; -.
DR ProteomicsDB; 83819; -.
DR Antibodypedia; 81; 124 antibodies from 25 providers.
DR DNASU; 53981; -.
DR Ensembl; ENST00000298875.9; ENSP00000298875.4; ENSG00000165934.13.
DR GeneID; 53981; -.
DR KEGG; hsa:53981; -.
DR MANE-Select; ENST00000298875.9; ENSP00000298875.4; NM_017437.3; NP_059133.1.
DR UCSC; uc001yah.3; human.
DR CTD; 53981; -.
DR DisGeNET; 53981; -.
DR GeneCards; CPSF2; -.
DR HGNC; HGNC:2325; CPSF2.
DR HPA; ENSG00000165934; Low tissue specificity.
DR MIM; 606028; gene.
DR neXtProt; NX_Q9P2I0; -.
DR OpenTargets; ENSG00000165934; -.
DR PharmGKB; PA26842; -.
DR VEuPathDB; HostDB:ENSG00000165934; -.
DR eggNOG; KOG1135; Eukaryota.
DR GeneTree; ENSGT00910000144260; -.
DR HOGENOM; CLU_002227_1_1_1; -.
DR InParanoid; Q9P2I0; -.
DR OMA; MELVENC; -.
DR OrthoDB; 1314980at2759; -.
DR PhylomeDB; Q9P2I0; -.
DR TreeFam; TF106131; -.
DR PathwayCommons; Q9P2I0; -.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
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; Q9P2I0; -.
DR SIGNOR; Q9P2I0; -.
DR BioGRID-ORCS; 53981; 783 hits in 1085 CRISPR screens.
DR ChiTaRS; CPSF2; human.
DR GeneWiki; CPSF2; -.
DR GenomeRNAi; 53981; -.
DR Pharos; Q9P2I0; Tbio.
DR PRO; PR:Q9P2I0; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q9P2I0; protein.
DR Bgee; ENSG00000165934; Expressed in buccal mucosa cell and 194 other tissues.
DR ExpressionAtlas; Q9P2I0; baseline and differential.
DR Genevisible; Q9P2I0; HS.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006398; P:mRNA 3'-end processing by stem-loop binding and cleavage; IDA:UniProtKB.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0098789; P:pre-mRNA cleavage required for polyadenylation; IBA:GO_Central.
DR CDD; cd16293; CPSF2-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR027075; CPSF2.
DR InterPro; IPR025069; Cpsf2_C.
DR InterPro; IPR035639; CPSF2_MBL.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR PANTHER; PTHR45922; PTHR45922; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF13299; CPSF100_C; 1.
DR Pfam; PF16661; Lactamase_B_6; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..782
FT /note="Cleavage and polyadenylation specificity factor
FT subunit 2"
FT /id="PRO_0000074393"
FT REGION 407..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..446
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MUTAGEN 67
FT /note="H->A: Inhibits histone 3'-end processing."
FT /evidence="ECO:0000269|PubMed:18688255"
FT MUTAGEN 289
FT /note="D->A: Does not inhibit histone 3'-end processing."
FT /evidence="ECO:0000269|PubMed:18688255"
FT MUTAGEN 543
FT /note="R->A: Inhibits histone 3'-end processing."
FT /evidence="ECO:0000269|PubMed:18688255"
FT CONFLICT 289
FT /note="D -> G (in Ref. 3; AAH70095)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="K -> R (in Ref. 3; AAH70095)"
FT /evidence="ECO:0000305"
FT STRAND 5..11
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:6V4X"
FT TURN 43..51
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 88..106
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 212..228
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 233..236
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 243..255
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 273..280
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 289..296
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 306..313
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 314..317
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 325..329
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 331..335
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 337..344
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 361..363
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 377..385
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:6URG"
FT STRAND 520..528
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:6V4X"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 549..555
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 559..563
FT /evidence="ECO:0007829|PDB:6V4X"
FT HELIX 568..578
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 606..610
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 615..617
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 622..624
FT /evidence="ECO:0007829|PDB:6V4X"
FT STRAND 630..634
FT /evidence="ECO:0007829|PDB:6V4X"
SQ SEQUENCE 782 AA; 88487 MW; F67B4813B9883CE8 CRC64;
MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SMDIIDSLRK HVHQIDAVLL
SHPDPLHLGA LPYAVGKLGL NCAIYATIPV YKMGQMFMYD LYQSRHNTED FTLFTLDDVD
AAFDKIQQLK FSQIVNLKGK GHGLSITPLP AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR
EIHLNGCSLE MLSRPSLLIT DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA
GRVLELAQLL DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN
NPFQFRHLSL CHGLSDLARV PSPKVVLASQ PDLECGFSRD LFIQWCQDPK NSIILTYRTT
PGTLARFLID NPSEKITEIE LRKRVKLEGK ELEEYLEKEK LKKEAAKKLE QSKEADIDSS
DESDIEEDID QPSAHKTKHD LMMKGEGSRK GSFFKQAKKS YPMFPAPEER IKWDEYGEII
KPEDFLVPEL QATEEEKSKL ESGLTNGDEP MDQDLSDVPT KCISTTESIE IKARVTYIDY
EGRSDGDSIK KIINQMKPRQ LIIVHGPPEA SQDLAECCRA FGGKDIKVYM PKLHETVDAT
SETHIYQVRL KDSLVSSLQF CKAKDAELAW IDGVLDMRVS KVDTGVILEE GELKDDGEDS
EMQVEAPSDS SVIAQQKAMK SLFGDDEKET GEESEIIPTL EPLPPHEVPG HQSVFMNEPR
LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV RRTETGRIGL EGCLCQDFYR IRDLLYEQYA
IV
