PSF3_HUMAN
ID PSF3_HUMAN Reviewed; 216 AA.
AC Q9BRX5; B2RDP3; E9PB21; Q9H870;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DNA replication complex GINS protein PSF3;
DE AltName: Full=GINS complex subunit 3;
GN Name=GINS3; Synonyms=PSF3;
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] (ISOFORMS 1 AND 2).
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 MRNA] (ISOFORM 2).
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 (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Muscle, and Skin;
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 [6]
RP SUBUNIT, AND INTERACTION WITH DNA PRIMASE.
RX PubMed=17170760; DOI=10.1038/sj.embor.7400870;
RA De Falco M., Ferrari E., De Felice M., Rossi M., Hubscher U., Pisani F.M.;
RT "The human GINS complex binds to and specifically stimulates human DNA
RT polymerase alpha-primase.";
RL EMBO Rep. 8:99-103(2007).
RN [7]
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 [8]
RP INTERACTION WITH GINS1.
RX PubMed=28414293; DOI=10.1172/jci90727;
RA Cottineau J., Kottemann M.C., Lach F.P., Kang Y.H., Vely F., Deenick E.K.,
RA Lazarov T., Gineau L., Wang Y., Farina A., Chansel M., Lorenzo L.,
RA Piperoglou C., Ma C.S., Nitschke P., Belkadi A., Itan Y., Boisson B.,
RA Jabot-Hanin F., Picard C., Bustamante J., Eidenschenk C., Boucherit S.,
RA Aladjidi N., Lacombe D., Barat P., Qasim W., Hurst J.A., Pollard A.J.,
RA Uhlig H.H., Fieschi C., Michon J., Bermudez V.P., Abel L.,
RA de Villartay J.P., Geissmann F., Tangye S.G., Hurwitz J., Vivier E.,
RA Casanova J.L., Smogorzewska A., Jouanguy E.;
RT "Inherited GINS1 deficiency underlies growth retardation along with
RT neutropenia and NK cell deficiency.";
RL J. Clin. Invest. 127:1991-2006(2017).
RN [9]
RP STRUCTURE BY ELECTRON MICROSCOPY (33 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS2 AND GINS4, SUBUNIT, AND MASS SPECTROMETRY OF GINS COMPLEX.
RX PubMed=17557111; DOI=10.1038/sj.embor.7401002;
RA Boskovic J., Coloma J., Aparicio T., Zhou M., Robinson C.V., Mendez J.,
RA Montoya G.;
RT "Molecular architecture of the human GINS complex.";
RL EMBO Rep. 8:678-684(2007).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GINS1; GINS2 AND
RP GINS4, AND SUBUNIT.
RX PubMed=17545466; DOI=10.1101/gad.1548107;
RA Choi J.M., Lim H.S., Kim J.J., Song O.K., Cho Y.;
RT "Crystal structure of the human GINS complex.";
RL Genes Dev. 21:1316-1321(2007).
RN [11]
RP FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS2 AND GINS4, AND SUBUNIT.
RX PubMed=17417653; DOI=10.1038/nsmb1231;
RA Kamada K., Kubota Y., Arata T., Shindo Y., Hanaoka F.;
RT "Structure of the human GINS complex and its assembly and functional
RT interface in replication initiation.";
RL Nat. Struct. Mol. Biol. 14:388-396(2007).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) OF 2-216 IN COMPLEX WITH GINS1;
RP GINS2 AND GINS4, SUBUNIT, AND REGION.
RX PubMed=17652513; DOI=10.1073/pnas.0705558104;
RA Chang Y.P., Wang G., Bermudez V., Hurwitz J., Chen X.S.;
RT "Crystal structure of the GINS complex and functional insights into its
RT role in DNA replication.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12685-12690(2007).
CC -!- FUNCTION: The GINS complex plays an essential role in the initiation of
CC DNA replication, and progression of DNA replication forks. GINS complex
CC seems to bind preferentially to single-stranded DNA.
CC {ECO:0000269|PubMed:17417653}.
CC -!- SUBUNIT: Component of the GINS complex which is a heterotetramer of
CC GINS1, GINS2, GINS3 and GINS4 (PubMed:17170760, PubMed:17417653,
CC PubMed:17545466, PubMed:17557111, PubMed:17652513, PubMed:28414293).
CC Forms a stable subcomplex with GINS2 (PubMed:17170760, PubMed:17417653,
CC PubMed:17545466, PubMed:17557111, PubMed:17652513, PubMed:28414293).
CC GINS complex interacts with DNA primase in vitro (PubMed:17170760,
CC PubMed:17417653, PubMed:17545466, PubMed:17557111, PubMed:17652513,
CC PubMed:28414293). Component of the CMG helicase complex, composed of
CC the MCM2-7 complex, the GINS complex and CDC45 (By similarity).
CC {ECO:0000250|UniProtKB:Q7ZT01, ECO:0000269|PubMed:17170760,
CC ECO:0000269|PubMed:17417653, ECO:0000269|PubMed:17545466,
CC ECO:0000269|PubMed:17557111, ECO:0000269|PubMed:17652513,
CC ECO:0000269|PubMed:28414293}.
CC -!- INTERACTION:
CC Q9BRX5; P46379-2: BAG6; NbExp=3; IntAct=EBI-2857315, EBI-10988864;
CC Q9BRX5; Q9UI47-2: CTNNA3; NbExp=3; IntAct=EBI-2857315, EBI-11962928;
CC Q9BRX5; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-2857315, EBI-12593112;
CC Q9BRX5; O14645: DNALI1; NbExp=3; IntAct=EBI-2857315, EBI-395638;
CC Q9BRX5; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-2857315, EBI-14103818;
CC Q9BRX5; Q9UMF0: ICAM5; NbExp=3; IntAct=EBI-2857315, EBI-6398041;
CC Q9BRX5; O14901: KLF11; NbExp=3; IntAct=EBI-2857315, EBI-948266;
CC Q9BRX5; Q6KB66-2: KRT80; NbExp=3; IntAct=EBI-2857315, EBI-11999246;
CC Q9BRX5; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-2857315, EBI-2811583;
CC Q9BRX5; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-2857315, EBI-358489;
CC Q9BRX5; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-2857315, EBI-8451480;
CC Q9BRX5; P14927: UQCRB; NbExp=3; IntAct=EBI-2857315, EBI-743128;
CC Q9BRX5; Q08AM6: VAC14; NbExp=6; IntAct=EBI-2857315, EBI-2107455;
CC Q9BRX5-3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-16436971, EBI-16439278;
CC Q9BRX5-3; Q08AM6: VAC14; NbExp=3; IntAct=EBI-16436971, EBI-2107455;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7ZT01}.
CC Chromosome {ECO:0000250|UniProtKB:Q7ZT01}. Note=Associates with
CC chromatin. {ECO:0000250|UniProtKB:Q7ZT01}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BRX5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRX5-2; Sequence=VSP_032737;
CC Name=3;
CC IsoId=Q9BRX5-3; Sequence=VSP_046694;
CC -!- MASS SPECTROMETRY: Mass=98373; Mass_error=13; Method=Electrospray;
CC Note=This is the measured mass for the GINS complex.;
CC Evidence={ECO:0000269|PubMed:17557111};
CC -!- SIMILARITY: Belongs to the GINS3/PSF3 family. {ECO:0000305}.
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DR EMBL; AK023974; BAB14747.1; -; mRNA.
DR EMBL; AK315622; BAG37990.1; -; mRNA.
DR EMBL; CR457283; CAG33564.1; -; mRNA.
DR EMBL; AC009107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009118; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC084063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW82973.1; -; Genomic_DNA.
DR EMBL; CH471092; EAW82976.1; -; Genomic_DNA.
DR EMBL; BC005879; AAH05879.1; -; mRNA.
DR EMBL; BC014437; AAH14437.1; -; mRNA.
DR CCDS; CCDS10796.1; -. [Q9BRX5-1]
DR CCDS; CCDS45498.1; -. [Q9BRX5-3]
DR CCDS; CCDS45499.1; -. [Q9BRX5-2]
DR RefSeq; NP_001119601.1; NM_001126129.1. [Q9BRX5-3]
DR RefSeq; NP_001119602.1; NM_001126130.1. [Q9BRX5-2]
DR RefSeq; NP_073607.2; NM_022770.3. [Q9BRX5-1]
DR PDB; 2E9X; X-ray; 2.30 A; C/G=1-216.
DR PDB; 2EHO; X-ray; 3.00 A; D/H/L=1-216.
DR PDB; 2Q9Q; X-ray; 2.36 A; D/H=2-216.
DR PDB; 6XTX; EM; 3.29 A; C=1-216.
DR PDB; 6XTY; EM; 6.77 A; C=1-216.
DR PDB; 7PFO; EM; 3.20 A; F=1-216.
DR PDB; 7PLO; EM; 2.80 A; F=1-216.
DR PDBsum; 2E9X; -.
DR PDBsum; 2EHO; -.
DR PDBsum; 2Q9Q; -.
DR PDBsum; 6XTX; -.
DR PDBsum; 6XTY; -.
DR PDBsum; 7PFO; -.
DR PDBsum; 7PLO; -.
DR AlphaFoldDB; Q9BRX5; -.
DR SMR; Q9BRX5; -.
DR BioGRID; 122295; 64.
DR ComplexPortal; CPX-787; GINS complex.
DR CORUM; Q9BRX5; -.
DR DIP; DIP-29333N; -.
DR IntAct; Q9BRX5; 31.
DR MINT; Q9BRX5; -.
DR GlyGen; Q9BRX5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BRX5; -.
DR PhosphoSitePlus; Q9BRX5; -.
DR BioMuta; GINS3; -.
DR DMDM; 74732939; -.
DR EPD; Q9BRX5; -.
DR jPOST; Q9BRX5; -.
DR MassIVE; Q9BRX5; -.
DR MaxQB; Q9BRX5; -.
DR PeptideAtlas; Q9BRX5; -.
DR PRIDE; Q9BRX5; -.
DR ProteomicsDB; 19126; -.
DR ProteomicsDB; 78847; -. [Q9BRX5-1]
DR ProteomicsDB; 78848; -. [Q9BRX5-2]
DR Antibodypedia; 29079; 95 antibodies from 20 providers.
DR DNASU; 64785; -.
DR Ensembl; ENST00000318129.6; ENSP00000318196.6; ENSG00000181938.14. [Q9BRX5-1]
DR Ensembl; ENST00000328514.11; ENSP00000327449.7; ENSG00000181938.14. [Q9BRX5-2]
DR Ensembl; ENST00000426538.6; ENSP00000401018.2; ENSG00000181938.14. [Q9BRX5-3]
DR GeneID; 64785; -.
DR KEGG; hsa:64785; -.
DR MANE-Select; ENST00000318129.6; ENSP00000318196.6; NM_022770.4; NP_073607.2.
DR UCSC; uc002enh.4; human. [Q9BRX5-1]
DR CTD; 64785; -.
DR DisGeNET; 64785; -.
DR GeneCards; GINS3; -.
DR HGNC; HGNC:25851; GINS3.
DR HPA; ENSG00000181938; Low tissue specificity.
DR MIM; 610610; gene.
DR neXtProt; NX_Q9BRX5; -.
DR OpenTargets; ENSG00000181938; -.
DR PharmGKB; PA145008327; -.
DR VEuPathDB; HostDB:ENSG00000181938; -.
DR GeneTree; ENSGT00390000001622; -.
DR HOGENOM; CLU_1906093_0_0_1; -.
DR InParanoid; Q9BRX5; -.
DR OMA; IYKEGWR; -.
DR PhylomeDB; Q9BRX5; -.
DR TreeFam; TF314626; -.
DR PathwayCommons; Q9BRX5; -.
DR Reactome; R-HSA-176974; Unwinding of DNA.
DR SignaLink; Q9BRX5; -.
DR BioGRID-ORCS; 64785; 702 hits in 1088 CRISPR screens.
DR ChiTaRS; GINS3; human.
DR EvolutionaryTrace; Q9BRX5; -.
DR GenomeRNAi; 64785; -.
DR Pharos; Q9BRX5; Tbio.
DR PRO; PR:Q9BRX5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BRX5; protein.
DR Bgee; ENSG00000181938; Expressed in oocyte and 172 other tissues.
DR ExpressionAtlas; Q9BRX5; baseline and differential.
DR Genevisible; Q9BRX5; HS.
DR GO; GO:0071162; C:CMG complex; IPI:ComplexPortal.
DR GO; GO:0000811; C:GINS complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:ComplexPortal.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR GO; GO:1903934; P:positive regulation of DNA primase activity; IDA:ComplexPortal.
DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IDA:ComplexPortal.
DR Gene3D; 1.20.58.2050; -; 1.
DR InterPro; IPR021151; GINS_A.
DR InterPro; IPR036224; GINS_bundle-like_dom_sf.
DR InterPro; IPR010492; GINS_Psf3.
DR InterPro; IPR038437; GINS_Psf3_sf.
DR PANTHER; PTHR22768; PTHR22768; 1.
DR Pfam; PF05916; Sld5; 1.
DR SUPFAM; SSF158573; SSF158573; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromosome; DNA replication; Nucleus;
KW Reference proteome.
FT CHAIN 1..216
FT /note="DNA replication complex GINS protein PSF3"
FT /id="PRO_0000327615"
FT REGION 1..16
FT /note="Not essential for folding and stability of GINS
FT complex, but may regulate accessibility to the central
FT complex pore"
FT VAR_SEQ 62..139
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_032737"
FT VAR_SEQ 63
FT /note="G -> GFALLPRLECSGVIWLTAALTSQAPEILPPQPPMWLVLQG (in
FT isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046694"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 22..27
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 30..38
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2EHO"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:2Q9Q"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2E9X"
FT TURN 109..111
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 131..153
FT /evidence="ECO:0007829|PDB:2E9X"
FT TURN 154..157
FT /evidence="ECO:0007829|PDB:2Q9Q"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 170..190
FT /evidence="ECO:0007829|PDB:2E9X"
SQ SEQUENCE 216 AA; 24535 MW; A1B264A72371C551 CRC64;
MSEAYFRVES GALGPEENFL SLDDILMSHE KLPVRTETAM PRLGAFFLER SAGAETDNAV
PQGSKLELPL WLAKGLFDNK RRILSVELPK IYQEGWRTVF SADPNVVDLH KMGPHFYGFG
SQLLHFDSPE NADISQSLLQ TFIGRFRRIM DSSQNAYNED TSALVARLDE MERGLFQTGQ
KGLNDFQCWE KGQASQITAS NLVQNYKKRK FTDMED
