PSF2_HUMAN
ID PSF2_HUMAN Reviewed; 185 AA.
AC Q9Y248; D3DUM5; Q6IAG9;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=DNA replication complex GINS protein PSF2;
DE AltName: Full=GINS complex subunit 2;
GN Name=GINS2; Synonyms=PSF2; ORFNames=CGI-122, DC5, HSPC037;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Dendritic cell;
RA Li Y., Peng Y., Li N., Gu W., Han Z., Fu G., Chen Z.;
RT "Novel genes expressed in human dendritic cells.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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-182, AND IDENTIFICATION BY
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-180 AND SER-182, AND
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 [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-182, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-109, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17]
RP STRUCTURE BY ELECTRON MICROSCOPY (33 ANGSTROMS) IN COMPLEX WITH PSF1; PSF3
RP 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 [18]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH GINS1; GINS3 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 [19]
RP FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS3 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 [20]
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) IN COMPLEX WITH GINS1; GINS3 AND
RP 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:17417653, PubMed:17545466,
CC PubMed:17557111, PubMed:17652513). Forms a stable subcomplex with
CC GINS3. GINS complex interacts with DNA primase in vitro
CC (PubMed:17417653, PubMed:17545466, PubMed:17557111, PubMed:17652513).
CC Component of the CMG helicase complex, composed of the MCM2-7 complex,
CC the GINS complex and CDC45 (By similarity).
CC {ECO:0000250|UniProtKB:Q7ZT46, ECO:0000269|PubMed:17417653,
CC ECO:0000269|PubMed:17545466, ECO:0000269|PubMed:17557111,
CC ECO:0000269|PubMed:17652513}.
CC -!- INTERACTION:
CC Q9Y248; O96017: CHEK2; NbExp=2; IntAct=EBI-747491, EBI-1180783;
CC Q9Y248; Q9BRT9: GINS4; NbExp=10; IntAct=EBI-747491, EBI-747500;
CC Q9Y248; Q9BTE3: MCMBP; NbExp=2; IntAct=EBI-747491, EBI-749378;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7ZT46}.
CC Chromosome {ECO:0000250|UniProtKB:Q7ZT46}. Note=Associates with
CC chromatin. {ECO:0000250|UniProtKB:Q7ZT46}.
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 GINS2/PSF2 family. {ECO:0000305}.
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DR EMBL; AF125098; AAD39915.1; -; mRNA.
DR EMBL; AF151880; AAD34117.1; -; mRNA.
DR EMBL; AF201939; AAF86875.1; -; mRNA.
DR EMBL; AK001275; BAA91595.1; -; mRNA.
DR EMBL; CR457186; CAG33467.1; -; mRNA.
DR EMBL; CH471114; EAW95443.1; -; Genomic_DNA.
DR EMBL; CH471114; EAW95444.1; -; Genomic_DNA.
DR EMBL; BC003186; AAH03186.1; -; mRNA.
DR EMBL; BC010164; AAH10164.1; -; mRNA.
DR EMBL; BC062444; AAH62444.1; -; mRNA.
DR CCDS; CCDS10953.1; -.
DR RefSeq; NP_057179.1; NM_016095.2.
DR PDB; 2E9X; X-ray; 2.30 A; B/F=1-185.
DR PDB; 2EHO; X-ray; 3.00 A; C/G/K=1-185.
DR PDB; 2Q9Q; X-ray; 2.36 A; A/E=1-185.
DR PDB; 6XTX; EM; 3.29 A; B=1-185.
DR PDB; 6XTY; EM; 6.77 A; B=1-185.
DR PDB; 7PFO; EM; 3.20 A; E=1-185.
DR PDB; 7PLO; EM; 2.80 A; E=1-185.
DR PDBsum; 2E9X; -.
DR PDBsum; 2EHO; -.
DR PDBsum; 2Q9Q; -.
DR PDBsum; 6XTX; -.
DR PDBsum; 6XTY; -.
DR PDBsum; 7PFO; -.
DR PDBsum; 7PLO; -.
DR AlphaFoldDB; Q9Y248; -.
DR SMR; Q9Y248; -.
DR BioGRID; 119664; 43.
DR ComplexPortal; CPX-787; GINS complex.
DR CORUM; Q9Y248; -.
DR DIP; DIP-29332N; -.
DR IntAct; Q9Y248; 13.
DR MINT; Q9Y248; -.
DR STRING; 9606.ENSP00000253462; -.
DR GlyGen; Q9Y248; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y248; -.
DR PhosphoSitePlus; Q9Y248; -.
DR SwissPalm; Q9Y248; -.
DR BioMuta; GINS2; -.
DR DMDM; 37999822; -.
DR EPD; Q9Y248; -.
DR jPOST; Q9Y248; -.
DR MassIVE; Q9Y248; -.
DR MaxQB; Q9Y248; -.
DR PaxDb; Q9Y248; -.
DR PeptideAtlas; Q9Y248; -.
DR PRIDE; Q9Y248; -.
DR ProteomicsDB; 85645; -.
DR Antibodypedia; 30642; 225 antibodies from 26 providers.
DR DNASU; 51659; -.
DR Ensembl; ENST00000253462.8; ENSP00000253462.3; ENSG00000131153.9.
DR GeneID; 51659; -.
DR KEGG; hsa:51659; -.
DR MANE-Select; ENST00000253462.8; ENSP00000253462.3; NM_016095.3; NP_057179.1.
DR UCSC; uc002fja.4; human.
DR CTD; 51659; -.
DR DisGeNET; 51659; -.
DR GeneCards; GINS2; -.
DR HGNC; HGNC:24575; GINS2.
DR HPA; ENSG00000131153; Tissue enhanced (bone).
DR MIM; 610609; gene.
DR neXtProt; NX_Q9Y248; -.
DR OpenTargets; ENSG00000131153; -.
DR PharmGKB; PA145008313; -.
DR VEuPathDB; HostDB:ENSG00000131153; -.
DR eggNOG; KOG4071; Eukaryota.
DR GeneTree; ENSGT00390000007838; -.
DR HOGENOM; CLU_078274_2_0_1; -.
DR InParanoid; Q9Y248; -.
DR OMA; PYHWLEL; -.
DR OrthoDB; 1382842at2759; -.
DR PhylomeDB; Q9Y248; -.
DR TreeFam; TF314359; -.
DR PathwayCommons; Q9Y248; -.
DR Reactome; R-HSA-176974; Unwinding of DNA.
DR SignaLink; Q9Y248; -.
DR BioGRID-ORCS; 51659; 806 hits in 1082 CRISPR screens.
DR ChiTaRS; GINS2; human.
DR EvolutionaryTrace; Q9Y248; -.
DR GeneWiki; GINS2; -.
DR GenomeRNAi; 51659; -.
DR Pharos; Q9Y248; Tbio.
DR PRO; PR:Q9Y248; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9Y248; protein.
DR Bgee; ENSG00000131153; Expressed in oocyte and 143 other tissues.
DR ExpressionAtlas; Q9Y248; baseline and differential.
DR Genevisible; Q9Y248; 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; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:ComplexPortal.
DR GO; GO:0000727; P:double-strand break repair via break-induced replication; 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 InterPro; IPR021151; GINS_A.
DR InterPro; IPR036224; GINS_bundle-like_dom_sf.
DR InterPro; IPR007257; GINS_Psf2.
DR PANTHER; PTHR12772; PTHR12772; 1.
DR Pfam; PF05916; Sld5; 1.
DR PIRSF; PIRSF028998; GINS_Psf2_subgr; 1.
DR SUPFAM; SSF158573; SSF158573; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; DNA replication; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..185
FT /note="DNA replication complex GINS protein PSF2"
FT /id="PRO_0000194813"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT CROSSLNK 109
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 13..21
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2EHO"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2EHO"
FT HELIX 110..137
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 150..170
FT /evidence="ECO:0007829|PDB:2E9X"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:2Q9Q"
SQ SEQUENCE 185 AA; 21428 MW; 4F6A18B1ED76F93C CRC64;
MDAAEVEFLA EKELVTIIPN FSLDKIYLIG GDLGPFNPGL PVEVPLWLAI NLKQRQKCRL
LPPEWMDVEK LEKMRDHERK EETFTPMPSP YYMELTKLLL NHASDNIPKA DEIRTLVKDM
WDTRIAKLRV SADSFVRQQE AHAKLDNLTL MEINTSGTFL TQALNHMYKL RTNLQPLEST
QSQDF
