SLD5_HUMAN
ID SLD5_HUMAN Reviewed; 223 AA.
AC Q9BRT9; B2R8H5; D3DSY0; Q8N648;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=DNA replication complex GINS protein SLD5;
DE AltName: Full=GINS complex subunit 4;
DE Contains:
DE RecName: Full=DNA replication complex GINS protein SLD5, N-terminally processed;
GN Name=GINS4; Synonyms=SLD5;
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] (ISOFORM 1).
RC TISSUE=Thymus, and Tongue;
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Placenta;
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 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 [5]
RP INDUCTION.
RX PubMed=17611626; DOI=10.1371/journal.pone.0000594;
RA Ryu B., Kim D.S., Deluca A.M., Alani R.M.;
RT "Comprehensive expression profiling of tumor cell lines identifies
RT molecular signatures of melanoma progression.";
RL PLoS ONE 2:E594-E594(2007).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-12 AND SER-16, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-12 AND SER-16, CLEAVAGE OF INITIATOR METHIONINE [LARGE
RP SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
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 [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (33 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS2 AND GINS3, 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 [11]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 11-213 IN COMPLEX WITH GINS1;
RP GINS2 AND GINS3, 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 [12]
RP FUNCTION, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH GINS1;
RP GINS2 AND GINS3, SUBUNIT, AND REGION.
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 [13]
RP X-RAY CRYSTALLOGRAPHY (2.36 ANGSTROMS) IN COMPLEX WITH GINS1; GINS2 AND
RP GINS3, AND SUBUNIT.
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. GINS4 is
CC important for GINS complex assembly. GINS complex seems to bind
CC preferentially to single-stranded DNA. {ECO:0000269|PubMed:17417653}.
CC -!- SUBUNIT: Component of the GINS complex which is a heterotetramer of
CC GINS1, GINS2, GINS3 and GINS4. Forms a stable subcomplex with GINS1.
CC GINS complex interacts with DNA primase in vitro. Component of the CMG
CC helicase complex, composed of the MCM2-7 complex, the GINS complex and
CC CDC45 (By similarity). {ECO:0000250|UniProtKB:Q7ZT48,
CC ECO:0000269|PubMed:17170760, ECO:0000269|PubMed:17417653,
CC ECO:0000269|PubMed:17545466, ECO:0000269|PubMed:17557111,
CC ECO:0000269|PubMed:17652513, ECO:0000269|PubMed:28414293}.
CC -!- INTERACTION:
CC Q9BRT9; Q9NQY0: BIN3; NbExp=3; IntAct=EBI-747500, EBI-2653038;
CC Q9BRT9; Q9NSA3: CTNNBIP1; NbExp=3; IntAct=EBI-747500, EBI-747082;
CC Q9BRT9; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-747500, EBI-399105;
CC Q9BRT9; Q9Y248: GINS2; NbExp=10; IntAct=EBI-747500, EBI-747491;
CC Q9BRT9; Q96L93-6: KIF16B; NbExp=3; IntAct=EBI-747500, EBI-10988217;
CC Q9BRT9; Q68G74: LHX8; NbExp=3; IntAct=EBI-747500, EBI-8474075;
CC Q9BRT9; Q9BTE3: MCMBP; NbExp=2; IntAct=EBI-747500, EBI-749378;
CC Q9BRT9; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-747500, EBI-10302990;
CC Q9BRT9; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-747500, EBI-1105153;
CC Q9BRT9; A0A0B4J2F2: SIK1B; NbExp=3; IntAct=EBI-747500, EBI-22345187;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99LZ3}.
CC Chromosome {ECO:0000250|UniProtKB:Q7ZT48}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q99LZ3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BRT9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BRT9-2; Sequence=VSP_032738, VSP_032739;
CC -!- INDUCTION: Significantly up-regulated in aggressive melanomas.
CC {ECO:0000269|PubMed:17611626}.
CC -!- MASS SPECTROMETRY: [DNA replication complex GINS protein SLD5]:
CC Mass=98373; Mass_error=13; Method=Electrospray; Note=This is the
CC measured mass for the GINS complex.;
CC Evidence={ECO:0000269|PubMed:17557111};
CC -!- SIMILARITY: Belongs to the GINS4/SLD5 family. {ECO:0000305}.
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DR EMBL; AK095334; BAG53029.1; -; mRNA.
DR EMBL; AK313373; BAG36172.1; -; mRNA.
DR EMBL; CH471080; EAW63256.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63257.1; -; Genomic_DNA.
DR EMBL; BC005995; AAH05995.1; -; mRNA.
DR EMBL; BC027454; AAH27454.1; -; mRNA.
DR CCDS; CCDS6116.1; -. [Q9BRT9-1]
DR RefSeq; NP_115712.1; NM_032336.2. [Q9BRT9-1]
DR RefSeq; XP_005273716.1; XM_005273659.3. [Q9BRT9-1]
DR PDB; 2E9X; X-ray; 2.30 A; D/H=1-223.
DR PDB; 2EHO; X-ray; 3.00 A; A/E/I=11-213.
DR PDB; 2Q9Q; X-ray; 2.36 A; B/F=1-223.
DR PDB; 6XTX; EM; 3.29 A; D=1-223.
DR PDB; 6XTY; EM; 6.77 A; D=1-223.
DR PDB; 7PFO; EM; 3.20 A; G=1-223.
DR PDB; 7PLO; EM; 2.80 A; G=1-223.
DR PDBsum; 2E9X; -.
DR PDBsum; 2EHO; -.
DR PDBsum; 2Q9Q; -.
DR PDBsum; 6XTX; -.
DR PDBsum; 6XTY; -.
DR PDBsum; 7PFO; -.
DR PDBsum; 7PLO; -.
DR AlphaFoldDB; Q9BRT9; -.
DR SMR; Q9BRT9; -.
DR BioGRID; 124023; 78.
DR ComplexPortal; CPX-787; GINS complex.
DR CORUM; Q9BRT9; -.
DR DIP; DIP-29334N; -.
DR IntAct; Q9BRT9; 31.
DR MINT; Q9BRT9; -.
DR STRING; 9606.ENSP00000276533; -.
DR GlyGen; Q9BRT9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BRT9; -.
DR PhosphoSitePlus; Q9BRT9; -.
DR BioMuta; GINS4; -.
DR DMDM; 74732928; -.
DR EPD; Q9BRT9; -.
DR jPOST; Q9BRT9; -.
DR MassIVE; Q9BRT9; -.
DR MaxQB; Q9BRT9; -.
DR PaxDb; Q9BRT9; -.
DR PeptideAtlas; Q9BRT9; -.
DR PRIDE; Q9BRT9; -.
DR ProteomicsDB; 78835; -. [Q9BRT9-1]
DR ProteomicsDB; 78836; -. [Q9BRT9-2]
DR Antibodypedia; 11239; 116 antibodies from 24 providers.
DR DNASU; 84296; -.
DR Ensembl; ENST00000276533.4; ENSP00000276533.3; ENSG00000147536.12. [Q9BRT9-1]
DR Ensembl; ENST00000518671.5; ENSP00000428754.1; ENSG00000147536.12. [Q9BRT9-1]
DR Ensembl; ENST00000520710.5; ENSP00000429581.1; ENSG00000147536.12. [Q9BRT9-2]
DR GeneID; 84296; -.
DR KEGG; hsa:84296; -.
DR MANE-Select; ENST00000276533.4; ENSP00000276533.3; NM_032336.3; NP_115712.1.
DR UCSC; uc003xnx.3; human. [Q9BRT9-1]
DR CTD; 84296; -.
DR DisGeNET; 84296; -.
DR GeneCards; GINS4; -.
DR HGNC; HGNC:28226; GINS4.
DR HPA; ENSG00000147536; Tissue enhanced (lymphoid).
DR MIM; 610611; gene.
DR neXtProt; NX_Q9BRT9; -.
DR OpenTargets; ENSG00000147536; -.
DR PharmGKB; PA145008337; -.
DR VEuPathDB; HostDB:ENSG00000147536; -.
DR eggNOG; KOG3176; Eukaryota.
DR GeneTree; ENSGT00390000003246; -.
DR HOGENOM; CLU_2252901_0_0_1; -.
DR InParanoid; Q9BRT9; -.
DR OMA; ILETAWI; -.
DR OrthoDB; 1434266at2759; -.
DR PhylomeDB; Q9BRT9; -.
DR TreeFam; TF105863; -.
DR PathwayCommons; Q9BRT9; -.
DR Reactome; R-HSA-176974; Unwinding of DNA.
DR SignaLink; Q9BRT9; -.
DR BioGRID-ORCS; 84296; 776 hits in 1095 CRISPR screens.
DR ChiTaRS; GINS4; human.
DR EvolutionaryTrace; Q9BRT9; -.
DR GenomeRNAi; 84296; -.
DR Pharos; Q9BRT9; Tbio.
DR PRO; PR:Q9BRT9; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9BRT9; protein.
DR Bgee; ENSG00000147536; Expressed in oocyte and 105 other tissues.
DR ExpressionAtlas; Q9BRT9; baseline and differential.
DR Genevisible; Q9BRT9; HS.
DR GO; GO:0071162; C:CMG complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0001833; P:inner cell mass cell proliferation; IEA:Ensembl.
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 CDD; cd11711; GINS_A_Sld5; 1.
DR InterPro; IPR021151; GINS_A.
DR InterPro; IPR036224; GINS_bundle-like_dom_sf.
DR InterPro; IPR008591; GINS_Sld5.
DR InterPro; IPR031633; SLD5_C.
DR InterPro; IPR038749; Sld5_GINS_A.
DR PANTHER; PTHR21206; PTHR21206; 1.
DR Pfam; PF05916; Sld5; 1.
DR Pfam; PF16922; SLD5_C; 1.
DR PIRSF; PIRSF007764; Sld5; 1.
DR SUPFAM; SSF158573; SSF158573; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromosome; Cytoplasm;
KW DNA replication; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..223
FT /note="DNA replication complex GINS protein SLD5"
FT /id="PRO_0000327620"
FT INIT_MET 1
FT /note="Removed; alternate"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CHAIN 2..223
FT /note="DNA replication complex GINS protein SLD5, N-
FT terminally processed"
FT /id="PRO_0000421794"
FT REGION 166..223
FT /note="Important for GINS complex assembly"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2
FT /note="N-acetylthreonine; in DNA replication complex GINS
FT protein SLD5, N-terminally processed"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VAR_SEQ 100
FT /note="I -> V (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032738"
FT VAR_SEQ 101..223
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032739"
FT HELIX 23..39
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:2EHO"
FT HELIX 48..60
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 72..102
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 124..144
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 146..148
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 170..177
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 203..207
FT /evidence="ECO:0007829|PDB:2E9X"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:2E9X"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:2E9X"
SQ SEQUENCE 223 AA; 26047 MW; 8FAB619A21968BB9 CRC64;
MTEEVDFLGQ DSDGGSEEVV LTPAELIERL EQAWMNEKFA PELLESKPEI VECVMEQLEH
MEENLRRAKR EDLKVSIHQM EMERIRYVLS SYLRCRLMKI EKFFPHVLEK EKTRPEGEPS
SLSPEELAFA REFMANTESY LKNVALKHMP PNLQKVDLFR AVPKPDLDSY VFLRVRERQE
NILVEPDTDE QRDYVIDLEK GSQHLIRYKT IAPLVASGAV QLI
