GEMI6_HUMAN
ID GEMI6_HUMAN Reviewed; 167 AA.
AC Q8WXD5; B2RDP8; Q53SI5; Q8WVB4; Q9H5G6;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Gem-associated protein 6;
DE Short=Gemin-6;
DE AltName: Full=SIP2;
GN Name=GEMIN6;
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], PROTEIN SEQUENCE OF 155-167, FUNCTION,
RP INTERACTION WITH SNRPB; SNRPD2; SNRPD3 AND SNRPE, AND SUBCELLULAR LOCATION.
RX PubMed=11748230; DOI=10.1074/jbc.m110141200;
RA Pellizzoni L., Baccon J., Rappsilber J., Mann M., Dreyfuss G.;
RT "Purification of native survival of motor neurons complexes and
RT identification of Gemin6 as a novel component.";
RL J. Biol. Chem. 277:7540-7545(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Small intestine;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-140.
RC TISSUE=Ovary;
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 INTERACTION WITH GEMIN7.
RX PubMed=12065586; DOI=10.1074/jbc.m203478200;
RA Baccon J., Pellizzoni L., Rappsilber J., Mann M., Dreyfuss G.;
RT "Identification and characterization of Gemin7, a novel component of the
RT survival of motor neuron complex.";
RL J. Biol. Chem. 277:31957-31962(2002).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE SMN COMPLEX, AND IDENTIFICATION IN SMN-SM
RP COMPLEX.
RX PubMed=16314521; DOI=10.1128/mcb.25.24.10989-11004.2005;
RA Golembe T.J., Yong J., Dreyfuss G.;
RT "Specific sequence features, recognized by the SMN complex, identify snRNAs
RT and determine their fate as snRNPs.";
RL Mol. Cell. Biol. 25:10989-11004(2005).
RN [8]
RP IDENTIFICATION IN THE SMN COMPLEX, AND INTERACTION WITH GEMIN7.
RX PubMed=17178713; DOI=10.1074/jbc.m608528200;
RA Otter S., Grimmler M., Neuenkirchen N., Chari A., Sickmann A., Fischer U.;
RT "A comprehensive interaction map of the human survival of motor neuron
RT (SMN) complex.";
RL J. Biol. Chem. 282:5825-5833(2007).
RN [9]
RP FUNCTION IN SNRNP BIOGENESIS, AND IDENTIFICATION IN SMN-SM COMPLEX.
RX PubMed=18984161; DOI=10.1016/j.cell.2008.09.020;
RA Chari A., Golas M.M., Klingenhager M., Neuenkirchen N., Sander B.,
RA Englbrecht C., Sickmann A., Stark H., Fischer U.;
RT "An assembly chaperone collaborates with the SMN complex to generate
RT spliceosomal SnRNPs.";
RL Cell 135:497-509(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, AND IDENTIFICATION BY
RP 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95, 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 [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-86 IN COMPLEX WITH GEMIN7, AND
RP INTERACTION WITH SNRPB; SNRPD2; SNRPD3 AND SNRPE.
RX PubMed=15939020; DOI=10.1016/j.str.2005.03.014;
RA Ma Y., Dostie J., Dreyfuss G., Van Duyne G.D.;
RT "The Gemin6-Gemin7 heterodimer from the survival of motor neurons complex
RT has an Sm protein-like structure.";
RL Structure 13:883-892(2005).
RN [15] {ECO:0007744|PDB:7BBL}
RP X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 1-92, AND INTERACTION WITH GEMIN7
RP AND GEMIN8.
RX PubMed=33754639; DOI=10.1093/nar/gkab158;
RA Veepaschit J., Viswanathan A., Bordonne R., Grimm C., Fischer U.;
RT "Identification and structural analysis of the Schizosaccharomyces pombe
RT SMN complex.";
RL Nucleic Acids Res. 49:gkab158-gkab158(2021).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP.
CC {ECO:0000269|PubMed:11748230, ECO:0000269|PubMed:18984161}.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP
CC (PubMed:18984161, PubMed:11748230, PubMed:15939020, PubMed:12065586,
CC PubMed:16314521, PubMed:17178713). Part of the SMN-Sm complex that
CC contains SMN1, GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6,
CC GEMIN7, GEMIN8, STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2,
CC SNRPD3, SNRPE, SNRPF and SNRPG (PubMed:18984161, PubMed:16314521).
CC Interacts with GEMIN7; the interaction is direct (PubMed:12065586,
CC PubMed:15939020, PubMed:33754639, PubMed:17178713). Interacts with
CC GEMIN8; the interaction is direct (PubMed:33754639). Interacts with
CC SNRPB, SNRPD2, SNRPD3 and SNRPE; the interaction is direct
CC (PubMed:11748230, PubMed:15939020). {ECO:0000269|PubMed:11748230,
CC ECO:0000269|PubMed:12065586, ECO:0000269|PubMed:15939020,
CC ECO:0000269|PubMed:16314521, ECO:0000269|PubMed:17178713,
CC ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:33754639}.
CC -!- INTERACTION:
CC Q8WXD5; Q8WXI4-2: ACOT11; NbExp=3; IntAct=EBI-752301, EBI-17721098;
CC Q8WXD5; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-752301, EBI-742054;
CC Q8WXD5; Q9H840: GEMIN7; NbExp=21; IntAct=EBI-752301, EBI-715455;
CC Q8WXD5; Q9BPW5: RASL11B; NbExp=3; IntAct=EBI-752301, EBI-745409;
CC Q8WXD5; P62314: SNRPD1; NbExp=2; IntAct=EBI-752301, EBI-372177;
CC Q8WXD5; P62304: SNRPE; NbExp=2; IntAct=EBI-752301, EBI-348082;
CC Q8WXD5; P62306: SNRPF; NbExp=2; IntAct=EBI-752301, EBI-356900;
CC Q8WXD5; Q9Y3F4: STRAP; NbExp=4; IntAct=EBI-752301, EBI-727414;
CC Q8WXD5; O94842: TOX4; NbExp=3; IntAct=EBI-752301, EBI-948613;
CC Q8WXD5; P12520: vpr; Xeno; NbExp=3; IntAct=EBI-752301, EBI-6164519;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:11748230}. Nucleus, gem
CC {ECO:0000269|PubMed:11748230}. Cytoplasm {ECO:0000269|PubMed:11748230}.
CC Note=Found both in the nucleoplasm and in nuclear bodies called gems
CC (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled)
CC bodies. Also found in the cytoplasm.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15660.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF453443; AAL48292.1; -; mRNA.
DR EMBL; AK027112; BAB15660.1; ALT_FRAME; mRNA.
DR EMBL; AK315627; BAG37995.1; -; mRNA.
DR EMBL; AC018693; AAY24255.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00360.1; -; Genomic_DNA.
DR EMBL; BC018195; AAH18195.1; -; mRNA.
DR CCDS; CCDS1799.1; -.
DR RefSeq; NP_079051.9; NM_024775.9.
DR PDB; 1Y96; X-ray; 2.00 A; A/C=1-86.
DR PDB; 7BBL; X-ray; 1.52 A; A/C=1-92.
DR PDBsum; 1Y96; -.
DR PDBsum; 7BBL; -.
DR AlphaFoldDB; Q8WXD5; -.
DR SMR; Q8WXD5; -.
DR BioGRID; 122925; 91.
DR ComplexPortal; CPX-6031; SMN complex.
DR CORUM; Q8WXD5; -.
DR DIP; DIP-41331N; -.
DR IntAct; Q8WXD5; 43.
DR MINT; Q8WXD5; -.
DR STRING; 9606.ENSP00000281950; -.
DR GlyGen; Q8WXD5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8WXD5; -.
DR PhosphoSitePlus; Q8WXD5; -.
DR BioMuta; GEMIN6; -.
DR DMDM; 34921901; -.
DR EPD; Q8WXD5; -.
DR jPOST; Q8WXD5; -.
DR MassIVE; Q8WXD5; -.
DR MaxQB; Q8WXD5; -.
DR PaxDb; Q8WXD5; -.
DR PeptideAtlas; Q8WXD5; -.
DR PRIDE; Q8WXD5; -.
DR ProteomicsDB; 75014; -.
DR Antibodypedia; 29530; 181 antibodies from 26 providers.
DR DNASU; 79833; -.
DR Ensembl; ENST00000281950.8; ENSP00000281950.2; ENSG00000152147.11.
DR GeneID; 79833; -.
DR KEGG; hsa:79833; -.
DR MANE-Select; ENST00000281950.8; ENSP00000281950.2; NM_024775.10; NP_079051.9.
DR UCSC; uc002rrc.4; human.
DR CTD; 79833; -.
DR DisGeNET; 79833; -.
DR GeneCards; GEMIN6; -.
DR HGNC; HGNC:20044; GEMIN6.
DR HPA; ENSG00000152147; Low tissue specificity.
DR MIM; 607006; gene.
DR neXtProt; NX_Q8WXD5; -.
DR OpenTargets; ENSG00000152147; -.
DR PharmGKB; PA134952855; -.
DR VEuPathDB; HostDB:ENSG00000152147; -.
DR eggNOG; ENOG502RZTW; Eukaryota.
DR GeneTree; ENSGT00390000006712; -.
DR HOGENOM; CLU_127294_0_0_1; -.
DR InParanoid; Q8WXD5; -.
DR OMA; KSPLEWE; -.
DR OrthoDB; 1625274at2759; -.
DR PhylomeDB; Q8WXD5; -.
DR TreeFam; TF314693; -.
DR PathwayCommons; Q8WXD5; -.
DR Reactome; R-HSA-191859; snRNP Assembly.
DR Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR SignaLink; Q8WXD5; -.
DR SIGNOR; Q8WXD5; -.
DR BioGRID-ORCS; 79833; 606 hits in 1050 CRISPR screens.
DR ChiTaRS; GEMIN6; human.
DR EvolutionaryTrace; Q8WXD5; -.
DR GeneWiki; Gem-associated_protein_6; -.
DR GenomeRNAi; 79833; -.
DR Pharos; Q8WXD5; Tbio.
DR PRO; PR:Q8WXD5; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8WXD5; protein.
DR Bgee; ENSG00000152147; Expressed in tendon of biceps brachii and 172 other tissues.
DR ExpressionAtlas; Q8WXD5; baseline and differential.
DR Genevisible; Q8WXD5; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR InterPro; IPR009422; Gemin6.
DR PANTHER; PTHR14710; PTHR14710; 1.
DR Pfam; PF06372; Gemin6; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..167
FT /note="Gem-associated protein 6"
FT /id="PRO_0000087460"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT VARIANT 140
FT /note="G -> D (in dbSNP:rs1056104)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_020391"
FT HELIX 3..6
FT /evidence="ECO:0007829|PDB:1Y96"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:7BBL"
FT TURN 14..17
FT /evidence="ECO:0007829|PDB:7BBL"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:7BBL"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:7BBL"
FT STRAND 28..37
FT /evidence="ECO:0007829|PDB:7BBL"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:7BBL"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:7BBL"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:7BBL"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:7BBL"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:7BBL"
FT HELIX 76..83
FT /evidence="ECO:0007829|PDB:7BBL"
SQ SEQUENCE 167 AA; 18824 MW; 908EEFDA73A0C07F CRC64;
MSEWMKKGPL EWQDYIYKEV RVTASEKNEY KGWVLTTDPV SANIVLVNFL EDGSMSVTGI
MGHAVQTVET MNEGDHRVRE KLMHLFTSGD CKAYSPEDLE ERKNSLKKWL EKNHIPITEQ
GDAPRTLCVA GVLTIDPPYG PENCSSSNEI ILSRVQDLIE GHLTASQ
