ID   GEMI7_HUMAN             Reviewed;         131 AA.
AC   Q9H840; Q6IA34;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   10-JUN-2026, entry version 191.
DE   RecName: Full=Gem-associated protein 7;
DE            Short=Gemin-7;
DE   AltName: Full=SIP3;
GN   Name=GEMIN7;
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 30-57, FUNCTION,
RP   INTERACTION WITH SMN1; GEMIN6; SNRPB; SNRPD2; SNRPD3 AND SNRPE, AND
RP   SUBCELLULAR LOCATION.
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Retinoblastoma;
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 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   [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].
RC   TISSUE=Uterus;
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   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   [7]
RP   IDENTIFICATION IN THE SMN COMPLEX, AND INTERACTION WITH GEMIN6 AND
RP   STRAP/UNRIP.
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   [8]
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   [9]
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   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND IDENTIFICATION BY MASS
RP   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   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 47-131 IN COMPLEX WITH GEMIN6, 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   [14] {ECO:0007744|PDB:7BBL}
RP   X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 46-131, AND INTERACTION WITH
RP   GEMIN6 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:12065586, 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:12065586, PubMed:15939020, PubMed:16314521, PubMed:17178713,
CC       PubMed:18984161). Part of the SMN-Sm complex that contains SMN1,
CC       GEMIN2/SIP1, DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8,
CC       STRAP/UNRIP and the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE,
CC       SNRPF and SNRPG (PubMed:16314521, PubMed:18984161). Interacts with
CC       GEMIN6; the interaction is direct (PubMed:12065586, PubMed:15939020,
CC       PubMed:17178713, PubMed:33754639). Interacts with STRAP/UNRIP; the
CC       interaction is direct (PubMed:17178713). Interacts with GEMIN8; the
CC       interaction is direct (PubMed:33754639). Interacts with SNRPB, SNRPD2,
CC       SNRPD3 and SNRPE; the interaction is direct (PubMed:12065586,
CC       PubMed:15939020). {ECO:0000269|PubMed:12065586,
CC       ECO:0000269|PubMed:15939020, ECO:0000269|PubMed:16314521,
CC       ECO:0000269|PubMed:17178713, ECO:0000269|PubMed:18984161,
CC       ECO:0000269|PubMed:33754639}.
CC   -!- INTERACTION:
CC       Q9H840; Q8WXD5: GEMIN6; NbExp=23; IntAct=EBI-715455, EBI-752301;
CC       Q9H840; Q9Y3F4: STRAP; NbExp=7; IntAct=EBI-715455, EBI-727414;
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000269|PubMed:12065586}. Nucleus, gem
CC       {ECO:0000269|PubMed:12065586}. Cytoplasm {ECO:0000269|PubMed:12065586}.
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   -!- SIMILARITY: Belongs to the gemin-7 family. {ECO:0000305}.
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DR   EMBL; AY114106; AAM44083.1; -; mRNA.
DR   EMBL; AK024018; BAB14780.1; -; mRNA.
DR   EMBL; CR457321; CAG33602.1; -; mRNA.
DR   EMBL; CH471126; EAW57321.1; -; Genomic_DNA.
DR   EMBL; BC007793; AAH07793.1; -; mRNA.
DR   CCDS; CCDS12654.1; -.
DR   RefSeq; NP_001007270.1; NM_001007269.2.
DR   RefSeq; NP_001007271.1; NM_001007270.2.
DR   RefSeq; NP_001305983.1; NM_001319054.1.
DR   RefSeq; NP_001305984.1; NM_001319055.2.
DR   RefSeq; NP_078983.1; NM_024707.3.
DR   RefSeq; XP_005259320.1; XM_005259263.6.
DR   PDB; 1Y96; X-ray; 2.00 A; B/D=47-131.
DR   PDB; 7BBL; X-ray; 1.52 A; B/D=46-131.
DR   AlphaFoldDB; Q9H840; -.
DR   SMR; Q9H840; -.
DR   BioGRID; 122869; 76.
DR   ComplexPortal; CPX-6031; Survival motor neuron complex.
DR   CORUM; Q9H840; -.
DR   DIP; DIP-41750N; -.
DR   FunCoup; Q9H840; 918.
DR   IntAct; Q9H840; 61.
DR   MINT; Q9H840; -.
DR   NDEx; IQUERY-CP-GEMIN7; 3 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000270257; -.
DR   ChEMBL; CHEMBL4105841; -.
DR   iPTMnet; Q9H840; -.
DR   PhosphoSitePlus; Q9H840; -.
DR   BioMuta; GEMIN7; -.
DR   DMDM; 34922127; -.
DR   jPOST; Q9H840; -.
DR   MassIVE; Q9H840; -.
DR   PaxDb; 9606-ENSP00000270257; -.
DR   PeptideAtlas; Q9H840; -.
DR   ProteomicsDB; 81175; -.
DR   Pumba; Q9H840; -.
DR   Antibodypedia; 31264; 155 antibodies from 22 providers.
DR   DNASU; 79760; -.
DR   Ensembl; ENST00000270257.9; ENSP00000270257.3; ENSG00000142252.12.
DR   Ensembl; ENST00000391951.2; ENSP00000375813.1; ENSG00000142252.12.
DR   Ensembl; ENST00000591607.1; ENSP00000466342.1; ENSG00000142252.12.
DR   Ensembl; ENST00000591747.5; ENSP00000465704.1; ENSG00000142252.12.
DR   Ensembl; ENST00000885624.1; ENSP00000555683.1; ENSG00000142252.12.
DR   Ensembl; ENST00000885625.1; ENSP00000555684.1; ENSG00000142252.12.
DR   Ensembl; ENST00000885626.1; ENSP00000555685.1; ENSG00000142252.12.
DR   Ensembl; ENST00000885627.1; ENSP00000555686.1; ENSG00000142252.12.
DR   Ensembl; ENST00000885628.1; ENSP00000555687.1; ENSG00000142252.12.
DR   Ensembl; ENST00000885629.1; ENSP00000555688.1; ENSG00000142252.12.
DR   Ensembl; ENST00000885630.1; ENSP00000555689.1; ENSG00000142252.12.
DR   Ensembl; ENST00000885631.1; ENSP00000555690.1; ENSG00000142252.12.
DR   Ensembl; ENST00000885632.1; ENSP00000555691.1; ENSG00000142252.12.
DR   Ensembl; ENST00000885633.1; ENSP00000555692.1; ENSG00000142252.12.
DR   Ensembl; ENST00000925297.1; ENSP00000595356.1; ENSG00000142252.12.
DR   Ensembl; ENST00000925298.1; ENSP00000595357.1; ENSG00000142252.12.
DR   Ensembl; ENST00000925299.1; ENSP00000595358.1; ENSG00000142252.12.
DR   Ensembl; ENST00000925300.1; ENSP00000595359.1; ENSG00000142252.12.
DR   Ensembl; ENST00000925301.1; ENSP00000595360.1; ENSG00000142252.12.
DR   Ensembl; ENST00000925302.1; ENSP00000595361.1; ENSG00000142252.12.
DR   Ensembl; ENST00000925303.1; ENSP00000595362.1; ENSG00000142252.12.
DR   Ensembl; ENST00000925304.1; ENSP00000595363.1; ENSG00000142252.12.
DR   Ensembl; ENST00000925305.1; ENSP00000595364.1; ENSG00000142252.12.
DR   Ensembl; ENST00000956990.1; ENSP00000627049.1; ENSG00000142252.12.
DR   Ensembl; ENST00000956991.1; ENSP00000627050.1; ENSG00000142252.12.
DR   GeneID; 79760; -.
DR   KEGG; hsa:79760; -.
DR   MANE-Select; ENST00000270257.9; ENSP00000270257.3; NM_024707.3; NP_078983.1.
DR   UCSC; uc002pap.2; human.
DR   AGR; HGNC:20045; -.
DR   ClinPGx; PA134959810; -.
DR   CTD; 79760; -.
DR   DisGeNET; 79760; -.
DR   GeneCards; GEMIN7; -.
DR   HGNC; HGNC:20045; GEMIN7.
DR   HPA; ENSG00000142252; Low tissue specificity.
DR   MIM; 607419; gene.
DR   OpenTargets; ENSG00000142252; -.
DR   VEuPathDB; HostDB:ENSG00000142252; -.
DR   eggNOG; ENOG502S59N; Eukaryota.
DR   GeneTree; ENSGT00390000018039; -.
DR   HOGENOM; CLU_2031900_0_0_1; -.
DR   InParanoid; Q9H840; -.
DR   OMA; CADIISY; -.
DR   OrthoDB; 70763at2759; -.
DR   PAN-GO; Q9H840; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9H840; -.
DR   PathwayCommons; Q9H840; -.
DR   Reactome; R-HSA-191859; snRNP Assembly.
DR   Reactome; R-HSA-9754678; SARS-CoV-2 modulates host translation machinery.
DR   SignaLink; Q9H840; -.
DR   SIGNOR; Q9H840; -.
DR   Agora; ENSG00000142252; -.
DR   BioGRID-ORCS; 79760; 586 hits in 1134 CRISPR screens.
DR   CD-CODE; 6F24707C; Cajal body.
DR   CD-CODE; DEE660B4; Stress granule.
DR   ChiTaRS; GEMIN7; human.
DR   EvolutionaryTrace; Q9H840; -.
DR   GenomeRNAi; 79760; -.
DR   Pharos; Q9H840; Tbio.
DR   PRO; PR:Q9H840; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q9H840; protein.
DR   Bgee; ENSG00000142252; Expressed in lower esophagus mucosa and 145 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0097504; C:Gemini of Cajal bodies; IDA:UniProtKB.
DR   GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR   GO; GO:0120114; C:Sm-like protein family complex; IBA:GO_Central.
DR   GO; GO:0032797; C:SMN complex; IDA:UniProtKB.
DR   GO; GO:0034719; C:SMN-Sm protein complex; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:UniProtKB.
DR   GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
DR   CDD; cd11677; Gemin7; 1.
DR   FunFam; 2.30.30.100:FF:000040; Gem-associated protein 7; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR020338; SMN_gemin7.
DR   InterPro; IPR024642; SUZ-C.
DR   PANTHER; PTHR14679; GEM-ASSOCIATED PROTEIN 7; 1.
DR   PANTHER; PTHR14679:SF1; GEM-ASSOCIATED PROTEIN 7; 1.
DR   Pfam; PF11095; Gemin7; 1.
DR   PROSITE; PS52002; SM; 1.
DR   PROSITE; PS51938; SUZ_C; 1.
DR   PDBsum; 1Y96; -.
DR   PDBsum; 7BBL; -.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW   mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW   Proteomics identification; Reference proteome.
FT   CHAIN           1..131
FT                   /note="Gem-associated protein 7"
FT                   /id="PRO_0000087462"
FT   DOMAIN          1..29
FT                   /note="SUZ-C"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01287"
FT   DOMAIN          65..131
FT                   /note="Sm"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0007744|PubMed:22223895,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         3
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   HELIX           46..50
FT                   /evidence="ECO:0007829|PDB:7BBL"
FT   HELIX           51..71
FT                   /evidence="ECO:0007829|PDB:7BBL"
FT   TURN            72..75
FT                   /evidence="ECO:0007829|PDB:7BBL"
FT   STRAND          76..82
FT                   /evidence="ECO:0007829|PDB:7BBL"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:7BBL"
FT   STRAND          87..95
FT                   /evidence="ECO:0007829|PDB:7BBL"
FT   STRAND          97..99
FT                   /evidence="ECO:0007829|PDB:7BBL"
FT   STRAND          102..109
FT                   /evidence="ECO:0007829|PDB:7BBL"
FT   STRAND          112..119
FT                   /evidence="ECO:0007829|PDB:7BBL"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:7BBL"
FT   STRAND          124..129
FT                   /evidence="ECO:0007829|PDB:7BBL"
SQ   SEQUENCE   131 AA;  14537 MW;  6E118922AFDCF567 CRC64;
     MQTPVNIPVP VLRLPRGPDG FSRGFAPDGR RAPLRPEVPE IQECPIAQES LESQEQRARA
     ALRERYLRSL LAMVGHQVSF TLHEGVRVAA HFGATDLDVA NFYVSQLQTP IGVQAEALLR
     CSDIISYTFK P
//