LIN9_HUMAN
ID LIN9_HUMAN Reviewed; 542 AA.
AC Q5TKA1; Q5U5L8; Q5U7E1; Q6PI55; Q6ZTV4; Q7Z3J1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein lin-9 homolog;
DE Short=HuLin-9;
DE Short=hLin-9;
DE AltName: Full=Beta subunit-associated regulator of apoptosis;
DE AltName: Full=TUDOR gene similar protein;
DE AltName: Full=Type I interferon receptor beta chain-associated protein;
DE AltName: Full=pRB-associated protein;
GN Name=LIN9; Synonyms=BARA, TGS;
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] (ISOFORM 1), FUNCTION, INTERACTION WITH RB1,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=15538385; DOI=10.1038/sj.emboj.7600470;
RA Gagrica S., Hauser S., Kolfschoten I., Osterloh L., Agami R., Gaubatz S.;
RT "Inhibition of oncogenic transformation by mammalian Lin-9, a pRB-
RT associated protein.";
RL EMBO J. 23:4627-4638(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), FUNCTION, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Myeloma;
RX PubMed=16730350; DOI=10.1016/j.yexcr.2006.04.002;
RA Sandoval R., Xue J., Tian X., Barrett K., Pilkinton M., Ucker D.S.,
RA Raychaudhuri P., Kineman R.D., Luque R.M., Baida G., Zou X., Valli V.E.,
RA Cook J.L., Kiyokawa H., Colamonici O.R.;
RT "A mutant allele of BARA/LIN-9 rescues the cdk4-/- phenotype by releasing
RT the repression on E2F-regulated genes.";
RL Exp. Cell Res. 312:2465-2475(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
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 IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17671431; DOI=10.4161/cc.6.15.4512;
RA Schmit F., Korenjak M., Mannefeld M., Schmitt K., Franke C., von Eyss B.,
RA Gagrica S., Haenel F., Brehm A., Gaubatz S.;
RT "LINC, a human complex that is related to pRB-containing complexes in
RT invertebrates regulates the expression of G2/M genes.";
RL Cell Cycle 6:1903-1913(2007).
RN [7]
RP IDENTIFICATION IN THE DREAM COMPLEX.
RX PubMed=17531812; DOI=10.1016/j.molcel.2007.04.015;
RA Litovchick L., Sadasivam S., Florens L., Zhu X., Swanson S.K.,
RA Velmurugan S., Chen R., Washburn M.P., Liu X.S., DeCaprio J.A.;
RT "Evolutionarily conserved multisubunit RBL2/p130 and E2F4 protein complex
RT represses human cell cycle-dependent genes in quiescence.";
RL Mol. Cell 26:539-551(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, AND
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, AND
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-321, AND
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; THR-304; SER-309 AND
RP SER-321, AND 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65 AND THR-96, AND
RP IDENTIFICATION BY 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-21, 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).
CC -!- FUNCTION: Acts as a tumor suppressor. Inhibits DNA synthesis. Its
CC ability to inhibit oncogenic transformation is mediated through its
CC association with RB1. Plays a role in the expression of genes required
CC for the G1/S transition. {ECO:0000269|PubMed:15538385,
CC ECO:0000269|PubMed:16730350}.
CC -!- SUBUNIT: Component of the DREAM complex (also named LINC complex) at
CC least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2,
CC RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent
CC cells where it represses cell cycle-dependent genes. It dissociates in
CC S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds
CC to MYBL2. Interacts with RB1. {ECO:0000269|PubMed:15538385,
CC ECO:0000269|PubMed:17531812, ECO:0000269|PubMed:17671431}.
CC -!- INTERACTION:
CC Q5TKA1; Q16254: E2F4; NbExp=3; IntAct=EBI-1389424, EBI-448943;
CC Q5TKA1; P10244: MYBL2; NbExp=7; IntAct=EBI-1389424, EBI-1389468;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:15538385, ECO:0000269|PubMed:16730350}. Note=Found
CC in perinucleolar structures. Associated with chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Lin9-L, Long form;
CC IsoId=Q5TKA1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5TKA1-2; Sequence=VSP_020509;
CC Name=3; Synonyms=Lin9-S, Short form;
CC IsoId=Q5TKA1-3; Sequence=VSP_020510;
CC -!- TISSUE SPECIFICITY: Expressed in thymus and testis.
CC {ECO:0000269|PubMed:15538385}.
CC -!- SIMILARITY: Belongs to the lin-9 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH43444.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD97871.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY786184; AAV41873.1; -; mRNA.
DR EMBL; AF190323; AAQ13710.1; -; mRNA.
DR EMBL; AF190324; AAQ13711.1; -; mRNA.
DR EMBL; AK126177; BAC86475.1; -; mRNA.
DR EMBL; BX537869; CAD97871.1; ALT_INIT; mRNA.
DR EMBL; BC043444; AAH43444.1; ALT_INIT; mRNA.
DR EMBL; BC045625; AAH45625.1; -; mRNA.
DR CCDS; CCDS1553.1; -. [Q5TKA1-2]
DR RefSeq; NP_001257338.1; NM_001270409.1.
DR RefSeq; NP_001257339.1; NM_001270410.1.
DR RefSeq; NP_775106.2; NM_173083.3. [Q5TKA1-2]
DR PDB; 6C48; X-ray; 2.32 A; A/D=333-450.
DR PDB; 7N40; X-ray; 2.55 A; B=95-274.
DR PDBsum; 6C48; -.
DR PDBsum; 7N40; -.
DR AlphaFoldDB; Q5TKA1; -.
DR SMR; Q5TKA1; -.
DR BioGRID; 130420; 104.
DR CORUM; Q5TKA1; -.
DR IntAct; Q5TKA1; 41.
DR MINT; Q5TKA1; -.
DR STRING; 9606.ENSP00000329102; -.
DR iPTMnet; Q5TKA1; -.
DR PhosphoSitePlus; Q5TKA1; -.
DR BioMuta; LIN9; -.
DR DMDM; 74708186; -.
DR EPD; Q5TKA1; -.
DR jPOST; Q5TKA1; -.
DR MassIVE; Q5TKA1; -.
DR MaxQB; Q5TKA1; -.
DR PaxDb; Q5TKA1; -.
DR PeptideAtlas; Q5TKA1; -.
DR PRIDE; Q5TKA1; -.
DR ProteomicsDB; 65201; -. [Q5TKA1-1]
DR ProteomicsDB; 65202; -. [Q5TKA1-2]
DR ProteomicsDB; 65203; -. [Q5TKA1-3]
DR Antibodypedia; 34650; 149 antibodies from 22 providers.
DR DNASU; 286826; -.
DR Ensembl; ENST00000328205.9; ENSP00000329102.5; ENSG00000183814.16. [Q5TKA1-2]
DR Ensembl; ENST00000681046.1; ENSP00000505590.1; ENSG00000183814.16. [Q5TKA1-1]
DR GeneID; 286826; -.
DR KEGG; hsa:286826; -.
DR MANE-Select; ENST00000681046.1; ENSP00000505590.1; NM_001366245.2; NP_001353174.1.
DR UCSC; uc001hqa.4; human. [Q5TKA1-1]
DR CTD; 286826; -.
DR DisGeNET; 286826; -.
DR GeneCards; LIN9; -.
DR HGNC; HGNC:30830; LIN9.
DR HPA; ENSG00000183814; Low tissue specificity.
DR MIM; 609375; gene.
DR neXtProt; NX_Q5TKA1; -.
DR OpenTargets; ENSG00000183814; -.
DR PharmGKB; PA134970771; -.
DR VEuPathDB; HostDB:ENSG00000183814; -.
DR eggNOG; KOG1019; Eukaryota.
DR GeneTree; ENSGT00390000003188; -.
DR InParanoid; Q5TKA1; -.
DR OMA; WIWCEFV; -.
DR OrthoDB; 622946at2759; -.
DR PhylomeDB; Q5TKA1; -.
DR TreeFam; TF314315; -.
DR PathwayCommons; Q5TKA1; -.
DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex.
DR Reactome; R-HSA-1362300; Transcription of E2F targets under negative control by p107 (RBL1) and p130 (RBL2) in complex with HDAC1.
DR Reactome; R-HSA-1538133; G0 and Early G1.
DR Reactome; R-HSA-156711; Polo-like kinase mediated events.
DR Reactome; R-HSA-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-HSA-69205; G1/S-Specific Transcription.
DR Reactome; R-HSA-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR SignaLink; Q5TKA1; -.
DR SIGNOR; Q5TKA1; -.
DR BioGRID-ORCS; 286826; 316 hits in 1088 CRISPR screens.
DR ChiTaRS; LIN9; human.
DR GeneWiki; LIN9; -.
DR GenomeRNAi; 286826; -.
DR Pharos; Q5TKA1; Tbio.
DR PRO; PR:Q5TKA1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q5TKA1; protein.
DR Bgee; ENSG00000183814; Expressed in ventricular zone and 126 other tissues.
DR ExpressionAtlas; Q5TKA1; baseline and differential.
DR Genevisible; Q5TKA1; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0017053; C:transcription repressor complex; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0051726; P:regulation of cell cycle; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0000003; P:reproduction; IBA:GO_Central.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR033471; DIRP.
DR InterPro; IPR010561; LIN-9/ALY1.
DR InterPro; IPR045831; LIN9_C.
DR PANTHER; PTHR21689; PTHR21689; 1.
DR Pfam; PF06584; DIRP; 1.
DR Pfam; PF19438; LIN9_C; 1.
DR SMART; SM01135; DIRP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Coiled coil;
KW DNA synthesis; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Tumor suppressor; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..542
FT /note="Protein lin-9 homolog"
FT /id="PRO_0000249546"
FT REGION 2..296
FT /note="Sufficient for interaction with RB1"
FT /evidence="ECO:0000269|PubMed:15538385"
FT COILED 354..413
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 95
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C735"
FT MOD_RES 96
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 304
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT CROSSLNK 21
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1
FT /note="M -> MHRGGQPLKKRRGSFKM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020509"
FT VAR_SEQ 54..88
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16730350"
FT /id="VSP_020510"
FT CONFLICT 436
FT /note="E -> V (in Ref. 5; AAH43444)"
FT /evidence="ECO:0000305"
FT CONFLICT 508
FT /note="S -> R (in Ref. 1; AAV41873)"
FT /evidence="ECO:0000305"
FT HELIX 340..375
FT /evidence="ECO:0007829|PDB:6C48"
FT HELIX 382..412
FT /evidence="ECO:0007829|PDB:6C48"
SQ SEQUENCE 542 AA; 61946 MW; 1107865E6FF33037 CRC64;
MAELDQLPDE SSSAKALVSL KEGSLSNTWN EKYSSLQKTP VWKGRNTSSA VEMPFRNSKR
SRLFSDEDDR QINTRSPKRN QRVAMVPQKF TATMSTPDKK ASQKIGFRLR NLLKLPKAHK
WCIYEWFYSN IDKPLFEGDN DFCVCLKESF PNLKTRKLTR VEWGKIRRLM GKPRRCSSAF
FEEERSALKQ KRQKIRLLQQ RKVADVSQFK DLPDEIPLPL VIGTKVTARL RGVHDGLFTG
QIDAVDTLNA TYRVTFDRTG LGTHTIPDYE VLSNEPHETM PIAAFGQKQR PSRFFMTPPR
LHYTPPLQSP IIDNDPLLGQ SPWRSKISGS DTETLGGFPV EFLIQVTRLS KILMIKKEHI
KKLREMNTEA EKLKSYSMPI SIEFQRRYAT IVLELEQLNK DLNKVLHKVQ QYCYELAPDQ
GLQPADQPTD MRRRCEEEAQ EIVRHANSST GQPCVENENL TDLISRLTAI LLQIKCLAEG
GDLNSFEFKS LTDSLNDIKS TIDASNISCF QNNVEIHVAH IQSGLSQMGN LHAFAANNTN
RD
