MARF1_MOUSE
ID MARF1_MOUSE Reviewed; 1730 AA.
AC Q8BJ34; E9QPE4; Q5DU29; Q8C6U4; Q8K2E6;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Meiosis regulator and mRNA stability factor 1 {ECO:0000250|UniProtKB:Q9Y4F3};
DE AltName: Full=Limkain-b1;
DE AltName: Full=Meiosis arrest female protein 1 {ECO:0000312|MGI:MGI:2444505};
GN Name=Marf1; Synonyms=Kiaa0430, Lkap;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1357-1730 (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Urinary bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-756 (ISOFORM 3).
RC TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SEQUENCE REVISION.
RA Okazaki N., Kikuno R.F., Nagase T., Ohara O., Koga H.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-698, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1083 AND SER-1684, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=22442484; DOI=10.1126/science.1214680;
RA Su Y.Q., Sugiura K., Sun F., Pendola J.K., Cox G.A., Handel M.A.,
RA Schimenti J.C., Eppig J.J.;
RT "MARF1 regulates essential oogenic processes in mice.";
RL Science 335:1496-1499(2012).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX PubMed=23090997; DOI=10.1073/pnas.1216904109;
RA Su Y.Q., Sun F., Handel M.A., Schimenti J.C., Eppig J.J.;
RT "Meiosis arrest female 1 (MARF1) has nuage-like function in mammalian
RT oocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18653-18660(2012).
CC -!- FUNCTION: Essential regulator of oogenesis required for female meiotic
CC progression to repress transposable elements and preventing their
CC mobilization, which is essential for the germline integrity. Probably
CC acts via some RNA metabolic process, equivalent to the piRNA system in
CC males, which mediates the repression of transposable elements during
CC meiosis by forming complexes composed of RNAs and governs the
CC methylation and subsequent repression of transposons. Also required to
CC protect from DNA double-strand breaks. {ECO:0000269|PubMed:22442484,
CC ECO:0000269|PubMed:23090997}.
CC -!- SUBUNIT: Interacts with LIMK2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q8BJ34-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJ34-2; Sequence=VSP_022992, VSP_022993, VSP_022997,
CC VSP_022999;
CC Name=3;
CC IsoId=Q8BJ34-3; Sequence=VSP_022992, VSP_022994, VSP_022995,
CC VSP_022996, VSP_022997;
CC Name=4;
CC IsoId=Q8BJ34-4; Sequence=VSP_023002;
CC Name=5;
CC IsoId=Q8BJ34-5; Sequence=VSP_022991, VSP_022998, VSP_023000,
CC VSP_023001;
CC Name=6;
CC IsoId=Q8BJ34-6; Sequence=VSP_022997, VSP_022998, VSP_023002;
CC -!- TISSUE SPECIFICITY: Predominantly present in oocytes and barely
CC detectable in granulosa cells (at protein level).
CC {ECO:0000269|PubMed:22442484}.
CC -!- DEVELOPMENTAL STAGE: Detected in germ cells in quiescent oocytes
CC isolated from newborn P0 ovaries that have not yet commenced the growth
CC phase. Protein levels increase after oocytes initiate growth, and
CC follicular development reach the primary follicle stage at P6.
CC Thereafter, protein levels remain at the similar levels (at protein
CC level). {ECO:0000269|PubMed:23090997}.
CC -!- DISRUPTION PHENOTYPE: Female infertility due to oocyte meiotic arrest
CC at the germinal vesicle stage: ovaries look normal, but oocytes do not
CC resume meiosis even after a superovulatory regimen of gonadotropins and
CC are ovulated at the immature germinal vesicle stage. Oocytes display
CC strong up-regulation of a transcripts, increased retrotransposon
CC expression, defective cytoplasmic maturation, and meiotic arrest.
CC Mutant males are fertile. {ECO:0000269|PubMed:22442484,
CC ECO:0000269|PubMed:23090997}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90407.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK035704; BAC29160.1; -; mRNA.
DR EMBL; AK053159; BAC35289.1; -; mRNA.
DR EMBL; AC119853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC164291; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC031575; AAH31575.1; -; mRNA.
DR EMBL; AK220341; BAD90407.2; ALT_INIT; Transcribed_RNA.
DR CCDS; CCDS37262.1; -. [Q8BJ34-6]
DR RefSeq; NP_001074623.1; NM_001081154.2. [Q8BJ34-6]
DR PDB; 5YAA; X-ray; 1.75 A; A/B/C/D=337-499.
DR PDB; 5YAD; X-ray; 1.76 A; A/B=858-932.
DR PDBsum; 5YAA; -.
DR PDBsum; 5YAD; -.
DR AlphaFoldDB; Q8BJ34; -.
DR SMR; Q8BJ34; -.
DR BioGRID; 230221; 1.
DR STRING; 10090.ENSMUSP00000087770; -.
DR iPTMnet; Q8BJ34; -.
DR PhosphoSitePlus; Q8BJ34; -.
DR EPD; Q8BJ34; -.
DR jPOST; Q8BJ34; -.
DR MaxQB; Q8BJ34; -.
DR PaxDb; Q8BJ34; -.
DR PeptideAtlas; Q8BJ34; -.
DR PRIDE; Q8BJ34; -.
DR ProteomicsDB; 295784; -. [Q8BJ34-1]
DR ProteomicsDB; 295785; -. [Q8BJ34-2]
DR ProteomicsDB; 295786; -. [Q8BJ34-3]
DR ProteomicsDB; 295787; -. [Q8BJ34-4]
DR ProteomicsDB; 295788; -. [Q8BJ34-5]
DR ProteomicsDB; 295789; -. [Q8BJ34-6]
DR Antibodypedia; 3042; 37 antibodies from 14 providers.
DR Ensembl; ENSMUST00000090300; ENSMUSP00000087770; ENSMUSG00000060657. [Q8BJ34-6]
DR GeneID; 223989; -.
DR KEGG; mmu:223989; -.
DR UCSC; uc007ygv.2; mouse. [Q8BJ34-6]
DR UCSC; uc007ygw.2; mouse. [Q8BJ34-5]
DR UCSC; uc007ygx.1; mouse. [Q8BJ34-2]
DR CTD; 9665; -.
DR MGI; MGI:2444505; Marf1.
DR VEuPathDB; HostDB:ENSMUSG00000060657; -.
DR eggNOG; ENOG502QUYZ; Eukaryota.
DR GeneTree; ENSGT00390000002393; -.
DR HOGENOM; CLU_002701_0_0_1; -.
DR InParanoid; Q8BJ34; -.
DR OMA; NNGHIME; -.
DR OrthoDB; 187067at2759; -.
DR TreeFam; TF329117; -.
DR BioGRID-ORCS; 223989; 3 hits in 108 CRISPR screens.
DR ChiTaRS; Marf1; mouse.
DR PRO; PR:Q8BJ34; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8BJ34; protein.
DR Bgee; ENSMUSG00000060657; Expressed in dorsal pancreas and 227 other tissues.
DR ExpressionAtlas; Q8BJ34; baseline and differential.
DR Genevisible; Q8BJ34; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005777; C:peroxisome; ISO:MGI.
DR GO; GO:1905762; F:CCR4-NOT complex binding; IBA:GO_Central.
DR GO; GO:1903231; F:mRNA base-pairing post-transcriptional repressor activity; IBA:GO_Central.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IMP:MGI.
DR GO; GO:0007143; P:female meiotic nuclear division; IMP:UniProtKB.
DR GO; GO:0048477; P:oogenesis; IMP:UniProtKB.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR CDD; cd12255; RRM1_LKAP; 1.
DR CDD; cd12256; RRM2_LKAP; 1.
DR Gene3D; 3.30.420.610; -; 6.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR041966; LOTUS-like.
DR InterPro; IPR024768; Marf1.
DR InterPro; IPR045602; MARF1_LOTUS.
DR InterPro; IPR034189; MARF1_RRM1.
DR InterPro; IPR034191; MARF1_RRM2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR021139; NYN_MARF1.
DR InterPro; IPR025605; OST-HTH/LOTUS_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR14379; PTHR14379; 3.
DR Pfam; PF11608; Limkain-b1; 1.
DR Pfam; PF19687; MARF1_LOTUS; 1.
DR Pfam; PF01936; NYN; 1.
DR Pfam; PF12872; OST-HTH; 5.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR PROSITE; PS51644; HTH_OST; 8.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Differentiation; Meiosis; Oogenesis;
KW Peroxisome; Phosphoprotein; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1730
FT /note="Meiosis regulator and mRNA stability factor 1"
FT /id="PRO_0000276847"
FT DOMAIN 352..489
FT /note="NYN"
FT DOMAIN 781..860
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 865..939
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 993..1069
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1089..1163
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1165..1241
FT /note="HTH OST-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1249..1324
FT /note="HTH OST-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1325..1400
FT /note="HTH OST-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1401..1475
FT /note="HTH OST-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1476..1550
FT /note="HTH OST-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT REGION 655..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1667..1714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F3"
FT MOD_RES 698
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 1081
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F3"
FT MOD_RES 1083
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..566
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022991"
FT VAR_SEQ 1..50
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.4"
FT /id="VSP_022992"
FT VAR_SEQ 97..275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022993"
FT VAR_SEQ 277..287
FT /note="PARNSIIDAAK -> VCIFYSLSWGRRGLVLLNGS (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_022994"
FT VAR_SEQ 291
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_022995"
FT VAR_SEQ 409..448
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_022996"
FT VAR_SEQ 508
FT /note="Missing (in isoform 2, isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.4"
FT /id="VSP_022997"
FT VAR_SEQ 755
FT /note="P -> PRSMSPNLLN (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_022998"
FT VAR_SEQ 757..1730
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022999"
FT VAR_SEQ 812..818
FT /note="KSVELSP -> TSVLLFG (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023000"
FT VAR_SEQ 819..1730
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023001"
FT VAR_SEQ 1591..1592
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_023002"
FT CONFLICT 664
FT /note="S -> T (in Ref. 3; AAH31575)"
FT /evidence="ECO:0000305"
FT STRAND 351..357
FT /evidence="ECO:0007829|PDB:5YAA"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:5YAA"
FT HELIX 369..380
FT /evidence="ECO:0007829|PDB:5YAA"
FT STRAND 385..393
FT /evidence="ECO:0007829|PDB:5YAA"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:5YAA"
FT HELIX 400..408
FT /evidence="ECO:0007829|PDB:5YAA"
FT STRAND 412..415
FT /evidence="ECO:0007829|PDB:5YAA"
FT HELIX 423..438
FT /evidence="ECO:0007829|PDB:5YAA"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:5YAA"
FT HELIX 452..454
FT /evidence="ECO:0007829|PDB:5YAA"
FT HELIX 455..463
FT /evidence="ECO:0007829|PDB:5YAA"
FT STRAND 468..473
FT /evidence="ECO:0007829|PDB:5YAA"
FT HELIX 479..482
FT /evidence="ECO:0007829|PDB:5YAA"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:5YAA"
FT HELIX 491..494
FT /evidence="ECO:0007829|PDB:5YAA"
FT HELIX 861..878
FT /evidence="ECO:0007829|PDB:5YAD"
FT HELIX 881..883
FT /evidence="ECO:0007829|PDB:5YAD"
FT STRAND 884..886
FT /evidence="ECO:0007829|PDB:5YAD"
FT HELIX 887..898
FT /evidence="ECO:0007829|PDB:5YAD"
FT HELIX 904..907
FT /evidence="ECO:0007829|PDB:5YAD"
FT TURN 911..913
FT /evidence="ECO:0007829|PDB:5YAD"
FT STRAND 914..917
FT /evidence="ECO:0007829|PDB:5YAD"
FT STRAND 924..927
FT /evidence="ECO:0007829|PDB:5YAD"
FT HELIX 929..931
FT /evidence="ECO:0007829|PDB:5YAD"
SQ SEQUENCE 1730 AA; 192064 MW; 5901384B5395F685 CRC64;
MEGKGTENPC SRTLGWFHQD NDAKPWLWKF SGCFSRPEQT LPLSSQTKEY MENKKAAVEL
KDIPSPLHVG SKFFPAVPLP DIRSLQQPKV QLSAIPKVSC CAHCPNEPST SPMRFGGGSG
SSGGSGSLIH TGSLLDSPST GTVTCQVGSG FAFQSVSSLQ NASTRNNLVG LSSDFPSMCV
ESNLPSCKHL SCCGKLHFQS CHSNVHKLHQ FQNLQGCASA GYFPCSDFPS GAPGHLEERL
SHSELTPHLC TNSLHLNVAP PVCLKGSLYC EDCLNKPARN SIIDAAKIWP NIPPPSTQPA
PPAIPVCNGC GTKGMEKETS LLLATSLGKT ASKFGSPEVA VTGQVLETLP PIGVFWDIEN
CSVPSGRSAT TVVQRIREKF FRGHREAEFI CVCDISKENK EVIQELNNCQ VTVAHINATA
KNAADDKLRQ SLRRFANTHT APATVVLVST DVNFALELSD LRHRHGFHII LVHKNQASEA
LLHHANQLIR FEEFISDLPP RLPLKIPQCH TLLYVYNLPA NKDGKSISNR LRRLSDNCGG
KVLSITGCSA ILRFINQDSA ERAQKRMENE DVFGNRIIVS FTPKHREFFE AKSSNAIADK
VKSPKKVKNT KLCLIKDTSE QSPSVKAMPG KVLQANSGSA TKTTNIKSLQ ELCRMESKSG
NRNSDHQQGH GRLAALPNSG PTASVPIVKN TGVTEPLYRS SQKKENPSSQ STVNSPVEKK
KREETVFQVS YPSAFSKLIA SRQVSPLLTS QSWSPRASPL AFNIANPSSG ADCPDPFANG
VDIQVSNVDY RLSRKELQQL LQEAFSKHGQ VKSVELSPHT DYQLKAIVQM RNLHEAICAV
NSLHRHKIGS KKILVSLSTG AANKSLSLLS TETMSILQDA PACCLPLFKF IDIYEKKYGH
KLNVSDLYKL TDTIAIREQG NGRLVCLLPS NQARQSPLGS SQSHDGSSSN CSPVLFEELE
YHEPVCKQHC SNKDFSELVF DPDSYKIPFV VLSLKVFAPQ VHSLLQTHQG TVPLLSFPDC
YAAEFGDLEI TQDSHKGVPL EHFITCIPGV NIATAQNGVK VVKWIHNKPP PPNTDPWLLR
SKSPVRNPQL IQFSREVIDL LKTQPSCILP VSNFIPSYHH HFGKQCRVSD YGYSKLIELL
EAVPHVLQIL GMGSKRLMTL THRAQVKRFT QDLLKLLKSQ ASKQVIVRDF SQAYHWCFSK
DWDVTEYGVC DLIDIISEIP DTTICLSQQD DDMVICIRKR ERTQDEIERT KQFSKDVVDL
LRHQPHFRMP FNKFIPSYHH HFGRQCKLAY YGFTKLLELL EAIPEILQVL ECGEEKILTL
TEVERFKALA AQFVKLLRSQ KGNCLMMTDL FTEYAKTFGY TFRLQDYDVS SVSALTQKLC
HVVKVADMES GKQIQLINRK SLRSLTAQLL VLLMSWEGDA YLPVDELRRH YETTHSTPLN
PCEYGFMTLT ELLKSLPYLV EVCTNDKAEE YVKLTSLYLF AKNVRSLLHT YHYQQIFLHE
FSMAYNKYVG ETLQPKTYGY SSVEELLGAI PQVVWIKGHG HKRIVVLKND MKNRLSSFDL
FSVNHEDQPA VSRQILAVPE SHLASELQLR TGTGPSQMEQ ELLHLASSSP VDLLCAPVPS
CLPSPQLRPD PVILKPADLI QFEEHPQEPL GVLVLNQEEK SEVPLPVQKG NLSCDSSPSS
PAASPAPPGP SSEAPRPLFS KDAVESPAKK QPKNRVKLAA NFSFAPVTKL
