MARF1_HUMAN
ID MARF1_HUMAN Reviewed; 1742 AA.
AC Q9Y4F3; A8MSK2; B2RNX2; B4DYY9; B7ZMG1; B7ZMG2; F8VV09; Q6P1R6; Q8WYR2;
AC Q9Y4J9;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 6.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Meiosis regulator and mRNA stability factor 1 {ECO:0000312|HGNC:HGNC:29562};
DE AltName: Full=Limkain-b1 {ECO:0000303|PubMed:15932519};
DE AltName: Full=Meiosis arrest female protein 1 {ECO:0000305};
GN Name=MARF1 {ECO:0000312|HGNC:HGNC:29562}; Synonyms=KIAA0430, LKAP;
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] (ISOFORMS 1 AND 2), AND SUBCELLULAR LOCATION.
RX PubMed=15932519; DOI=10.1111/j.1365-2249.2005.02774.x;
RA Dunster K., Lai F.P.L., Sentry J.W.;
RT "Limkain b1, a novel human autoantigen localized to a subset of ABCD3 and
RT PXF marked peroxisomes.";
RL Clin. Exp. Immunol. 140:556-563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Testis;
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=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Brain, and 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 237-1742 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [8]
RP SEQUENCE REVISION.
RA Ohara O., Nagase T., Kikuno R.;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 312-615 (ISOFORM 1), AND INTERACTION WITH
RP LIMK2.
RA Miyamoto K., Nakamura T., Shirakawa K., Matsumoto K.;
RT "Molecular cloning and characterization of novel large protein, limkain b1,
RT which associates with the LIM-kinase 2.";
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [10]
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1091, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION OF THE HTH OST-TYPE DOMAIN.
RX PubMed=20305267; DOI=10.1093/bioinformatics/btq122;
RA Callebaut I., Mornon J.P.;
RT "LOTUS, a new domain associated with small RNA pathways in the germline.";
RL Bioinformatics 26:1140-1144(2010).
RN [13]
RP IDENTIFICATION OF THE HTH OST-TYPE DOMAIN.
RX PubMed=20302647; DOI=10.1186/1745-6150-5-13;
RA Anantharaman V., Zhang D., Aravind L.;
RT "OST-HTH: a novel predicted RNA-binding domain.";
RL Biol. Direct 5:13-13(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-760; SER-1093 AND
RP SER-1571, AND 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 STRUCTURE BY NMR OF 789-875.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RNA recognition motif in KIAA0430 protein.";
RL Submitted (SEP-2006) to the PDB data bank.
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LIMK2. {ECO:0000269|Ref.9}.
CC -!- INTERACTION:
CC Q9Y4F3; O15499: GSC2; NbExp=3; IntAct=EBI-5235902, EBI-19954058;
CC Q9Y4F3; Q0VD86: INCA1; NbExp=3; IntAct=EBI-5235902, EBI-6509505;
CC Q9Y4F3; O75381: PEX14; NbExp=3; IntAct=EBI-5235902, EBI-594898;
CC Q9Y4F3; P15884-3: TCF4; NbExp=3; IntAct=EBI-5235902, EBI-13636688;
CC Q9Y4F3; Q05086-3: UBE3A; NbExp=3; IntAct=EBI-5235902, EBI-11026619;
CC Q9Y4F3; P61964: WDR5; NbExp=6; IntAct=EBI-5235902, EBI-540834;
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:15932519}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9Y4F3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4F3-3; Sequence=VSP_022988;
CC Name=3;
CC IsoId=Q9Y4F3-4; Sequence=VSP_037757;
CC Name=4;
CC IsoId=Q9Y4F3-5; Sequence=VSP_037758, VSP_037759;
CC Name=5;
CC IsoId=Q9Y4F3-6; Sequence=VSP_037755, VSP_037756;
CC -!- MISCELLANEOUS: [Isoform 5]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC31662.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAH64914.2; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=EAW53920.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK302667; BAG63901.1; -; mRNA.
DR EMBL; U95740; AAC31662.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC026401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471226; EAW53920.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC064914; AAH64914.2; ALT_SEQ; mRNA.
DR EMBL; BC137165; AAI37166.1; -; mRNA.
DR EMBL; BC137170; AAI37171.1; -; mRNA.
DR EMBL; BC144514; AAI44515.1; -; mRNA.
DR EMBL; BC144515; AAI44516.1; -; mRNA.
DR EMBL; AB007890; BAA24860.3; -; mRNA.
DR EMBL; AB012134; BAB82433.1; -; mRNA.
DR CCDS; CCDS10562.2; -. [Q9Y4F3-1]
DR CCDS; CCDS53990.1; -. [Q9Y4F3-5]
DR CCDS; CCDS55991.1; -. [Q9Y4F3-4]
DR PIR; T00060; T00060.
DR RefSeq; NP_001171927.1; NM_001184998.1. [Q9Y4F3-5]
DR RefSeq; NP_001171928.1; NM_001184999.1. [Q9Y4F3-4]
DR RefSeq; NP_055462.2; NM_014647.3. [Q9Y4F3-1]
DR RefSeq; XP_005255764.1; XM_005255707.1.
DR RefSeq; XP_016879390.1; XM_017023901.1. [Q9Y4F3-5]
DR PDB; 2DGX; NMR; -; A=789-871.
DR PDB; 2DIU; NMR; -; A=510-592.
DR PDB; 6FDL; X-ray; 1.75 A; A/B=352-500.
DR PDBsum; 2DGX; -.
DR PDBsum; 2DIU; -.
DR PDBsum; 6FDL; -.
DR AlphaFoldDB; Q9Y4F3; -.
DR SMR; Q9Y4F3; -.
DR BioGRID; 115020; 109.
DR IntAct; Q9Y4F3; 14.
DR STRING; 9606.ENSP00000379654; -.
DR iPTMnet; Q9Y4F3; -.
DR PhosphoSitePlus; Q9Y4F3; -.
DR BioMuta; MARF1; -.
DR DMDM; 387912929; -.
DR EPD; Q9Y4F3; -.
DR jPOST; Q9Y4F3; -.
DR MassIVE; Q9Y4F3; -.
DR MaxQB; Q9Y4F3; -.
DR PaxDb; Q9Y4F3; -.
DR PeptideAtlas; Q9Y4F3; -.
DR PRIDE; Q9Y4F3; -.
DR ProteomicsDB; 86189; -. [Q9Y4F3-1]
DR ProteomicsDB; 86190; -. [Q9Y4F3-3]
DR ProteomicsDB; 86191; -. [Q9Y4F3-4]
DR ProteomicsDB; 86192; -. [Q9Y4F3-5]
DR ProteomicsDB; 86193; -. [Q9Y4F3-6]
DR Antibodypedia; 3042; 37 antibodies from 14 providers.
DR DNASU; 9665; -.
DR Ensembl; ENST00000396368.8; ENSP00000379654.3; ENSG00000166783.22. [Q9Y4F3-1]
DR Ensembl; ENST00000548025.5; ENSP00000449376.1; ENSG00000166783.22. [Q9Y4F3-4]
DR Ensembl; ENST00000551742.5; ENSP00000450309.1; ENSG00000166783.22. [Q9Y4F3-5]
DR Ensembl; ENST00000621511.2; ENSP00000479383.1; ENSG00000277140.2. [Q9Y4F3-1]
DR Ensembl; ENST00000632465.1; ENSP00000487685.1; ENSG00000277140.2. [Q9Y4F3-4]
DR Ensembl; ENST00000632628.1; ENSP00000488025.1; ENSG00000277140.2. [Q9Y4F3-5]
DR GeneID; 9665; -.
DR KEGG; hsa:9665; -.
DR MANE-Select; ENST00000396368.8; ENSP00000379654.3; NM_014647.4; NP_055462.2.
DR UCSC; uc002ddr.4; human. [Q9Y4F3-1]
DR CTD; 9665; -.
DR DisGeNET; 9665; -.
DR GeneCards; MARF1; -.
DR HGNC; HGNC:29562; MARF1.
DR HPA; ENSG00000166783; Low tissue specificity.
DR MIM; 614593; gene.
DR neXtProt; NX_Q9Y4F3; -.
DR OpenTargets; ENSG00000166783; -.
DR PharmGKB; PA145148631; -.
DR VEuPathDB; HostDB:ENSG00000166783; -.
DR eggNOG; ENOG502QUYZ; Eukaryota.
DR GeneTree; ENSGT00390000002393; -.
DR InParanoid; Q9Y4F3; -.
DR OMA; NNGHIME; -.
DR OrthoDB; 187067at2759; -.
DR PhylomeDB; Q9Y4F3; -.
DR TreeFam; TF329117; -.
DR PathwayCommons; Q9Y4F3; -.
DR SignaLink; Q9Y4F3; -.
DR BioGRID-ORCS; 9665; 17 hits in 1085 CRISPR screens.
DR ChiTaRS; KIAA0430; human.
DR EvolutionaryTrace; Q9Y4F3; -.
DR GeneWiki; KIAA0430; -.
DR GenomeRNAi; 9665; -.
DR Pharos; Q9Y4F3; Tdark.
DR PRO; PR:Q9Y4F3; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9Y4F3; protein.
DR Bgee; ENSG00000166783; Expressed in colonic epithelium and 108 other tissues.
DR ExpressionAtlas; Q9Y4F3; baseline and differential.
DR Genevisible; Q9Y4F3; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005777; C:peroxisome; IDA:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0007143; P:female meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
DR GO; GO:0016441; P:post-transcriptional gene silencing; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; ISS: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; 2.
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..1742
FT /note="Meiosis regulator and mRNA stability factor 1"
FT /id="PRO_0000276846"
FT DOMAIN 353..490
FT /note="NYN"
FT DOMAIN 791..870
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 875..949
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1003..1079
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1099..1173
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1175..1250
FT /note="HTH OST-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1259..1334
FT /note="HTH OST-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1335..1410
FT /note="HTH OST-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1411..1485
FT /note="HTH OST-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1486..1560
FT /note="HTH OST-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT REGION 619..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1677..1726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 699
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ34"
FT MOD_RES 760
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 278..291
FT /note="PARNSIIDAAKVWP -> VRIFLFLKLGAAED (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037755"
FT VAR_SEQ 293..1742
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_037756"
FT VAR_SEQ 336..338
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037757"
FT VAR_SEQ 509
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037758"
FT VAR_SEQ 754
FT /note="W -> WS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_037759"
FT VAR_SEQ 1026..1084
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15932519"
FT /id="VSP_022988"
FT CONFLICT 451
FT /note="T -> A (in Ref. 4; AC026401)"
FT /evidence="ECO:0000305"
FT CONFLICT 941
FT /note="S -> R (in Ref. 7; BAA24860)"
FT /evidence="ECO:0000305"
FT CONFLICT 1541
FT /note="P -> S (in Ref. 6; AAI44516)"
FT /evidence="ECO:0000305"
FT STRAND 352..358
FT /evidence="ECO:0007829|PDB:6FDL"
FT TURN 359..361
FT /evidence="ECO:0007829|PDB:6FDL"
FT HELIX 370..381
FT /evidence="ECO:0007829|PDB:6FDL"
FT STRAND 385..394
FT /evidence="ECO:0007829|PDB:6FDL"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:6FDL"
FT HELIX 401..409
FT /evidence="ECO:0007829|PDB:6FDL"
FT STRAND 413..416
FT /evidence="ECO:0007829|PDB:6FDL"
FT HELIX 424..438
FT /evidence="ECO:0007829|PDB:6FDL"
FT STRAND 445..449
FT /evidence="ECO:0007829|PDB:6FDL"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:6FDL"
FT HELIX 456..464
FT /evidence="ECO:0007829|PDB:6FDL"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:6FDL"
FT HELIX 481..484
FT /evidence="ECO:0007829|PDB:6FDL"
FT STRAND 487..491
FT /evidence="ECO:0007829|PDB:6FDL"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:6FDL"
FT STRAND 510..518
FT /evidence="ECO:0007829|PDB:2DIU"
FT HELIX 525..537
FT /evidence="ECO:0007829|PDB:2DIU"
FT TURN 538..540
FT /evidence="ECO:0007829|PDB:2DIU"
FT STRAND 543..545
FT /evidence="ECO:0007829|PDB:2DIU"
FT STRAND 551..557
FT /evidence="ECO:0007829|PDB:2DIU"
FT HELIX 558..568
FT /evidence="ECO:0007829|PDB:2DIU"
FT STRAND 573..576
FT /evidence="ECO:0007829|PDB:2DIU"
FT STRAND 579..583
FT /evidence="ECO:0007829|PDB:2DIU"
FT STRAND 791..797
FT /evidence="ECO:0007829|PDB:2DGX"
FT HELIX 804..818
FT /evidence="ECO:0007829|PDB:2DGX"
FT STRAND 821..826
FT /evidence="ECO:0007829|PDB:2DGX"
FT STRAND 836..842
FT /evidence="ECO:0007829|PDB:2DGX"
FT HELIX 843..853
FT /evidence="ECO:0007829|PDB:2DGX"
FT STRAND 856..858
FT /evidence="ECO:0007829|PDB:2DGX"
FT STRAND 861..867
FT /evidence="ECO:0007829|PDB:2DGX"
SQ SEQUENCE 1742 AA; 192859 MW; 9A0C0687B93A6A4B CRC64;
MMEGNGTENS CSRTRGWLQQ DNDAKPWLWK FSNCFSRPEQ TLPHSPQTKE YMENKKVAVE
LKDVPSPLHA GSKLFPAVPL PDIRSLQQPK IQLSSVPKVS CCAHCPNEPS TSPMRFGGGG
GGSGGTSSLI HPGALLDSQS TRTITCQVGS GFAFQSASSL QNASARNNLA GIASDFPSMC
LESNLSSCKH LPCCGKLHFQ SCHGNVHKLH QFPSLQGCTS AGYFPCSDFT SGAPGHLEEH
ISQSELTPHL CTNSLHLNVV PPVCLKGSLY CEDCLNKPAR NSIIDAAKVW PNIPPPNTQP
APLAVPLCNG CGTKGTGKET TLLLATSLGK AASKFGSPEV AVAGQVLENL PPIGVFWDIE
NCSVPSGRSA TAVVQRIREK FFKGHREAEF ICVCDISKEN KEVIQELNNC QVTVAHINAT
AKNAADDKLR QSLRRFANTH TAPATVVLVS TDVNFALELS DLRHRHGFHI ILVHKNQASE
ALLHHANELI RFEEFISDLP PRLPLKMPQC HTLLYVYNLP ANKDGKSVSN RLRRLSDNCG
GKVLSITGCS AILRFINQDS AERAQKRMEN EDVFGNRIIV SFTPKNRELC ETKSSNAIAD
KVKSPKKLKN PKLCLIKDAS EQSSSAKATP GKGSQANSGS ATKNTNVKSL QELCRMESKT
GHRNSEHQQG HLRLVVPTHG NSSAAVSTPK NSGVAEPVYK TSQKKENLSA RSVTSSPVEK
KDKEETVFQV SYPSAFSKLV ASRQVSPLLA SQSWSSRSMS PNLLNRASPL AFNIANSSSE
ADCPDPFANG ADVQVSNIDY RLSRKELQQL LQEAFARHGK VKSVELSPHT DYQLKAVVQM
ENLQDAIGAV NSLHRYKIGS KKILVSLATG AASKSLSLLS AETMSVLQDA PACCLPLFKF
TDIYEKKFGH KLNVSDLYKL TDTVAIREQG NGRLVCLLPS SQARQSPLGS SQSHDGSSTN
CSPIIFEELE YHEPVCRQHC SNKDFSEHEF DPDSYKIPFV ILSLKTFAPQ VHSLLQTHEG
TVPLLSFPDC YIAEFGDLEV VQENQGGVPL EHFITCVPGV NIATAQNGIK VVKWIHNKPP
PPNTDPWLLR SKSPVGNPQL IQFSREVIDL LKSQPSCVIP ISHFIPSYHH HFAKQCRVSD
YGYSKLIELL EAVPHVLQIL GMGSKRLLTL THRAQVKRFT QDLLKLLKSQ ASKQVIVREF
SQAYHWCFSK DWDVTEYGVC ELIDIVSEIP DTTICLSQQD NEMVICIPKR ERTQDEIERT
KQFSKDVVDL LRHQPHFRMP FNKFIPSYHH HFGRQCKLAY YGFTKLLELF EAIPDTLQVL
ECGEEKILTL TEVERFKALA AQFVKLLRSQ KDNCLMMTDL LTEYAKTFGY TFRLQDYDVS
SISALTQKLC HVVKVADIES GRQIQLINRK SLRSLTAQLL VLLMSWEGTT HLSVEELKRH
YESTHNTPLN PCEYGFMTLT ELLKSLPYLV EVFTNDKMEE CVKLTSLYLF AKNVRSLLHT
YHYQQIFLHE FSMAYTKYVG ETLQPKTYGH SSVEELLGAI PQVVWIKGHG HKRIVVLKND
MKSRLSSLSL SPANHENQPS EGERILEVPE SHTASELKLG ADGSGPSHTE QELLRLTDDS
PVDLLCAPVP SCLPSPQLRP DPVILQSADL IQFEERPQEP SEIMILNQEE KMEIPIPGKS
KTLTSDSSSS CISAAVPVPP CPSSETSESL LSKDPVESPA KKQPKNRVKL AANFSLAPIT
KL
