ID MARF1_BOVIN Reviewed; 1742 AA.
AC E1BP74;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Meiosis regulator and mRNA stability factor 1 {ECO:0000250|UniProtKB:Q9Y4F3};
DE AltName: Full=Limkain-b1 {ECO:0000250|UniProtKB:Q9Y4F3};
DE AltName: Full=Meiosis arrest female protein 1 {ECO:0000250|UniProtKB:Q9Y4F3};
GN Name=MARF1 {ECO:0000250|UniProtKB:Q9Y4F3}; Synonyms=LKAP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford;
RX PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT "A whole-genome assembly of the domestic cow, Bos taurus.";
RL Genome Biol. 10:R42.01-R42.10(2009).
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:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
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DR EMBL; DAAA02057550; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E1BP74; -.
DR SMR; E1BP74; -.
DR STRING; 9913.ENSBTAP00000027175; -.
DR PaxDb; 9913-ENSBTAP00000027175; -.
DR eggNOG; ENOG502QUYZ; Eukaryota.
DR HOGENOM; CLU_002701_0_0_1; -.
DR InParanoid; E1BP74; -.
DR TreeFam; TF329117; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:1905762; F:CCR4-NOT complex binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR GO; GO:0007143; P:female meiotic nuclear division; ISS:UniProtKB.
DR GO; GO:0048477; P:oogenesis; ISS:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; ISS:UniProtKB.
DR CDD; cd09977; LOTUS_1_Limkain_b1; 1.
DR CDD; cd09978; LOTUS_2_Limkain_b1; 1.
DR CDD; cd09979; LOTUS_3_Limkain_b1; 1.
DR CDD; cd09980; LOTUS_4_Limkain_b1; 1.
DR CDD; cd09981; LOTUS_5_Limkain_b1; 1.
DR CDD; cd09982; LOTUS_6_Limkain_b1; 1.
DR CDD; cd09983; LOTUS_7_Limkain_b1; 1.
DR CDD; cd09984; LOTUS_8_Limkain_b1; 1.
DR CDD; cd10910; PIN_limkain_b1_N_like; 1.
DR CDD; cd12255; RRM1_LKAP; 1.
DR CDD; cd12256; RRM2_LKAP; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR Gene3D; 3.30.420.610; LOTUS domain-like; 6.
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.
DR InterPro; IPR025605; OST-HTH/LOTUS_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR14379; LIMKAIN B LKAP; 1.
DR PANTHER; PTHR14379:SF82; MEIOSIS REGULATOR AND MRNA STABILITY FACTOR 1; 1.
DR Pfam; PF19687; MARF1_LOTUS; 1.
DR Pfam; PF11608; MARF1_RRM1; 1.
DR Pfam; PF01936; NYN; 1.
DR Pfam; PF12872; OST-HTH; 5.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS51644; HTH_OST; 8.
DR PROSITE; PS50102; RRM; 2.
PE 3: Inferred from homology;
KW Differentiation; Meiosis; Oogenesis; Peroxisome; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..1742
FT /note="Meiosis regulator and mRNA stability factor 1"
FT /id="PRO_0000417527"
FT DOMAIN 351..488
FT /note="NYN"
FT DOMAIN 788..867
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 872..946
FT /note="HTH OST-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1000..1077
FT /note="HTH OST-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1097..1171
FT /note="HTH OST-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1173..1247
FT /note="HTH OST-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1257..1332
FT /note="HTH OST-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1333..1408
FT /note="HTH OST-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00975"
FT DOMAIN 1409..1484
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 620..642
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 655..721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 624..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1704
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F3"
FT MOD_RES 696
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ34"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F3"
FT MOD_RES 1089
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F3"
FT MOD_RES 1091
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F3"
FT MOD_RES 1571
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4F3"
SQ SEQUENCE 1742 AA; 192127 MW; 4D77DE9984098AE4 CRC64;
MEGSGTENPC STTVGWLQQD NDAKPWLWRF SNCFSRPQQT LPLSPQTKDY MENKKVAVEL
KDVPSPLHAG SKLFPAVPLP DIHSLQQPKV QLSTVPKVSC CAHCTNDPST SPVRFGGGSG
GGAGSLVPPG ALLDSQSTRT ITCQVGSGLA FQSAPPLQNA SARNTLAGVA SDFPSMCLES
NLSSCKHLPC CGKLHFQSCR GNVHKLHQFP ALQGCPSSAG YFPCSDFTSG APGHVEEHVS
QSELTPHLCT NSLHLNVVPP VCLKGSLYCE DCLSKPARNS IIDAAKVWPN IPPPNTQTAP
VTVPLCNGCG TKGMGKETTL LLATSLGKAA SKFGSPEVAL AGQMLENLPP IGVFWDIENC
SVPSGRSATA VVQRIREKFF KGHREAEFIC VCDISKENKE VIQELNNCQV TVAHINATAK
NAADDKLRQS LRRFANTHTA PATVVLVSTD VNFALELSDL RHRHGFHIIL VHKNQASEAL
LHHANELIRF EEFISDLPPR LPLKMPCHTL LYVYNLPANK DGKSISNRLR RLSDNCGGKV
LNITGCSAIL RFINRDSAER ALKRMENEDV FGNRIVVSFT PKSSELCETK SSNATADKVK
SPKKLKNPKL CLIKDISESP SSAKAAPGKG SQANSGSATR NANVKSLQEL CRLESKTGTR
SSEPQQGHLR LGAPPHRSSS AAAPAPKAPG LAESVYKTNP KKESLGARSV TSSPVEKKEK
EETLFQVSYP SAFSKLIASR QVSPLLTAQP WSSRNLSPNL LNRASPLAFN AAHSSVGADG
PDPFAHGVDV QISNLDYRLS RKELQQLMQE AFSRHGKVKS VELSPHTDYQ LKAVVQMENL
QEAIGAVNSL HRYKIGSKKI LVSLATGAAN KSLSLLSAET MSILQDAPAC CLPLFKFTDI
YEKKFGHRLN VSDLYKLTDT VAIREQGNGR LVCLLPSSQA RQSPLGSSQS HDGSSTNCSP
IIFEELEYHE PVCRQHCPNK DFSEHEFDPD SYKIPFVILS LKTFAPQVHS LLQTHEGTVP
LLSFPDCYAA EFGELEIVQE NRGGGVPLEH LITCVPGVNI ATAQNGVKVV KWIHNKPPPP
NTDPWLLRSK SPVGNPQLIQ FSREVIDLLK NQPSCVIPIS NFIPSYHHHF AKQCRVSDYG
YSKLIELLEA VPHVLQILGM GSKRLLTLTH RAQVKRFTQD LLKLLKSQAS KQVIVKEFAQ
AYHWCFSKDW DVTEYGVCEL IDIISEIPDT TICLSQQDSE AMICIPRRER TQDEIERTKQ
FSKDVVDLLR HQPHFRMPFN KFIPSYHHHF GRQCKLAYYG FTKLLELFEA IPDILQVLEC
GEEKILTLTE VERFKALAAQ FVKLLRSQKD NCLMMTDLLK EYAKTFGYTF RLQDYDVSSV
SALTQKLCHV VKVADMESGK QIQLINRKSL RALTAQLLVL LMSWEGTTHL SVDELKRHYE
STHSTPLNPC EYGFMTLTEL LKSLPYLVED QVFTNDKTEE CVKLTSLYLF AKNVRSLLHT
YHYQQLFLHE FSMAYSKYVG ETLQPKTYGF SSVEELLGAI PQVVWIKGHG HKRIVVLKND
MKSRVNSLGP SPASHETQPS APERILEVPE SPPASELRLG VGGDGPHPAE QELLRLTDDS
PVDLLCAPVP SCLPSPQLRP DPVVLQAADL IWFEEHPQEP SEIMILNQEE KIEIPVPIRN
ENLPPDPSSP GVSAAVPAPP SPSSETPESL LSKDPTESPA KKQPKNRVKL AANFSFAPIT
KL
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