MOR2B_MOUSE
ID MOR2B_MOUSE Reviewed; 1022 AA.
AC Q8C5W4; B8JK02; Q8CG24;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=ATPase MORC2B {ECO:0000305};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:Q9Y6X9};
DE AltName: Full=MORC family CW-type zinc finger protein 2B {ECO:0000305};
DE AltName: Full=TCE6;
GN Name=Morc2b {ECO:0000312|MGI:MGI:3045293};
GN Synonyms=Tce6 {ECO:0000312|EMBL:AAO17388.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAC36567.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC36567.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC36567.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAO17388.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=129/Sv {ECO:0000312|EMBL:AAO17388.1};
RX PubMed=15112104; DOI=10.1007/s00335-003-2329-1;
RA Abe K., Yuzuriha M., Sugimoto M., Ko M.S., Brathwaite M.E., Waeltz P.,
RA Nagaraja R.;
RT "Gene content of the 750-kb critical region for mouse embryonic ectoderm
RT lethal tcl-w5.";
RL Mamm. Genome 15:265-276(2004).
RN [3]
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 [4]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH MORC2A, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=29329290; DOI=10.1371/journal.pgen.1007175;
RA Shi B., Xue J., Zhou J., Kasowitz S.D., Zhang Y., Liang G., Guan Y.,
RA Shi Q., Liu M., Sha J., Huang X., Wang P.J.;
RT "MORC2B is essential for meiotic progression and fertility.";
RL PLoS Genet. 14:E1007175-E1007175(2018).
CC -!- FUNCTION: Required for chromosomal synapsis and meiotic recombination
CC in males and females. {ECO:0000269|PubMed:29329290}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9Y6X9};
CC -!- SUBUNIT: Interacts with Morc2a. {ECO:0000269|PubMed:29329290}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29329290}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:16141072};
CC IsoId=Q8C5W4-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15112104};
CC IsoId=Q8C5W4-2; Sequence=VSP_052135;
CC -!- TISSUE SPECIFICITY: Protein is abundant in testes but not detected in
CC other adult tissues examined (at protein level). Detected in germ cells
CC with a distinct developmental-specific expression pattern but not in
CC somatic cells such as Sertoli cells. {ECO:0000269|PubMed:29329290}.
CC -!- DEVELOPMENTAL STAGE: In juvenile testes, expression is absent prior to
CC postnatal day 12, is detected at a low level at day 12, and increased
CC significantly at day 14 and beyond. In adul testes, expressed in
CC meiotic spermatocytes, abundant in post-meiotic haploid round
CC spermatids, and absent from elongated spermatids.
CC {ECO:0000269|PubMed:29329290}.
CC -!- DISRUPTION PHENOTYPE: Knockouts are viable and appear to be grossly
CC normal. Mutant males and females show meiotic arrest and sterility.
CC Males have significantly smaller testes than control males. Their
CC testes weigh approximately 70% less than control testes. Their
CC spermatocytes and oocytes exhibit failures in chromosomal synapsis,
CC blockades in meiotic recombination, and increased apoptosis
CC (PubMed:29329290). The ovaries of adult female mutant mice are much
CC smaller than those from heterozygous littermates and are devoid of
CC oocytes (PubMed:29329290). {ECO:0000269|PubMed:29329290}.
CC -!- MISCELLANEOUS: Retrotransposed homolog of Morc2a.
CC {ECO:0000269|PubMed:29329290}.
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DR EMBL; AK077016; BAC36567.1; -; mRNA.
DR EMBL; AF528164; AAO17388.1; -; Genomic_DNA.
DR EMBL; CT033756; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS37561.1; -. [Q8C5W4-1]
DR RefSeq; NP_808387.2; NM_177719.4. [Q8C5W4-1]
DR RefSeq; XP_006524320.1; XM_006524257.2. [Q8C5W4-1]
DR RefSeq; XP_006524321.1; XM_006524258.2. [Q8C5W4-1]
DR RefSeq; XP_006524322.1; XM_006524259.2.
DR RefSeq; XP_011244746.1; XM_011246444.1. [Q8C5W4-1]
DR AlphaFoldDB; Q8C5W4; -.
DR SMR; Q8C5W4; -.
DR IntAct; Q8C5W4; 1.
DR STRING; 10090.ENSMUSP00000123354; -.
DR iPTMnet; Q8C5W4; -.
DR PhosphoSitePlus; Q8C5W4; -.
DR PaxDb; Q8C5W4; -.
DR PRIDE; Q8C5W4; -.
DR ProteomicsDB; 291479; -. [Q8C5W4-1]
DR ProteomicsDB; 291480; -. [Q8C5W4-2]
DR Ensembl; ENSMUST00000053896; ENSMUSP00000056879; ENSMUSG00000048602. [Q8C5W4-1]
DR Ensembl; ENSMUST00000131954; ENSMUSP00000123354; ENSMUSG00000048602. [Q8C5W4-1]
DR GeneID; 240069; -.
DR KEGG; mmu:240069; -.
DR UCSC; uc008byc.2; mouse. [Q8C5W4-1]
DR CTD; 240069; -.
DR MGI; MGI:3045293; Morc2b.
DR VEuPathDB; HostDB:ENSMUSG00000048602; -.
DR eggNOG; KOG1845; Eukaryota.
DR GeneTree; ENSGT00940000153998; -.
DR HOGENOM; CLU_011516_0_0_1; -.
DR InParanoid; Q8C5W4; -.
DR OMA; DNARDAH; -.
DR OrthoDB; 193855at2759; -.
DR PhylomeDB; Q8C5W4; -.
DR TreeFam; TF329118; -.
DR BioGRID-ORCS; 240069; 2 hits in 73 CRISPR screens.
DR PRO; PR:Q8C5W4; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8C5W4; protein.
DR Bgee; ENSMUSG00000048602; Expressed in spermatocyte and 28 other tissues.
DR Genevisible; Q8C5W4; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000792; C:heterochromatin; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IMP:UniProtKB.
DR GO; GO:0005524; F:ATP binding; ISO:MGI.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0000287; F:magnesium ion binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IMP:UniProtKB.
DR GO; GO:0007276; P:gamete generation; IMP:UniProtKB.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; ISO:MGI.
DR GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; ISO:MGI.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR041006; Morc_S5.
DR InterPro; IPR011124; Znf_CW.
DR Pfam; PF17942; Morc6_S5; 1.
DR Pfam; PF07496; zf-CW; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Coiled coil; Hydrolase;
KW Isopeptide bond; Magnesium; Metal-binding; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT CHAIN 2..1022
FT /note="ATPase MORC2B"
FT /id="PRO_0000248244"
FT ZN_FING 490..544
FT /note="CW-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT COILED 285..362
FT /evidence="ECO:0000255"
FT COILED 555..583
FT /evidence="ECO:0000255"
FT COILED 962..1001
FT /evidence="ECO:0000255"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT BINDING 39
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT BINDING 87..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT BINDING 99..105
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT BINDING 427
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT BINDING 499
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 525
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT BINDING 536
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00454"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT MOD_RES 615
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT MOD_RES 690
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT MOD_RES 733
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX6"
FT MOD_RES 737
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX6"
FT MOD_RES 768
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX6"
FT MOD_RES 770
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT MOD_RES 827
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX6"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX6"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZX6"
FT CROSSLNK 649
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT CROSSLNK 758
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT CROSSLNK 922
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6X9"
FT VAR_SEQ 812..835
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15112104"
FT /id="VSP_052135"
FT CONFLICT 521
FT /note="I -> V (in Ref. 2; AAO17388)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="L -> P (in Ref. 2; AAO17388)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="K -> E (in Ref. 1; BAC36567)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="Q -> R (in Ref. 1; BAC36567)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1022 AA; 117186 MW; 6AFABF5964A1B8A0 CRC64;
MAFTNYSTLN RAQLTFDYLH TNSTTHAFLF GALAELIDNA RDADATRIDI YAEKREDLQG
GFMLCFLDNG VGMDPNDVIN VIQFGKSAKR TPESTQIGRY GNGLKSGSMR IGKDFILFTK
KENTMSCLFL SRTFHEEEGI DEVIVPLPTW NSQTREPVTD NMEKFAIETE LIYKYSPFHT
EEEVMTQFTK ISGTSGTLVV IFNLKLTDNG EPELDVTSNP KDIRMAEISQ EGVKPERHSF
CAYAAVLYID PRMRIFIHGH KVQTKKLCCC LYKPRKYTFT SHRFKTRAEQ EVKKADQVAQ
LAEEKAREAE SKARTLEIHM GGDITRDSRV MLRQVQNTAI TLRREADVKK RIRDAKQQAL
KEPKELTFVF GVNIEHRDHD GMFIYNCSRL IKMYEKVGPQ LEKGMVCGGV VGVIDVPYLV
LEPTHNKQDF ADAKEYRHLL RAMGEHLAQY WKDIEIAQHG IIKFWDEFGY LSANWNRPPS
DELHFKRKRA MQVPTTIQCD LCLKWRTLPF QLSAVEEGYP INWVCSMNPD PEQDQCEAFE
LKQKIPLGIL KKAPKTQEER QKQLTEKIQQ EQRKLKALKK IKPIHSQSDL KKLPLEVTSR
PFSKYPAHIF QGPQSSFHVV KTNARRRPQS RHAPFRQLQR SSIICTNPKP PFLVDKTEAV
LLQPPETPQK SVSLLVKTIP QPPPLVQSLS PSVVPKSNNP WKVETPQIMN TPVAEMPYVP
VNPSLVICDH KRSPEVSDEI EDEDRRKRMC KRGRFTVKKE KIQASELSDS SGEENPVDLK
TAQKDKGLYV EVRMMGECYK GHVTAVEVGD NVVWWKVKFE DMPKDSTPRD CWVEKGSENV
WLVKPSPEYQ STDEQQEDRK GEEDTVVQQA LALQQTSTSE CFCTEPDTTA STANHKTIDL
LVQILWNCLH YFMPLSFPIS KKELGAMNSE ELLSLPLKEC FKQYEVGLQN LCRSYQRCAD
SQAKVSEESL RISQKKLQET EEKLQKLRTN IQTLLQMAQQ GINIRADDEL DAYIEDLVSS
DD
