MAJIN_MOUSE
ID MAJIN_MOUSE Reviewed; 256 AA.
AC Q9D992; E9Q4N4;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2016, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Membrane-anchored junction protein {ECO:0000303|PubMed:26548954};
GN Name=Majin {ECO:0000303|PubMed:26548954};
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).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, IDENTIFICATION BY MASS
RP SPECTROMETRY, IDENTIFICATION IN THE MAJIN-TERB1-TERB2 COMPLEX, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF 140-ARG--LYS-145.
RX PubMed=26548954; DOI=10.1016/j.cell.2015.10.030;
RA Shibuya H., Hernandez-Hernandez A., Morimoto A., Negishi L., Hoeoeg C.,
RA Watanabe Y.;
RT "MAJIN links telomeric DNA to the nuclear membrane by exchanging telomere
RT cap.";
RL Cell 163:1252-1266(2015).
CC -!- FUNCTION: Meiosis-specific telomere-associated protein involved in
CC meiotic telomere attachment to the nucleus inner membrane, a crucial
CC step for homologous pairing and synapsis. Component of the MAJIN-TERB1-
CC TERB2 complex, which promotes telomere cap exchange by mediating
CC attachment of telomeric DNA to the inner nuclear membrane and
CC replacement of the protective cap of telomeric chromosomes: in early
CC meiosis, the MAJIN-TERB1-TERB2 complex associates with telomeric DNA
CC and the shelterin/telosome complex. During prophase, the complex
CC matures and promotes release of the shelterin/telosome complex from
CC telomeric DNA. In the complex, MAJIN acts as the anchoring subunit to
CC the nucleus inner membrane. MAJIN shows DNA-binding activity, possibly
CC for the stabilization of telomere attachment on the nucleus inner
CC membrane. {ECO:0000269|PubMed:26548954}.
CC -!- SUBUNIT: Component of the MAJIN-TERB1-TERB2 complex, composed of MAJIN,
CC TERB1 and TERB2. {ECO:0000269|PubMed:26548954}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000269|PubMed:26548954}; Single-pass membrane protein
CC {ECO:0000305|PubMed:26548954}. Chromosome, telomere
CC {ECO:0000269|PubMed:26548954}. Note=Localizes to telomeres throughout
CC meiotic prophase I and disappears in metaphase I. In leptotene
CC spermatocytes, localizes to telomeres that localize to the nucleus
CC inner membrane. {ECO:0000269|PubMed:26548954}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9D992-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9D992-2; Sequence=VSP_058064;
CC -!- TISSUE SPECIFICITY: Specifically expressed in germline tissues.
CC {ECO:0000269|PubMed:26548954}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally, exhibit no overt
CC phenotype, but are infertile (both males and females). Gonads are
CC characterized by the absence of post-meiotic cells. Impaired
CC localization of Terb1 and Terb2 to the nucleus inner membrane.
CC {ECO:0000269|PubMed:26548954}.
CC -!- MISCELLANEOUS: MAJIN was named after the 'genie in Aladdin's lamp' in
CC Japanese. {ECO:0000303|PubMed:26548954}.
CC -!- SIMILARITY: Belongs to the MAJIN family. {ECO:0000305}.
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DR EMBL; AK007250; BAB24915.1; -; mRNA.
DR EMBL; AC127556; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50364.1; -. [Q9D992-1]
DR RefSeq; NP_001159391.1; NM_001165919.1. [Q9D992-1]
DR RefSeq; XP_006531883.1; XM_006531820.2.
DR AlphaFoldDB; Q9D992; -.
DR SMR; Q9D992; -.
DR STRING; 10090.ENSMUSP00000109156; -.
DR iPTMnet; Q9D992; -.
DR PhosphoSitePlus; Q9D992; -.
DR PaxDb; Q9D992; -.
DR PRIDE; Q9D992; -.
DR ProteomicsDB; 292004; -. [Q9D992-1]
DR ProteomicsDB; 292005; -. [Q9D992-2]
DR Antibodypedia; 52613; 44 antibodies from 13 providers.
DR Ensembl; ENSMUST00000025699; ENSMUSP00000025699; ENSMUSG00000024786. [Q9D992-2]
DR Ensembl; ENSMUST00000113528; ENSMUSP00000109156; ENSMUSG00000024786. [Q9D992-1]
DR GeneID; 622554; -.
DR KEGG; mmu:622554; -.
DR UCSC; uc008ghr.2; mouse. [Q9D992-1]
DR UCSC; uc012bhj.1; mouse.
DR CTD; 283129; -.
DR MGI; MGI:1923913; Majin.
DR VEuPathDB; HostDB:ENSMUSG00000024786; -.
DR eggNOG; ENOG502S50S; Eukaryota.
DR GeneTree; ENSGT00390000007971; -.
DR HOGENOM; CLU_094252_1_1_1; -.
DR InParanoid; Q9D992; -.
DR OMA; HLKFKHE; -.
DR OrthoDB; 1129208at2759; -.
DR TreeFam; TF336863; -.
DR BioGRID-ORCS; 622554; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Majin; mouse.
DR PRO; PR:Q9D992; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9D992; protein.
DR Bgee; ENSMUSG00000024786; Expressed in spermatocyte and 19 other tissues.
DR Genevisible; Q9D992; MM.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:UniProtKB.
DR GO; GO:0070197; P:meiotic attachment of telomere to nuclear envelope; IMP:UniProtKB.
DR GO; GO:0045141; P:meiotic telomere clustering; IMP:UniProtKB.
DR InterPro; IPR027816; MAJIN.
DR PANTHER; PTHR35824; PTHR35824; 1.
DR Pfam; PF15077; MAJIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; DNA-binding; Meiosis; Membrane; Nucleus;
KW Reference proteome; Telomere; Transmembrane; Transmembrane helix.
FT CHAIN 1..256
FT /note="Membrane-anchored junction protein"
FT /id="PRO_0000325833"
FT TOPO_DOM 1..232
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 233..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 252..256
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT REGION 143..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..188
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 50..181
FT /note="Missing (in isoform 2)"
FT /id="VSP_058064"
FT MUTAGEN 140..145
FT /note="RKWKRK->AAWAAA: Impaired DNA-binding activity."
FT /evidence="ECO:0000269|PubMed:26548954"
SQ SEQUENCE 256 AA; 29175 MW; 7980FEB7DB388088 CRC64;
MSLKPFTYPF PETRFLHAGP NVYKFKIRYG NSIRGEEIED KEVIVQELED SIRAVLANMD
SLQPFVTEHF IVFPYKSKWE RVSHLKFKHG ESILTPYPFV FTLYIEMKWF AEDLPSGKPA
DDIPLELVLA ETEAEEATMR KWKRKLMEEP SSPSRQGPHR AKMETSSEAS SNKKPLKESK
RSTDEEAQQE YQDTPASNAI AVKEQDAALG HGLQGLVVPP LQHSSPPPPK EPGARGFLGF
LSALFPFRYF FKKSGQ
