MAJIN_RAT
ID MAJIN_RAT Reviewed; 251 AA.
AC Q6AYM7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Membrane-anchored junction protein {ECO:0000250|UniProtKB:Q9D992};
GN Name=Majin {ECO:0000250|UniProtKB:Q9D992};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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).
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:0000250|UniProtKB:Q9D992}.
CC -!- SUBUNIT: Component of the MAJIN-TERB1-TERB2 complex, composed of MAJIN,
CC TERB1 and TERB2. {ECO:0000250|UniProtKB:Q9D992}.
CC -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC {ECO:0000250|UniProtKB:Q9D992}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9D992}. Chromosome, telomere
CC {ECO:0000250|UniProtKB:Q9D992}. Note=In leptotene spermatocytes,
CC localizes to telomeres that localize to the nucleus inner membrane.
CC {ECO:0000250|UniProtKB:Q9D992}.
CC -!- SIMILARITY: Belongs to the MAJIN family. {ECO:0000305}.
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DR EMBL; BC078985; AAH78985.1; -; mRNA.
DR RefSeq; NP_001019462.1; NM_001024291.1.
DR AlphaFoldDB; Q6AYM7; -.
DR SMR; Q6AYM7; -.
DR STRING; 10116.ENSRNOP00000065294; -.
DR PaxDb; Q6AYM7; -.
DR Ensembl; ENSRNOT00000077274; ENSRNOP00000072946; ENSRNOG00000054336.
DR GeneID; 499306; -.
DR KEGG; rno:499306; -.
DR UCSC; RGD:1563886; rat.
DR CTD; 283129; -.
DR RGD; 1563886; Majin.
DR eggNOG; ENOG502S50S; Eukaryota.
DR GeneTree; ENSGT00390000007971; -.
DR HOGENOM; CLU_094252_1_0_1; -.
DR InParanoid; Q6AYM7; -.
DR OMA; HLKFKHE; -.
DR OrthoDB; 1129208at2759; -.
DR PhylomeDB; Q6AYM7; -.
DR TreeFam; TF336863; -.
DR PRO; PR:Q6AYM7; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000054336; Expressed in testis and 2 other tissues.
DR GO; GO:0000781; C:chromosome, telomeric region; ISS:UniProtKB.
DR GO; GO:0005639; C:integral component of nuclear inner membrane; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; ISS:UniProtKB.
DR GO; GO:0070197; P:meiotic attachment of telomere to nuclear envelope; ISS:UniProtKB.
DR GO; GO:0045141; P:meiotic telomere clustering; ISS:UniProtKB.
DR InterPro; IPR027816; MAJIN.
DR PANTHER; PTHR35824; PTHR35824; 1.
DR Pfam; PF15077; MAJIN; 1.
PE 2: Evidence at transcript level;
KW Chromosome; DNA-binding; Meiosis; Membrane; Nucleus; Reference proteome;
KW Telomere; Transmembrane; Transmembrane helix.
FT CHAIN 1..251
FT /note="Membrane-anchored junction protein"
FT /id="PRO_0000325834"
FT TOPO_DOM 1..227
FT /note="Nuclear"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..251
FT /note="Perinuclear space"
FT /evidence="ECO:0000305"
FT REGION 140..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 251 AA; 28646 MW; CAA3B87C573C4C93 CRC64;
MSLKPFTYPF PETRFLHAGT NVYKFKIRYG NSIRGEEIED KGVIIQELED SIRAVLANMD
SLQPFVTEHF IVFPYKSKWE RVSHLKFKHG EIILTPYPFV FTLYIEMKCF AESLPSGKPT
DDIPLELVLT AKEAEEATMR KRKLMEEPST PSRPGPHRAK METWSEASST KKALKEHKRS
WGEDSQQDTP ASDSTAVTEQ DPMLGHSLPG LVVPPLEHSN PPPLKEPAAR GFLGFLSALF
PFRYFFRKST Q