ID   MNS1_RAT                Reviewed;         498 AA.
AC   Q6AXQ8;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Meiosis-specific nuclear structural protein 1;
GN   Name=Mns1;
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: May play a role in the control of meiotic division and germ
CC       cell differentiation through regulation of pairing and recombination
CC       during meiosis (By similarity). Required for sperm flagella assembly
CC       (By similarity). May play a role in the assembly and function of the
CC       outer dynein arm-docking complex (ODA-DC). ODA-DC mediates outer dynein
CC       arms (ODA) binding onto the axonemal doublet microtubules (By
CC       similarity). {ECO:0000250|UniProtKB:Q61884,
CC       ECO:0000250|UniProtKB:Q8NEH6}.
CC   -!- SUBUNIT: Able to form oligomers (By similarity). Interacts with ODAD1
CC       (By similarity). {ECO:0000250|UniProtKB:Q61884,
CC       ECO:0000250|UniProtKB:Q8NEH6}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q61884}.
CC       Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q2KIQ2}.
CC       Cytoplasm, cytoskeleton, flagellum axoneme
CC       {ECO:0000250|UniProtKB:Q8NEH6}. Note=Microtubule inner protein (MIP)
CC       part of the dynein-decorated doublet microtubules (DMTs) in cilia
CC       axoneme. {ECO:0000250|UniProtKB:Q2KIQ2}.
CC   -!- SIMILARITY: Belongs to the MNS1 family. {ECO:0000305}.
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DR   EMBL; BC079390; AAH79390.1; -; mRNA.
DR   RefSeq; NP_001007753.1; NM_001007752.1.
DR   AlphaFoldDB; Q6AXQ8; -.
DR   SMR; Q6AXQ8; -.
DR   BioGRID; 263961; 1.
DR   STRING; 10116.ENSRNOP00000007941; -.
DR   PhosphoSitePlus; Q6AXQ8; -.
DR   PaxDb; Q6AXQ8; -.
DR   PRIDE; Q6AXQ8; -.
DR   Ensembl; ENSRNOT00000077613; ENSRNOP00000069371; ENSRNOG00000057867.
DR   GeneID; 363093; -.
DR   KEGG; rno:363093; -.
DR   UCSC; RGD:1549718; rat.
DR   CTD; 55329; -.
DR   RGD; 1549718; Mns1.
DR   eggNOG; ENOG502QS9D; Eukaryota.
DR   GeneTree; ENSGT00730000111210; -.
DR   HOGENOM; CLU_034848_0_0_1; -.
DR   InParanoid; Q6AXQ8; -.
DR   OMA; EHKRFLR; -.
DR   OrthoDB; 962490at2759; -.
DR   PhylomeDB; Q6AXQ8; -.
DR   TreeFam; TF329219; -.
DR   PRO; PR:Q6AXQ8; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000057867; Expressed in testis and 19 other tissues.
DR   Genevisible; Q6AXQ8; RN.
DR   GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR   GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR   GO; GO:0005882; C:intermediate filament; ISO:RGD.
DR   GO; GO:0031514; C:motile cilium; IBA:GO_Central.
DR   GO; GO:0005635; C:nuclear envelope; ISO:RGD.
DR   GO; GO:0036126; C:sperm flagellum; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0044782; P:cilium organization; ISO:RGD.
DR   GO; GO:0070986; P:left/right axis specification; ISO:RGD.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0045724; P:positive regulation of cilium assembly; ISO:RGD.
DR   GO; GO:0007288; P:sperm axoneme assembly; ISO:RGD.
DR   GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR   InterPro; IPR026504; MNS1.
DR   InterPro; IPR043597; TPH_dom.
DR   PANTHER; PTHR19265; PTHR19265; 1.
DR   Pfam; PF13868; TPH; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Cilium; Coiled coil; Cytoplasm; Cytoskeleton; Flagellum;
KW   Meiosis; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..498
FT                   /note="Meiosis-specific nuclear structural protein 1"
FT                   /id="PRO_0000298924"
FT   COILED          29..253
FT                   /evidence="ECO:0000255"
FT   COILED          287..360
FT                   /evidence="ECO:0000255"
FT   COILED          390..437
FT                   /evidence="ECO:0000255"
FT   MOD_RES         188
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q61884"
SQ   SEQUENCE   498 AA;  61240 MW;  5E6611EF664B51B1 CRC64;
     MANKKRAMSF SEKHQQLVDE NFRKSLHVQV LNKLERQAKN QVVQNENDER VERQRFLRVL
     QNEQFELDME EAVQKAEENK RMRDRQLEQE ERLANELARL KHESLKDEKM RQQVRENSIE
     LRELEQKLKA AYMNKERAAQ IVEKDVIKYE QMKRDAEIER IMMEEHKRLL KEENVKQEKR
     DKERAQYYVD LEKQLEDQER RKQEAYEQLL KEKLMIDEIV RKIYEEDQLE RQQKLEKRNA
     IQKYIKEFQR AQDLWRQKKR EEMEEENRKI LEFAKIQEQR EGERMARVQE SEEKRVQRQN
     LLIQKLEETL RQRDDLERVR QELYLEEYAE FIKLKMKEEV EQRLRKQRDR KQDFKDQMAL
     REVLLQAAKE EEEAFKKAML AKFAEDDRIE LMNAQKQRMK QLEHKRAVEK LIEERRNQFL
     ADKQRELEEL QLQQRRQGCI NEIIEEERLR LLKEHASKLL GYLPKGVFKK EDDVDMLGEE
     FRKAYQKKSE VCEEKGSS