TM262_MOUSE
ID TM262_MOUSE Reviewed; 116 AA.
AC D3Z338;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Cation channel sperm-associated auxiliary subunit TMEM262 {ECO:0000305};
DE AltName: Full=Cation channel sperm-associated auxiliary subunit eta {ECO:0000303|PubMed:34225353};
DE AltName: Full=Transmembrane protein 262 {ECO:0000312|MGI:MGI:3690536};
GN Name=Tmem262 {ECO:0000312|MGI:MGI:3690536};
GN Synonyms=Catsperh {ECO:0000303|PubMed:34225353};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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 [2] {ECO:0000305}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF THE CATSPER COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, TRANSMEMBRANE DOMAINS, AND
RP TOPOLOGY.
RX PubMed=34225353; DOI=10.1038/s41586-021-03742-6;
RA Lin S., Ke M., Zhang Y., Yan Z., Wu J.;
RT "Structure of a mammalian sperm cation channel complex.";
RL Nature 595:746-750(2021).
CC -!- FUNCTION: Auxiliary component of the CatSper complex, a complex
CC involved in sperm cell hyperactivation. {ECO:0000269|PubMed:34225353}.
CC -!- SUBUNIT: Component of the CatSper complex or CatSpermasome composed of
CC the core pore-forming members CATSPER1, CATSPER2, CATSPER3 and CATSPER4
CC as well as auxiliary members CATSPERB, CATSPERG, CATSPERD, CATSPERE,
CC CATSPERZ, C2CD6/CATSPERT, SLCO6C1, TMEM249, TMEM262 and EFCAB9
CC (PubMed:34225353). HSPA1 may be an additional auxiliary complex member
CC (By similarity). The core complex members CATSPER1, CATSPER2, CATSPER3
CC and CATSPER4 form a heterotetrameric channel (PubMed:34225353). The
CC auxiliary CATSPERB, CATSPERG2, CATSPERD and CATSPERE subunits form a
CC pavilion-like structure over the pore which stabilizes the complex
CC through interactions with CATSPER4, CATSPER3, CATSPER1 and CATSPER2
CC respectively (PubMed:34225353). SLCO6C1 interacts with CATSPERE and
CC TMEM262/CATSPERH interacts with CATSPERB, further stabilizing the
CC complex (PubMed:34225353). C2CD6/CATSPERT interacts at least with
CC CATSPERD and is required for targeting the CatSper complex in the
CC flagellar membrane (Probable). {ECO:0000250|UniProtKB:Q91ZR5,
CC ECO:0000269|PubMed:34225353, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:34225353}.
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DR CCDS; CCDS50363.1; -.
DR RefSeq; NP_001104787.1; NM_001111317.1.
DR PDB; 7EEB; EM; 2.90 A; M=1-116.
DR PDBsum; 7EEB; -.
DR AlphaFoldDB; D3Z338; -.
DR SMR; D3Z338; -.
DR STRING; 10090.ENSMUSP00000121339; -.
DR PaxDb; D3Z338; -.
DR PRIDE; D3Z338; -.
DR ProteomicsDB; 335333; -.
DR Ensembl; ENSMUST00000143303; ENSMUSP00000121339; ENSMUSG00000047733.
DR GeneID; 433215; -.
DR KEGG; mmu:433215; -.
DR UCSC; uc008ghe.2; mouse.
DR CTD; 100130348; -.
DR MGI; MGI:3690536; Tmem262.
DR VEuPathDB; HostDB:ENSMUSG00000047733; -.
DR eggNOG; ENOG502S7IB; Eukaryota.
DR GeneTree; ENSGT00530000064783; -.
DR HOGENOM; CLU_160801_0_0_1; -.
DR InParanoid; D3Z338; -.
DR OMA; DKFLRCF; -.
DR OrthoDB; 1596404at2759; -.
DR BioGRID-ORCS; 433215; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Tmem262; mouse.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; D3Z338; protein.
DR Bgee; ENSMUSG00000047733; Expressed in testis and 42 other tissues.
DR ExpressionAtlas; D3Z338; baseline and differential.
DR GO; GO:0036128; C:CatSper complex; IDA:UniProtKB.
DR GO; GO:0031514; C:motile cilium; IEA:UniProtKB-KW.
DR InterPro; IPR040431; TM262.
DR PANTHER; PTHR37998; PTHR37998; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cilium; Flagellum; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..116
FT /note="Cation channel sperm-associated auxiliary subunit
FT TMEM262"
FT /id="PRO_0000454936"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 17..38
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 39..51
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 73..84
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 85..107
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 108..116
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 14..41
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 54..78
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 81..101
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:7EEB"
SQ SEQUENCE 116 AA; 13475 MW; 8C6497D4F2D33619 CRC64;
MRWRDRIAVL CFPPGLMLTV AALILFFIHM GVFASDVHNF CVIHNYDHMS FRYTVVLIFS
QVISIGWAAM GSLYAEMTGD KFLRCFALTI LILNGAMFFN RLCLEFLAIN YREERH
