TM249_MOUSE
ID TM249_MOUSE Reviewed; 171 AA.
AC A0A2R8VHF7;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2018, sequence version 1.
DT 03-AUG-2022, entry version 12.
DE RecName: Full=Cation channel sperm-associated auxiliary subunit TMEM249 {ECO:0000305};
DE AltName: Full=Transmembrane protein 249 {ECO:0000312|MGI:MGI:3647471};
GN Name=Tmem249 {ECO:0000312|MGI:MGI:3647471};
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, SUBCELLULAR LOCATION,
RP TRANSMEMBRANE DOMAINS, AND 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, CATSPERG2, 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:0000269|PubMed:34225353}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:34225353}. Note=Predominantly located in the
CC principal piece of the sperm tail. {ECO:0000269|PubMed:34225353}.
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DR PDB; 7EEB; EM; 2.90 A; J=1-171.
DR PDBsum; 7EEB; -.
DR AlphaFoldDB; A0A2R8VHF7; -.
DR SMR; A0A2R8VHF7; -.
DR Antibodypedia; 72998; 7 antibodies from 3 providers.
DR Ensembl; ENSMUST00000230604; ENSMUSP00000155040; ENSMUSG00000116376.
DR MGI; MGI:3647471; Tmem249.
DR VEuPathDB; HostDB:ENSMUSG00000116376; -.
DR GeneTree; ENSGT00510000050177; -.
DR OMA; MDYGENT; -.
DR Proteomes; UP000000589; Chromosome 15.
DR Bgee; ENSMUSG00000116376; Expressed in spermatid and 19 other tissues.
DR GO; GO:0036128; C:CatSper complex; IDA:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; IDA:UniProtKB.
DR InterPro; IPR027861; TMEM249.
DR PANTHER; PTHR35442; PTHR35442; 1.
DR Pfam; PF15158; DUF4579; 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..171
FT /note="Cation channel sperm-associated auxiliary subunit
FT TMEM249"
FT /evidence="ECO:0000255"
FT /id="PRO_5015341210"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 3..17
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 18..28
FT /note="Extracellular"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TRANSMEM 29..40
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:34225353"
FT TOPO_DOM 41..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:34225353"
FT HELIX 2..16
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:7EEB"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:7EEB"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:7EEB"
SQ SEQUENCE 171 AA; 19893 MW; 2BDA38251A8D86FC CRC64;
MLFIICLVFI SCNVLREVKY QETWCFPAYG MVIGLWLMLS SIPQRRLVLN HTRGMYHFSI
QGRTVCQGPM HLVYVRLALS SDAYGGRFFQ LVLCGHKLEP LVLVQLSERY EQMEFLGRHL
ARKLNINYFD YLASSYRHVV RHWPLGASFS PGIVQRKTQV YTKSSVNDLD V
