ID   CTSRD_BOVIN             Reviewed;         781 AA.
AC   E1B9E5;
DT   18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Cation channel sperm-associated auxiliary subunit delta {ECO:0000250|UniProtKB:Q86XM0};
DE            Short=CatSper-delta;
DE            Short=CatSperdelta;
DE   AltName: Full=Transmembrane protein 146;
DE   Flags: Precursor;
GN   Name=CATSPERD {ECO:0000250|UniProtKB:Q86XM0}; Synonyms=TMEM146;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hereford;
RX   PubMed=19393038; DOI=10.1186/gb-2009-10-4-r42;
RA   Zimin A.V., Delcher A.L., Florea L., Kelley D.R., Schatz M.C., Puiu D.,
RA   Hanrahan F., Pertea G., Van Tassell C.P., Sonstegard T.S., Marcais G.,
RA   Roberts M., Subramanian P., Yorke J.A., Salzberg S.L.;
RT   "A whole-genome assembly of the domestic cow, Bos taurus.";
RL   Genome Biol. 10:R42.01-R42.10(2009).
CC   -!- FUNCTION: Auxiliary component of the CatSper complex, a complex
CC       involved in sperm cell hyperactivation. Sperm cell hyperactivation is
CC       needed for sperm motility which is essential late in the preparation of
CC       sperm for fertilization. Required for CATSPER1 stability before
CC       intraflagellar transport and/or incorporation of the CatSper complex
CC       channel into the flagellar membrane. {ECO:0000250|UniProtKB:E9Q9F6}.
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, TMEM249, TMEM262 and EFCAB9 (By similarity).
CC       HSPA1 may be an additional auxiliary complex member (By similarity).
CC       The core complex members CATSPER1, CATSPER2, CATSPER3 and CATSPER4 form
CC       a heterotetrameric channel. The auxiliary CATSPERB, CATSPERG, CATSPERD
CC       and CATSPERE subunits form a pavilion-like structure over the pore
CC       which stabilizes the complex through interactions with CATSPER4,
CC       CATSPER3, CATSPER1 and CATSPER2 respectively. TMEM262/CATSPERH
CC       interacts with CATSPERB, further stabilizing the complex.
CC       C2CD6/CATSPERT interacts at least with CATSPERD and is required for
CC       targeting the CatSper complex in the flagellar membrane (By
CC       similarity). {ECO:0000250|UniProtKB:E9Q9F6,
CC       ECO:0000250|UniProtKB:Q91ZR5}.
CC   -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC       {ECO:0000250|UniProtKB:E9Q9F6}; Single-pass type I membrane protein
CC       {ECO:0000255}. Note=Specifically located in the principal piece of
CC       sperm tail. {ECO:0000250|UniProtKB:E9Q9F6}.
CC   -!- SIMILARITY: Belongs to the CATSPERD family. {ECO:0000305}.
CC   -!- CAUTION: In mouse, Slco6c1 is an additional auxiliary subunit of the
CC       CatSper complex. It is unclear if the related SLCO6A1 protein performs
CC       the same role in non-rodent species. {ECO:0000305}.
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DR   EMBL; DAAA02019576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; E1B9E5; -.
DR   SMR; E1B9E5; -.
DR   STRING; 9913.ENSBTAP00000002352; -.
DR   PaxDb; E1B9E5; -.
DR   PRIDE; E1B9E5; -.
DR   eggNOG; ENOG502QSPE; Eukaryota.
DR   HOGENOM; CLU_019182_0_0_1; -.
DR   InParanoid; E1B9E5; -.
DR   OrthoDB; 213907at2759; -.
DR   TreeFam; TF337973; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
DR   GO; GO:0097228; C:sperm principal piece; ISS:UniProtKB.
DR   GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR   GO; GO:0048240; P:sperm capacitation; ISS:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR   InterPro; IPR028751; CATSPERD/E.
DR   PANTHER; PTHR33722; PTHR33722; 1.
DR   Pfam; PF15020; CATSPERD; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell projection; Cilium; Developmental protein;
KW   Differentiation; Disulfide bond; Flagellum; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Spermatogenesis; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..781
FT                   /note="Cation channel sperm-associated auxiliary subunit
FT                   delta"
FT                   /id="PRO_0000416883"
FT   TOPO_DOM        21..725
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   TRANSMEM        726..749
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   TOPO_DOM        750..781
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   CARBOHYD        231
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        473
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        539
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        631
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        24..370
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        60..146
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        145..153
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        388..497
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        511..705
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        526..573
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT   DISULFID        625..655
FT                   /evidence="ECO:0000250|UniProtKB:E9Q9F6"
SQ   SEQUENCE   781 AA;  88415 MW;  86EE60D57BA21B9C CRC64;
     MLVLMLVVAT TFRLCPLVKA RPLCRIRTLR TGKVFPVEEK IQGDRLYFSS GKTHLIKHPC
     KKNLALYLGR QIFLTKDTFE SSLIPFSIPT SMQVGTPEVT SAHFAGSVLL LVVNQKVYVY
     DYEANFWTAS TGIQHPVSHV SGDNCCYSGN SFCMDISNSV FAYLRGDQVS QANIYFSNSR
     GYRFQKYTQE RRAELVGTFG GIFSFHSLSQ VGLLLVDEQM AMFSYSDHPL NRSFGLPFDY
     DRALDILIAP GQKGILIFWS EKNLLVSRNS GQLVESVQVR EGQRILYNSI VKANVTIHSV
     AANENELAVL TEENNLYYGS LGIQSSSLIK FADQNIWSQE AVLMFTDVGM LEILTPLRDV
     LFPAFDFQKC RLNIQALLMD PQLQAGVCKV ELLQGEFENK MYTIDMNSQL ELTALMIPRP
     GMLPVPLVSV SNPHSLGLQA VICEDGYTYD GNTKHRLNIS LKQQHHWGRA DPNFTSSIKR
     PTISTITLDI ANKEISCVDL KPLTALISVG CDLEKKIVIQ NELSACYHGV LDPVALQDNY
     SYIIEREAYD PNFQGQQAKK DLEVHYPYEK LGCPLLAYYD IPWKPVVELW REGKFQEVVE
     AEYVLLEMNG LFTYTYSLTA STAGCSAQPQ NWTTITKMAG DTAPFSWDRE NYISCHDPNY
     HEPLRWPDVP YQILGGQTEN KVVFDQRNGI YIFFISIVDP SYSYCRLETT FSVYVYGAFP
     LSIFPPEITI VLLTAATLLS IWLAYMIPQL LHTEQGLEGN GFWVRLYQRC RKSCACLWGR
     C