CTSRD_MACFA
ID CTSRD_MACFA Reviewed; 793 AA.
AC Q95JI2; Q95JI4; Q95LM7;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 54.
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;
GN ORFNames=QtsA-17095, QtsA-17108, QtsA-19758;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Testis;
RX PubMed=12498619; DOI=10.1186/1471-2164-3-36;
RA Osada N., Hida M., Kusuda J., Tanuma R., Hirata M., Suto Y., Hirai M.,
RA Terao K., Sugano S., Hashimoto K.;
RT "Cynomolgus monkey testicular cDNAs for discovery of novel human genes in
RT the human genome sequence.";
RL BMC Genomics 3:36-36(2002).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q95JI2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q95JI2-2; Sequence=VSP_025347;
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB63142.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB070197; BAB63142.1; ALT_INIT; mRNA.
DR EMBL; AB070199; BAB63144.1; -; mRNA.
DR EMBL; AB072761; BAB69730.1; -; mRNA.
DR AlphaFoldDB; Q95JI2; -.
DR SMR; Q95JI2; -.
DR STRING; 9541.XP_005587708.1; -.
DR eggNOG; ENOG502QSPE; Eukaryota.
DR Proteomes; UP000233100; 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 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Cell projection; Cilium;
KW Developmental protein; Differentiation; Disulfide bond; Flagellum;
KW Glycoprotein; Membrane; Reference proteome; Signal; Spermatogenesis;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..793
FT /note="Cation channel sperm-associated auxiliary subunit
FT delta"
FT /id="PRO_0000287151"
FT TOPO_DOM 21..725
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT TRANSMEM 726..747
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT TOPO_DOM 748..793
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 231
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
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..703
FT /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT DISULFID 526..573
FT /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT DISULFID 625..653
FT /evidence="ECO:0000250|UniProtKB:E9Q9F6"
FT VAR_SEQ 249..439
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12498619"
FT /id="VSP_025347"
FT CONFLICT 83
FT /note="L -> P (in Ref. 1; BAB63142)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="T -> S (in Ref. 1; BAB63144/BAB69730)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="D -> N (in Ref. 1; BAB63142)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="Q -> E (in Ref. 1; BAB69730)"
FT /evidence="ECO:0000305"
FT CONFLICT 546
FT /note="K -> E (in Ref. 1; BAB63144)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="P -> S (in Ref. 1; BAB63144)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 793 AA; 89771 MW; 1B00B908AA96847F CRC64;
MLMLMLVAAV TMWLRPLVTA QPLCRARTVR TGKVFNVIQD VQGDRLYFRS TTTRLIKHPC
KKNIALYLGK QVFFTTDNFE TSLLPFTIPT SMQVGVPEVT SAHFTGSLLL LVVNHKVYTY
DYESNSWNLS LGIKHPVTHV SGDNCCYTGS LFCVDVSNLV FAYFRGDQIS QTYIYYSNTG
GFSFWKYHYD RQAEIVGSLG GIFHLFSLSQ VGMLVVDQGK GMFKYSDHPL NRSLGLSFDY
NGTLDIVIAP GQKGILLLWF EKSLLFSRNA GQLVDTVRVK KGEQTLFTSI FEAQITIHNI
AVNENELAVI TREDNLYYGN LGIVPSSIIK FAHQHIWSED AALMFRSSGI LEILTPVRDT
AFAAFDFQKC LLNIQAILMD PDLHVGRCNI EFLKGEFTYR MYTIDMHSQL ELTALLIPQP
GTSLIPLVMV SNPHSLGFQA TFYESGYTSD GNTKYKLDIY LKQQQHWGRT DFNFTSSLKR
ATMSTLTVDI ANKEISCVDI KPLSTLISVG CDLDKKIVIQ NTVSACSKGV LDALALQDNY
SFIIEKEFYD PGFQGRQSSK DLHVFYSYQQ LGCPLLVYYD TPWKPVVELW KKDRFQEVVD
AEYVLLEVNG QFSYSYSLTA KSAMCTSQPQ NWTTMIKESG GPFFWNRENY VSCHDPNNDA
PLRWPDVQYQ ILGGRTANQI VFSHNNGFYV FYISIVDPYY SYCQLETVFS IYVYGAFPVQ
LVSAGVVMVL LISSILGSVW LAYMIPRLLR TARGRRMTSF VAQLYGRCKT VCQFRASATA
RTGSKPMGRH RSS
