CTSR1_HUMAN
ID CTSR1_HUMAN Reviewed; 780 AA.
AC Q8NEC5; Q96P76;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cation channel sperm-associated protein 1;
DE Short=CatSper1;
DE Short=hCatSper;
GN Name=CATSPER1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT ILE-652.
RX PubMed=11595941; DOI=10.1038/35098027;
RA Ren D., Navarro B., Perez G., Jackson A.C., Hsu S., Shi Q., Tilly J.L.,
RA Clapham D.E.;
RT "A sperm ion channel required for sperm motility and male fertility.";
RL Nature 413:603-609(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-652.
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).
RN [4]
RP INDUCTION.
RX PubMed=14688170; DOI=10.1093/humrep/deh043;
RA Nikpoor P., Mowla S.J., Movahedin M., Ziaee S.A.-M., Tiraihi T.;
RT "CatSper gene expression in postnatal development of mouse testis and in
RT subfertile men with deficient sperm motility.";
RL Hum. Reprod. 19:124-128(2004).
RN [5]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=16625279; DOI=10.1111/j.1745-7262.2006.00132.x;
RA Li H.-G., Liao A.-H., Ding X.-F., Zhou H., Xiong C.-L.;
RT "The expression and significance of CATSPER1 in human testis and ejaculated
RT spermatozoa.";
RL Asian J. Androl. 8:301-306(2006).
RN [6]
RP INTERACTION WITH CACNA1I.
RX PubMed=16740636; DOI=10.1074/jbc.m511288200;
RA Zhang D., Chen J., Saraf A., Cassar S., Han P., Rogers J.C., Brioni J.D.,
RA Sullivan J.P., Gopalakrishnan M.;
RT "Association of Catsper1 or -2 with Ca(v)3.3 leads to suppression of T-type
RT calcium channel activity.";
RL J. Biol. Chem. 281:22332-22341(2006).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=17347248; DOI=10.1093/molehr/gam009;
RA Li H.-G., Ding X.-F., Liao A.-H., Kong X.-B., Xiong C.-L.;
RT "Expression of CatSper family transcripts in the mouse testis during post-
RT natal development and human ejaculated spermatozoa: relationship to sperm
RT motility.";
RL Mol. Hum. Reprod. 13:299-306(2007).
RN [8]
RP INVOLVEMENT IN SPGF7.
RX PubMed=19344877; DOI=10.1016/j.ajhg.2009.03.004;
RA Avenarius M.R., Hildebrand M.S., Zhang Y., Meyer N.C., Smith L.L.H.,
RA Kahrizi K., Najmabadi H., Smith R.J.H.;
RT "Human male infertility caused by mutations in the CATSPER1 channel
RT protein.";
RL Am. J. Hum. Genet. 84:505-510(2009).
RN [9]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=21412338; DOI=10.1038/nature09769;
RA Strunker T., Goodwin N., Brenker C., Kashikar N.D., Weyand I., Seifert R.,
RA Kaupp U.B.;
RT "The CatSper channel mediates progesterone-induced Ca2+ influx in human
RT sperm.";
RL Nature 471:382-386(2011).
RN [10]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=21412339; DOI=10.1038/nature09767;
RA Lishko P.V., Botchkina I.L., Kirichok Y.;
RT "Progesterone activates the principal Ca2+ channel of human sperm.";
RL Nature 471:387-391(2011).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=26989199; DOI=10.1126/science.aad6887;
RA Miller M.R., Mannowetz N., Iavarone A.T., Safavi R., Gracheva E.O.,
RA Smith J.F., Hill R.Z., Bautista D.M., Kirichok Y., Lishko P.V.;
RT "Unconventional endocannabinoid signaling governs sperm activation via sex
RT hormone progesterone.";
RL Science 352:555-559(2016).
CC -!- FUNCTION: Voltage-gated calcium channel that plays a central role in
CC calcium-dependent physiological responses essential for successful
CC fertilization, such as sperm hyperactivation, acrosome reaction and
CC chemotaxis towards the oocyte. {ECO:0000269|PubMed:21412338,
CC ECO:0000269|PubMed:21412339}.
CC -!- ACTIVITY REGULATION: The CatSper calcium channel is indirectly
CC activated by extracellular progesterone and prostaglandins following
CC the sequence: progesterone > PGF1-alpha = PGE1 > PGA1 > PGE2 >> PGD2
CC (PubMed:21412338, PubMed:21412339, PubMed:26989199). The CatSper
CC calcium channel is directly inhibited by endocannabinoid 2-
CC arachidonoylglycerol (2AG) (PubMed:26989199). Indirect activation by
CC progesterone takes place via the following mechanism: progesterone
CC binds and activates the acylglycerol lipase ABHD2, which in turn
CC mediates hydrolysis of 2AG inhibitor, relieving inhibition of the
CC CatSper channel (PubMed:26989199). The primary effect of progesterone
CC activation is to shift voltage dependence towards more physiological,
CC negative membrane potentials; it is not mediated by metabotropic
CC receptors and second messengers (PubMed:21412338, PubMed:21412339).
CC Sperm capacitation enhances the effect of progesterone by providing
CC additional negative shift. Also activated by the elevation of
CC intracellular pH (PubMed:21412338, PubMed:21412339).
CC {ECO:0000269|PubMed:21412338, ECO:0000269|PubMed:21412339,
CC ECO:0000269|PubMed:26989199}.
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 (By similarity). The auxiliary CATSPERB,
CC CATSPERG, CATSPERD and CATSPERE subunits form a pavilion-like structure
CC over the pore which stabilizes the complex through interactions with
CC CATSPER4, CATSPER3, CATSPER1 and CATSPER2 respectively (By similarity).
CC TMEM262/CATSPERH interacts with CATSPERB, further stabilizing the
CC complex. C2CD6/CATSPERT interacts at least with CATSPERD and is
CC required for targeting the CatSper complex in the flagellar membrane
CC (By similarity). Interacts with Ca(v)3.3/CACNA1I, leading to
CC suppression of T-type calcium channel activity (PubMed:16740636).
CC {ECO:0000250|UniProtKB:Q91ZR5, ECO:0000269|PubMed:16740636}.
CC -!- INTERACTION:
CC Q8NEC5; O94929-2: ABLIM3; NbExp=3; IntAct=EBI-744545, EBI-11961672;
CC Q8NEC5; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-744545, EBI-10173507;
CC Q8NEC5; O95994: AGR2; NbExp=6; IntAct=EBI-744545, EBI-712648;
CC Q8NEC5; Q8TD06: AGR3; NbExp=3; IntAct=EBI-744545, EBI-3925742;
CC Q8NEC5; Q96IF1: AJUBA; NbExp=3; IntAct=EBI-744545, EBI-949782;
CC Q8NEC5; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-744545, EBI-357530;
CC Q8NEC5; P02652: APOA2; NbExp=7; IntAct=EBI-744545, EBI-1171525;
CC Q8NEC5; Q03989: ARID5A; NbExp=3; IntAct=EBI-744545, EBI-948603;
CC Q8NEC5; Q9H5F2: C11orf1; NbExp=5; IntAct=EBI-744545, EBI-718615;
CC Q8NEC5; Q9P0X4: CACNA1I; NbExp=5; IntAct=EBI-744545, EBI-1220829;
CC Q8NEC5; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-744545, EBI-3866279;
CC Q8NEC5; Q6NVV7: CDPF1; NbExp=3; IntAct=EBI-744545, EBI-2802782;
CC Q8NEC5; Q9UKJ5: CHIC2; NbExp=4; IntAct=EBI-744545, EBI-741528;
CC Q8NEC5; Q9H2X0: CHRD; NbExp=3; IntAct=EBI-744545, EBI-947551;
CC Q8NEC5; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-744545, EBI-11523759;
CC Q8NEC5; P56545-3: CTBP2; NbExp=3; IntAct=EBI-744545, EBI-10171902;
CC Q8NEC5; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-744545, EBI-3867333;
CC Q8NEC5; P50402: EMD; NbExp=9; IntAct=EBI-744545, EBI-489887;
CC Q8NEC5; O00167-2: EYA2; NbExp=3; IntAct=EBI-744545, EBI-12807776;
CC Q8NEC5; Q5TD97: FHL5; NbExp=3; IntAct=EBI-744545, EBI-750641;
CC Q8NEC5; O43559: FRS3; NbExp=3; IntAct=EBI-744545, EBI-725515;
CC Q8NEC5; P19883: FST; NbExp=3; IntAct=EBI-744545, EBI-1571188;
CC Q8NEC5; P08151: GLI1; NbExp=3; IntAct=EBI-744545, EBI-308084;
CC Q8NEC5; P31943: HNRNPH1; NbExp=3; IntAct=EBI-744545, EBI-351590;
CC Q8NEC5; P49639: HOXA1; NbExp=3; IntAct=EBI-744545, EBI-740785;
CC Q8NEC5; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-744545, EBI-747204;
CC Q8NEC5; Q5VWX1: KHDRBS2; NbExp=6; IntAct=EBI-744545, EBI-742808;
CC Q8NEC5; Q5T749: KPRP; NbExp=5; IntAct=EBI-744545, EBI-10981970;
CC Q8NEC5; Q15323: KRT31; NbExp=3; IntAct=EBI-744545, EBI-948001;
CC Q8NEC5; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-744545, EBI-11959885;
CC Q8NEC5; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-744545, EBI-11749135;
CC Q8NEC5; Q9BYS1: KRTAP1-5; NbExp=3; IntAct=EBI-744545, EBI-11741292;
CC Q8NEC5; P60014: KRTAP10-10; NbExp=3; IntAct=EBI-744545, EBI-11955579;
CC Q8NEC5; P60412: KRTAP10-11; NbExp=6; IntAct=EBI-744545, EBI-10217483;
CC Q8NEC5; P60372: KRTAP10-4; NbExp=3; IntAct=EBI-744545, EBI-10178153;
CC Q8NEC5; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-744545, EBI-10172150;
CC Q8NEC5; P60410: KRTAP10-8; NbExp=8; IntAct=EBI-744545, EBI-10171774;
CC Q8NEC5; P60411: KRTAP10-9; NbExp=11; IntAct=EBI-744545, EBI-10172052;
CC Q8NEC5; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-744545, EBI-10210845;
CC Q8NEC5; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-744545, EBI-10176379;
CC Q8NEC5; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-744545, EBI-11953334;
CC Q8NEC5; Q9BYP8: KRTAP17-1; NbExp=3; IntAct=EBI-744545, EBI-11988175;
CC Q8NEC5; Q3LI72: KRTAP19-5; NbExp=3; IntAct=EBI-744545, EBI-1048945;
CC Q8NEC5; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-744545, EBI-12805508;
CC Q8NEC5; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-744545, EBI-10241353;
CC Q8NEC5; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-744545, EBI-14065470;
CC Q8NEC5; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-744545, EBI-751260;
CC Q8NEC5; A0A087WY89: KRTAP4-1; NbExp=3; IntAct=EBI-744545, EBI-11957260;
CC Q8NEC5; Q9BYQ6: KRTAP4-11; NbExp=6; IntAct=EBI-744545, EBI-10302392;
CC Q8NEC5; Q9BQ66: KRTAP4-12; NbExp=9; IntAct=EBI-744545, EBI-739863;
CC Q8NEC5; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-744545, EBI-10172511;
CC Q8NEC5; Q9BYR3: KRTAP4-4; NbExp=3; IntAct=EBI-744545, EBI-11958132;
CC Q8NEC5; Q9BYR0: KRTAP4-7; NbExp=3; IntAct=EBI-744545, EBI-10302547;
CC Q8NEC5; Q6L8G4: KRTAP5-11; NbExp=3; IntAct=EBI-744545, EBI-11993296;
CC Q8NEC5; Q6L8H2: KRTAP5-3; NbExp=6; IntAct=EBI-744545, EBI-11974251;
CC Q8NEC5; Q6L8H1: KRTAP5-4; NbExp=3; IntAct=EBI-744545, EBI-11963072;
CC Q8NEC5; Q6L8G9: KRTAP5-6; NbExp=6; IntAct=EBI-744545, EBI-10250562;
CC Q8NEC5; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-744545, EBI-3958099;
CC Q8NEC5; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-744545, EBI-12111050;
CC Q8NEC5; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-744545, EBI-11962084;
CC Q8NEC5; Q9BYQ4: KRTAP9-2; NbExp=8; IntAct=EBI-744545, EBI-1044640;
CC Q8NEC5; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-744545, EBI-1043191;
CC Q8NEC5; Q9BYQ2: KRTAP9-4; NbExp=3; IntAct=EBI-744545, EBI-10185730;
CC Q8NEC5; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-744545, EBI-11958364;
CC Q8NEC5; Q14847-2: LASP1; NbExp=3; IntAct=EBI-744545, EBI-9088686;
CC Q8NEC5; Q5T752: LCE1D; NbExp=3; IntAct=EBI-744545, EBI-11741311;
CC Q8NEC5; Q5T753: LCE1E; NbExp=3; IntAct=EBI-744545, EBI-11955335;
CC Q8NEC5; Q5T754: LCE1F; NbExp=3; IntAct=EBI-744545, EBI-11958008;
CC Q8NEC5; Q5TA81: LCE2C; NbExp=3; IntAct=EBI-744545, EBI-11973993;
CC Q8NEC5; P48059-3: LIMS1; NbExp=3; IntAct=EBI-744545, EBI-12864460;
CC Q8NEC5; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-744545, EBI-741037;
CC Q8NEC5; Q99750: MDFI; NbExp=4; IntAct=EBI-744545, EBI-724076;
CC Q8NEC5; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-744545, EBI-742948;
CC Q8NEC5; P12524-2: MYCL; NbExp=3; IntAct=EBI-744545, EBI-18936665;
CC Q8NEC5; Q7Z3S9: NOTCH2NLA; NbExp=4; IntAct=EBI-744545, EBI-945833;
CC Q8NEC5; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-744545, EBI-22310682;
CC Q8NEC5; Q9P286: PAK5; NbExp=3; IntAct=EBI-744545, EBI-741896;
CC Q8NEC5; Q9NR12: PDLIM7; NbExp=5; IntAct=EBI-744545, EBI-350517;
CC Q8NEC5; O15496: PLA2G10; NbExp=3; IntAct=EBI-744545, EBI-726466;
CC Q8NEC5; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-744545, EBI-2876622;
CC Q8NEC5; O15162: PLSCR1; NbExp=3; IntAct=EBI-744545, EBI-740019;
CC Q8NEC5; Q9NRY6: PLSCR3; NbExp=8; IntAct=EBI-744545, EBI-750734;
CC Q8NEC5; Q6P1K2-3: PMF1; NbExp=3; IntAct=EBI-744545, EBI-12906008;
CC Q8NEC5; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-744545, EBI-12000762;
CC Q8NEC5; Q16825: PTPN21; NbExp=3; IntAct=EBI-744545, EBI-2860264;
CC Q8NEC5; Q8HWS3: RFX6; NbExp=6; IntAct=EBI-744545, EBI-746118;
CC Q8NEC5; P49795: RGS19; NbExp=3; IntAct=EBI-744545, EBI-874907;
CC Q8NEC5; O76081: RGS20; NbExp=4; IntAct=EBI-744545, EBI-1052678;
CC Q8NEC5; O76081-6: RGS20; NbExp=3; IntAct=EBI-744545, EBI-10178530;
CC Q8NEC5; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-744545, EBI-10182375;
CC Q8NEC5; Q6UXX9-2: RSPO2; NbExp=3; IntAct=EBI-744545, EBI-12009390;
CC Q8NEC5; O75711: SCRG1; NbExp=3; IntAct=EBI-744545, EBI-10189029;
CC Q8NEC5; O15304-2: SIVA1; NbExp=3; IntAct=EBI-744545, EBI-12372219;
CC Q8NEC5; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-744545, EBI-10269322;
CC Q8NEC5; O60504: SORBS3; NbExp=3; IntAct=EBI-744545, EBI-741237;
CC Q8NEC5; O43597: SPRY2; NbExp=3; IntAct=EBI-744545, EBI-742487;
CC Q8NEC5; O43610: SPRY3; NbExp=3; IntAct=EBI-744545, EBI-12290641;
CC Q8NEC5; P01137: TGFB1; NbExp=3; IntAct=EBI-744545, EBI-779636;
CC Q8NEC5; Q63HR2: TNS2; NbExp=3; IntAct=EBI-744545, EBI-949753;
CC Q8NEC5; Q12933: TRAF2; NbExp=3; IntAct=EBI-744545, EBI-355744;
CC Q8NEC5; P14373: TRIM27; NbExp=3; IntAct=EBI-744545, EBI-719493;
CC Q8NEC5; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-744545, EBI-5235829;
CC Q8NEC5; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-744545, EBI-2340370;
CC Q8NEC5; Q15654: TRIP6; NbExp=7; IntAct=EBI-744545, EBI-742327;
CC Q8NEC5; O14817: TSPAN4; NbExp=3; IntAct=EBI-744545, EBI-8652667;
CC Q8NEC5; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-744545, EBI-11957238;
CC Q8NEC5; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-744545, EBI-12287587;
CC Q8NEC5; Q9NZV7: ZIM2; NbExp=5; IntAct=EBI-744545, EBI-11962760;
CC Q8NEC5; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-744545, EBI-4395732;
CC Q8NEC5; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-744545, EBI-10251462;
CC Q8NEC5; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-744545, EBI-11962574;
CC Q8NEC5; Q7Z783; NbExp=3; IntAct=EBI-744545, EBI-9088990;
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000269|PubMed:16625279}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q91ZR5}. Note=Specifically located in the
CC principal piece of the sperm tail. {ECO:0000269|PubMed:16625279}.
CC -!- TISSUE SPECIFICITY: Testis-specific. {ECO:0000269|PubMed:11595941,
CC ECO:0000269|PubMed:16625279, ECO:0000269|PubMed:17347248}.
CC -!- DEVELOPMENTAL STAGE: Expressed meiotically and post-meiotically.
CC {ECO:0000269|PubMed:16625279}.
CC -!- INDUCTION: Down-regulated in patients lacking sperm motility.
CC {ECO:0000269|PubMed:14688170}.
CC -!- DISEASE: Spermatogenic failure 7 (SPGF7) [MIM:612997]: An infertility
CC disorder characterized by non-motile sperm or sperm motility below the
CC normal threshold, low sperm count, increased abnormally structured
CC spermatozoa, and reduced semen volume. {ECO:0000269|PubMed:19344877}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the cation channel sperm-associated (TC
CC 1.A.1.19) 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; AF407333; AAL14105.1; -; mRNA.
DR EMBL; AP006287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032950; AAH32950.1; -; mRNA.
DR EMBL; BC036522; AAH36522.1; -; mRNA.
DR CCDS; CCDS8127.1; -.
DR RefSeq; NP_444282.3; NM_053054.3.
DR AlphaFoldDB; Q8NEC5; -.
DR SMR; Q8NEC5; -.
DR BioGRID; 125556; 119.
DR IntAct; Q8NEC5; 117.
DR MINT; Q8NEC5; -.
DR STRING; 9606.ENSP00000309052; -.
DR ChEMBL; CHEMBL1628462; -.
DR DrugBank; DB11093; Calcium citrate.
DR DrugBank; DB11348; Calcium Phosphate.
DR DrugBank; DB14481; Calcium phosphate dihydrate.
DR DrugCentral; Q8NEC5; -.
DR GuidetoPHARMACOLOGY; 388; -.
DR TCDB; 1.A.1.19.1; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q8NEC5; -.
DR PhosphoSitePlus; Q8NEC5; -.
DR BioMuta; CATSPER1; -.
DR DMDM; 296439381; -.
DR MassIVE; Q8NEC5; -.
DR PaxDb; Q8NEC5; -.
DR PeptideAtlas; Q8NEC5; -.
DR PRIDE; Q8NEC5; -.
DR ProteomicsDB; 73148; -.
DR Antibodypedia; 58041; 128 antibodies from 24 providers.
DR DNASU; 117144; -.
DR Ensembl; ENST00000312106.6; ENSP00000309052.5; ENSG00000175294.6.
DR GeneID; 117144; -.
DR KEGG; hsa:117144; -.
DR MANE-Select; ENST00000312106.6; ENSP00000309052.5; NM_053054.4; NP_444282.3.
DR UCSC; uc001ogt.3; human.
DR CTD; 117144; -.
DR DisGeNET; 117144; -.
DR GeneCards; CATSPER1; -.
DR GeneReviews; CATSPER1; -.
DR HGNC; HGNC:17116; CATSPER1.
DR HPA; ENSG00000175294; Tissue enriched (testis).
DR MalaCards; CATSPER1; -.
DR MIM; 606389; gene.
DR MIM; 612997; phenotype.
DR neXtProt; NX_Q8NEC5; -.
DR OpenTargets; ENSG00000175294; -.
DR Orphanet; 276234; Non-syndromic male infertility due to sperm motility disorder.
DR PharmGKB; PA38438; -.
DR VEuPathDB; HostDB:ENSG00000175294; -.
DR eggNOG; KOG2302; Eukaryota.
DR GeneTree; ENSGT00940000162437; -.
DR HOGENOM; CLU_016037_0_0_1; -.
DR InParanoid; Q8NEC5; -.
DR OMA; EVRGEWY; -.
DR OrthoDB; 920162at2759; -.
DR PhylomeDB; Q8NEC5; -.
DR TreeFam; TF329330; -.
DR PathwayCommons; Q8NEC5; -.
DR Reactome; R-HSA-1300642; Sperm Motility And Taxes.
DR SignaLink; Q8NEC5; -.
DR BioGRID-ORCS; 117144; 19 hits in 1068 CRISPR screens.
DR GeneWiki; CatSper1; -.
DR GenomeRNAi; 117144; -.
DR Pharos; Q8NEC5; Tchem.
DR PRO; PR:Q8NEC5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NEC5; protein.
DR Bgee; ENSG00000175294; Expressed in monocyte and 98 other tissues.
DR Genevisible; Q8NEC5; HS.
DR GO; GO:0036128; C:CatSper complex; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0097228; C:sperm principal piece; ISS:UniProtKB.
DR GO; GO:0005227; F:calcium activated cation channel activity; IEA:InterPro.
DR GO; GO:0005245; F:voltage-gated calcium channel activity; IBA:GO_Central.
DR GO; GO:0006816; P:calcium ion transport; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030317; P:flagellated sperm motility; IBA:GO_Central.
DR GO; GO:0060296; P:regulation of cilium beat frequency involved in ciliary motility; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0007283; P:spermatogenesis; IBA:GO_Central.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR028746; CatSper1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR47193; PTHR47193; 1.
DR Pfam; PF00520; Ion_trans; 1.
PE 1: Evidence at protein level;
KW Calcium; Calcium channel; Calcium transport; Cell membrane;
KW Cell projection; Cilium; Developmental protein; Differentiation; Flagellum;
KW Ion channel; Ion transport; Membrane; Reference proteome; Spermatogenesis;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..780
FT /note="Cation channel sperm-associated protein 1"
FT /id="PRO_0000295674"
FT TOPO_DOM 1..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TRANSMEM 448..469
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TOPO_DOM 470..478
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TRANSMEM 479..500
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TOPO_DOM 501..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TRANSMEM 509..531
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TOPO_DOM 532..540
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TRANSMEM 541..563
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TOPO_DOM 564..581
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TRANSMEM 582..604
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TOPO_DOM 605..615
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT INTRAMEM 616..628
FT /note="Helical; Pore-forming"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TOPO_DOM 629..645
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TRANSMEM 646..671
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT TOPO_DOM 672..780
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91ZR5"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 71..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..237
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..301
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 383..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 133
FT /note="G -> S (in dbSNP:rs1203998)"
FT /id="VAR_033304"
FT VARIANT 652
FT /note="V -> I (in dbSNP:rs3814747)"
FT /evidence="ECO:0000269|PubMed:11595941,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_033305"
FT VARIANT 730
FT /note="T -> P (in dbSNP:rs34958219)"
FT /id="VAR_033306"
FT CONFLICT 88
FT /note="G -> V (in Ref. 2; AAH32950)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 780 AA; 90091 MW; E09C4339F8AF5044 CRC64;
MDQNSVPEKA QNEADTNNAD RFFRSHSSPP HHRPGHSRAL HHYELHHHGV PHQRGESHHP
PEFQDFHDQA LSSHVHQSHH HSEARNHGRA HGPTGFGLAP SQGAVPSHRS YGEDYHDELQ
RDGRRHHDGS QYGGFHQQSD SHYHRGSHHG RPQYLGENLS HYSSGVPHHG EASHHGGSYL
PHGPNPYSES FHHSEASHLS GLQHDESQHH QVPHRGWPHH HQVHHHGRSR HHEAHQHGKS
PHHGETISPH SSVGSYQRGI SDYHSEYHQG DHHPSEYHHG DHPHHTQHHY HQTHRHRDYH
QHQDHHGAYH SSYLHGDYVQ STSQLSIPHT SRSLIHDAPG PAASRTGVFP YHVAHPRGSA
HSMTRSSSTI RSRVTQMSKK VHTQDISTKH SEDWGKEEGQ FQKRKTGRLQ RTRKKGHSTN
LFQWLWEKLT FLIQGFREMI RNLTQSLAFE TFIFFVVCLN TVMLVAQTFA EVEIRGEWYF
MALDSIFFCI YVVEALLKII ALGLSYFFDF WNNLDFFIMA MAVLDFLLMQ THSFAIYHQS
LFRILKVFKS LRALRAIRVL RRLSFLTSVQ EVTGTLGQSL PSIAAILILM FTCLFLFSAV
LRALFRKSDP KRFQNIFTTI FTLFTLLTLD DWSLIYMDSR AQGAWYIIPI LVIYIIIQYF
IFLNLVITVL VDSFQTALFK GLEKAKQERA ARIQEKLLED SLTELRAAEP KEVASEGTML
KRLIEKKFGT MTEKQQELLF HYLQLVASVE QEQQKFRSQA AVIDEIVDTT FEAGEEDFRN
