CTSRZ_MOUSE
ID CTSRZ_MOUSE Reviewed; 194 AA.
AC Q9CQP8; Q9DAA2; Q9DAP8;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Cation channel sperm-associated auxiliary subunit zeta {ECO:0000312|MGI:MGI:1914327};
DE Short=CatSper-zeta {ECO:0000303|PubMed:28226241};
DE Short=CatSperzeta {ECO:0000303|PubMed:28226241};
DE AltName: Full=Protein expressed in male leptotene and zygotene spermatocytes 622 {ECO:0000303|PubMed:20339383};
DE Short=MLZ-622 {ECO:0000303|PubMed:20339383};
DE AltName: Full=Testis-expressed protein 40;
GN Name=Catsperz {ECO:0000303|PubMed:28226241, ECO:0000312|MGI:MGI:1914327};
GN Synonyms=Tex40 {ECO:0000312|MGI:MGI:1914327};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP TISSUE SPECIFICITY.
RX PubMed=20339383; DOI=10.1038/jhg.2010.26;
RA Kogo H., Kowa-Sugiyama H., Yamada K., Bolor H., Tsutsumi M., Ohye T.,
RA Inagaki H., Taniguchi M., Toda T., Kurahashi H.;
RT "Screening of genes involved in chromosome segregation during meiosis I:
RT toward the identification of genes responsible for infertility in humans.";
RL J. Hum. Genet. 55:293-299(2010).
RN [4]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE
RP CATSPER COMPLEX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=28226241; DOI=10.7554/elife.23082;
RA Chung J.J., Miki K., Kim D., Shim S.H., Shi H.F., Hwang J.Y., Cai X.,
RA Iseri Y., Zhuang X., Clapham D.E.;
RT "CatSperzeta regulates the structural continuity of sperm Ca(2+) signaling
RT domains and is required for normal fertility.";
RL Elife 6:0-0(2017).
RN [5]
RP FUNCTION, AND INTERACTION WITH EFCAB9.
RX PubMed=31056283; DOI=10.1016/j.cell.2019.03.047;
RA Hwang J.Y., Mannowetz N., Zhang Y., Everley R.A., Gygi S.P., Bewersdorf J.,
RA Lishko P.V., Chung J.J.;
RT "Dual sensing of physiologic pH and calcium by EFCAB9 regulates sperm
RT motility.";
RL Cell 0:0-0(2019).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) OF THE CATSPER COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND FUNCTION.
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 (PubMed:28226241,
CC PubMed:31056283, PubMed:34225353). Sperm cell hyperactivation is needed
CC for sperm motility which is essential late in the preparation of sperm
CC for fertilization (PubMed:28226241, PubMed:31056283). Required for a
CC distribution of the CatSper complex in linear quadrilateral nanodomains
CC along the flagellum, maximizing fertilization inside the mammalian
CC female reproductive tract (PubMed:28226241). Together with EFCAB9,
CC associates with the CatSper channel pore and is required for the two-
CC row structure of each single CatSper channel (PubMed:31056283).
CC {ECO:0000269|PubMed:28226241, ECO:0000269|PubMed:31056283,
CC 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, PubMed:28226241). HSPA1 may be an additional
CC auxiliary complex member (By similarity). The core complex members
CC CATSPER1, CATSPER2, CATSPER3 and CATSPER4 form a heterotetrameric
CC channel (PubMed:34225353). The auxiliary CATSPERB, CATSPERG2, 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 (PubMed:34225353). SLCO6C1
CC interacts with CATSPERE and TMEM262/CATSPERH interacts with CATSPERB,
CC further stabilizing the complex (PubMed:34225353). C2CD6/CATSPERT
CC interacts at least with CATSPERD and is required for targeting the
CC CatSper complex in the flagellar membrane (Probable). Interacts with
CC EFCAB9; the interaction is direct, Ca(2+)-dependent and connects EFCAB9
CC with the CatSper complex (PubMed:31056283). Dissociates from EFCAB9 at
CC elevated pH (PubMed:31056283). {ECO:0000250|UniProtKB:Q91ZR5,
CC ECO:0000269|PubMed:28226241, ECO:0000269|PubMed:31056283,
CC ECO:0000269|PubMed:34225353, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane
CC {ECO:0000269|PubMed:28226241}; Peripheral membrane protein
CC {ECO:0000305}. Note=Specifically located in the principal piece of
CC sperm tail (PubMed:28226241). Although it does not contain a
CC transmembrane domain, localizes with the CatSper complex at the
CC flagellum membrane (PubMed:28226241). {ECO:0000269|PubMed:28226241}.
CC -!- TISSUE SPECIFICITY: Testis-specific (PubMed:20339383, PubMed:28226241).
CC Expressed in adult but not in fetal testis (PubMed:20339383). Not
CC expressed in ovary. Within testis, expression is restricted to
CC spermatids (PubMed:20339383). {ECO:0000269|PubMed:20339383,
CC ECO:0000269|PubMed:28226241}.
CC -!- DISRUPTION PHENOTYPE: Mice are normal but males show severe male
CC subfertility. Mutant males display fragmented patterns of CatSper
CC complex stripes in the tails of their sperm, leading to a reduction of
CC calcium ions that pass through the channels to enter the cell. As
CC consequence, the sperm tail is more rigid, preventing it from moving
CC efficiently within the female. Mutant sperm are less able to penetrate
CC the egg than normal sperm. {ECO:0000269|PubMed:28226241}.
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DR EMBL; AK005644; BAB24164.1; -; mRNA.
DR EMBL; AK006034; BAB24375.1; -; mRNA.
DR EMBL; AK006134; BAB24425.1; -; mRNA.
DR EMBL; AK007089; BAB24857.1; -; mRNA.
DR EMBL; BC048452; AAH48452.1; -; mRNA.
DR EMBL; BC061075; AAH61075.1; -; mRNA.
DR CCDS; CCDS29510.1; -.
DR RefSeq; NP_001034583.1; NM_001039494.2.
DR PDB; 7EEB; EM; 2.90 A; K=1-194.
DR PDBsum; 7EEB; -.
DR AlphaFoldDB; Q9CQP8; -.
DR SMR; Q9CQP8; -.
DR CORUM; Q9CQP8; -.
DR STRING; 10090.ENSMUSP00000056681; -.
DR iPTMnet; Q9CQP8; -.
DR PhosphoSitePlus; Q9CQP8; -.
DR jPOST; Q9CQP8; -.
DR PaxDb; Q9CQP8; -.
DR PeptideAtlas; Q9CQP8; -.
DR PRIDE; Q9CQP8; -.
DR ProteomicsDB; 285229; -.
DR Antibodypedia; 66419; 35 antibodies from 12 providers.
DR DNASU; 67077; -.
DR Ensembl; ENSMUST00000057716; ENSMUSP00000056681; ENSMUSG00000050623.
DR GeneID; 67077; -.
DR KEGG; mmu:67077; -.
DR UCSC; uc008gji.1; mouse.
DR CTD; 25858; -.
DR MGI; MGI:1914327; Catsperz.
DR VEuPathDB; HostDB:ENSMUSG00000050623; -.
DR eggNOG; ENOG502RU31; Eukaryota.
DR GeneTree; ENSGT00400000022853; -.
DR HOGENOM; CLU_123654_0_0_1; -.
DR InParanoid; Q9CQP8; -.
DR OMA; EMDEHAL; -.
DR OrthoDB; 1360720at2759; -.
DR PhylomeDB; Q9CQP8; -.
DR BioGRID-ORCS; 67077; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Kcnk4; mouse.
DR PRO; PR:Q9CQP8; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9CQP8; protein.
DR Bgee; ENSMUSG00000050623; Expressed in spermatocyte and 56 other tissues.
DR ExpressionAtlas; Q9CQP8; baseline and differential.
DR Genevisible; Q9CQP8; MM.
DR GO; GO:0036128; C:CatSper complex; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0097228; C:sperm principal piece; IDA:UniProtKB.
DR GO; GO:0030317; P:flagellated sperm motility; IMP:UniProtKB.
DR GO; GO:0007140; P:male meiotic nuclear division; IEP:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; IDA:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; IMP:UniProtKB.
DR InterPro; IPR039019; CATSPERZ.
DR PANTHER; PTHR42155; PTHR42155; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Cilium; Differentiation;
KW Flagellum; Membrane; Reference proteome; Spermatogenesis.
FT CHAIN 1..194
FT /note="Cation channel sperm-associated auxiliary subunit
FT zeta"
FT /id="PRO_0000349323"
FT CONFLICT 10
FT /note="K -> Q (in Ref. 1; BAB24164)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="R -> G (in Ref. 1; BAB24375)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="S -> W (in Ref. 1; BAB24375)"
FT /evidence="ECO:0000305"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 57..74
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 113..134
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 140..161
FT /evidence="ECO:0007829|PDB:7EEB"
FT HELIX 169..185
FT /evidence="ECO:0007829|PDB:7EEB"
SQ SEQUENCE 194 AA; 22741 MW; 6D9E823A7264A89E CRC64;
MEESVKPVPK HANHRRSSVR SSLYGDVRDL WSTATMSTAN VSVSDVCEDF DEEGKSVRNR
IRKYSQTISI RDSLNLEPEE IQQQARRELE LCHGRSLEHG EDHEESETSL ASSTSESLIF
SLWKPHRTYW TEQQNRLPLP LMELMETEVL DILKKALITY RSTIGRNHFM TKELQGYIEG
IRKRRNKRLY FLDQ
